| Year |
Citation |
Score |
| 2020 |
Klatt F, Leitner A, Kim IV, Ho-Xuan H, Schneider EV, Langhammer F, Weinmann R, Müller MR, Huber R, Meister G, Kuhn CD. A precisely positioned MED12 activation helix stimulates CDK8 kinase activity. Proceedings of the National Academy of Sciences of the United States of America. PMID 31988137 DOI: 10.1073/Pnas.1917635117 |
0.328 |
|
| 2020 |
Merdanovic M, Burston SG, Schmitz AL, Köcher S, Knapp S, Clausen T, Kaiser M, Huber R, Ehrmann M. Activation by substoichiometric inhibition. Proceedings of the National Academy of Sciences of the United States of America. PMID 31907318 DOI: 10.1073/Pnas.1918721117 |
0.74 |
|
| 2018 |
Garcia-Guerrero MC, Garcia-Pardo J, Berenguer E, Fernandez-Alvarez R, Barfi GB, Lyons PJ, Aviles FX, Huber R, Lorenzo J, Reverter D. Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues. Proceedings of the National Academy of Sciences of the United States of America. PMID 29636417 DOI: 10.1073/Pnas.1803685115 |
0.631 |
|
| 2018 |
Ross B, Krapp S, Augustin M, Kierfersauer R, Arciniega M, Geiss-Friedlander R, Huber R. Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. Proceedings of the National Academy of Sciences of the United States of America. PMID 29382749 DOI: 10.1073/Pnas.1717565115 |
0.411 |
|
| 2016 |
Dahms SO, Arciniega M, Steinmetzer T, Huber R, Than ME. Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism. Proceedings of the National Academy of Sciences of the United States of America. PMID 27647913 DOI: 10.1073/Pnas.1613630113 |
0.415 |
|
| 2015 |
Hierold J, Baek S, Rieger R, Lim TG, Zakpur S, Arciniega M, Lee KW, Huber R, Tietze LF. Design, Synthesis, and Biological Evaluation of Quercetagetin Analogues as JNK1 Inhibitors. Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 16887-94. PMID 26541354 DOI: 10.1002/Chem.201502475 |
0.317 |
|
| 2014 |
Beaufort N, Scharrer E, Kremmer E, Lux V, Ehrmann M, Huber R, Houlden H, Werring D, Haffner C, Dichgans M. Cerebral small vessel disease-related protease HtrA1 processes latent TGF-β binding protein 1 and facilitates TGF-β signaling. Proceedings of the National Academy of Sciences of the United States of America. 111: 16496-501. PMID 25369932 DOI: 10.1073/Pnas.1418087111 |
0.582 |
|
| 2014 |
Lesca E, Lammens A, Huber R, Augustin M. Structural analysis of the human fibroblast growth factor receptor 4 kinase. Journal of Molecular Biology. 426: 3744-56. PMID 25219510 DOI: 10.1016/J.Jmb.2014.09.004 |
0.34 |
|
| 2014 |
Arciniega M, Beck P, Lange OF, Groll M, Huber R. Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding. Proceedings of the National Academy of Sciences of the United States of America. 111: 9479-84. PMID 24979800 DOI: 10.1073/Pnas.1408018111 |
0.314 |
|
| 2013 |
Schneider EV, Böttcher J, Huber R, Maskos K, Neumann L. Structure-kinetic relationship study of CDK8/CycC specific compounds. Proceedings of the National Academy of Sciences of the United States of America. 110: 8081-6. PMID 23630251 DOI: 10.1073/Pnas.1305378110 |
0.36 |
|
| 2013 |
Baek S, Kang NJ, Popowicz GM, Arciniega M, Jung SK, Byun S, Song NR, Heo YS, Kim BY, Lee HJ, Holak TA, Augustin M, Bode AM, Huber R, Dong Z, et al. Structural and functional analysis of the natural JNK1 inhibitor quercetagetin. Journal of Molecular Biology. 425: 411-23. PMID 23142567 DOI: 10.1016/J.Jmb.2012.10.019 |
0.334 |
|
| 2012 |
Tennstaedt A, Pöpsel S, Truebestein L, Hauske P, Brockmann A, Schmidt N, Irle I, Sacca B, Niemeyer CM, Brandt R, Ksiezak-Reding H, Tirniceriu AL, Egensperger R, Baldi A, Dehmelt L, ... ... Huber R, et al. Human high temperature requirement serine protease A1 (HTRA1) degrades tau protein aggregates. The Journal of Biological Chemistry. 287: 20931-41. PMID 22535953 DOI: 10.1074/Jbc.M111.316232 |
0.727 |
|
| 2012 |
Weski J, Meltzer M, Spaan L, Mönig T, Oeljeklaus J, Hauske P, Vouilleme L, Volkmer R, Boisguerin P, Boyd D, Huber R, Kaiser M, Ehrmann M. Chemical biology approaches reveal conserved features of a C-terminal processing PDZ protease. Chembiochem : a European Journal of Chemical Biology. 13: 402-8. PMID 22267294 DOI: 10.1002/Cbic.201100643 |
0.658 |
|
| 2012 |
Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM. Structure of the stapled p53 peptide bound to Mdm2. Journal of the American Chemical Society. 134: 103-6. PMID 22148351 DOI: 10.1021/Ja2090367 |
0.351 |
|
| 2012 |
Gallastegui N, Beck P, Arciniega M, Huber R, Hillebrand S, Groll M. Hydroxyureas as noncovalent proteasome inhibitors. Angewandte Chemie (International Ed. in English). 51: 247-9. PMID 22105886 DOI: 10.1002/Anie.201106010 |
0.336 |
|
| 2011 |
Sitar T, Gallinger J, Ducka AM, Ikonen TP, Wohlhoefler M, Schmoller KM, Bausch AR, Joel P, Trybus KM, Noegel AA, Schleicher M, Huber R, Holak TA. Molecular architecture of the Spire-actin nucleus and its implication for actin filament assembly. Proceedings of the National Academy of Sciences of the United States of America. 108: 19575-80. PMID 22106272 DOI: 10.1073/Pnas.1115465108 |
0.317 |
|
| 2011 |
Schneider EV, Böttcher J, Blaesse M, Neumann L, Huber R, Maskos K. The structure of CDK8/CycC implicates specificity in the CDK/cyclin family and reveals interaction with a deep pocket binder. Journal of Molecular Biology. 412: 251-66. PMID 21806996 DOI: 10.1016/J.Jmb.2011.07.020 |
0.36 |
|
| 2011 |
Merdanovic M, Clausen T, Kaiser M, Huber R, Ehrmann M. Protein quality control in the bacterial periplasm. Annual Review of Microbiology. 65: 149-68. PMID 21639788 DOI: 10.1146/Annurev-Micro-090110-102925 |
0.731 |
|
| 2011 |
Clausen T, Kaiser M, Huber R, Ehrmann M. HTRA proteases: regulated proteolysis in protein quality control. Nature Reviews. Molecular Cell Biology. 12: 152-62. PMID 21326199 DOI: 10.1038/Nrm3065 |
0.761 |
|
| 2010 |
Merdanovic M, Mamant N, Meltzer M, Poepsel S, Auckenthaler A, Melgaard R, Hauske P, Nagel-Steger L, Clarke AR, Kaiser M, Huber R, Ehrmann M. Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nature Structural & Molecular Biology. 17: 837-43. PMID 20581826 DOI: 10.1038/Nsmb.1839 |
0.704 |
|
| 2010 |
Krojer T, Sawa J, Huber R, Clausen T. HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nature Structural & Molecular Biology. 17: 844-52. PMID 20581825 DOI: 10.1038/Nsmb.1840 |
0.785 |
|
| 2010 |
Ducka AM, Joel P, Popowicz GM, Trybus KM, Schleicher M, Noegel AA, Huber R, Holak TA, Sitar T. Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation. Proceedings of the National Academy of Sciences of the United States of America. 107: 11757-62. PMID 20538977 DOI: 10.1073/Pnas.1005347107 |
0.37 |
|
| 2010 |
Hasenbein S, Meltzer M, Hauske P, Kaiser M, Huber R, Clausen T, Ehrmann M. Conversion of a regulatory into a degradative protease. Journal of Molecular Biology. 397: 957-66. PMID 20184896 DOI: 10.1016/J.Jmb.2010.02.027 |
0.763 |
|
| 2009 |
Ottmann C, Rose R, Huttenlocher F, Cedzich A, Hauske P, Kaiser M, Huber R, Schaller A. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3. Proceedings of the National Academy of Sciences of the United States of America. 106: 17223-8. PMID 19805099 DOI: 10.1073/Pnas.0907587106 |
0.371 |
|
| 2009 |
Meltzer M, Hasenbein S, Mamant N, Merdanovic M, Poepsel S, Hauske P, Kaiser M, Huber R, Krojer T, Clausen T, Ehrmann M. Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli. Research in Microbiology. 160: 660-6. PMID 19695325 DOI: 10.1016/J.Resmic.2009.07.012 |
0.79 |
|
| 2009 |
Breithaupt C, Kurzbauer R, Schaller F, Stintzi A, Schaller A, Huber R, Macheroux P, Clausen T. Structural basis of substrate specificity of plant 12-oxophytodienoate reductases. Journal of Molecular Biology. 392: 1266-77. PMID 19660473 DOI: 10.1016/J.Jmb.2009.07.087 |
0.658 |
|
| 2009 |
Lee JH, Maskos K, Huber R. Structural and functional studies of the yeast class II Hda1 histone deacetylase complex. Journal of Molecular Biology. 391: 744-57. PMID 19573535 DOI: 10.1016/J.Jmb.2009.06.059 |
0.4 |
|
| 2009 |
Wolschner C, Giese A, Kretzschmar HA, Huber R, Moroder L, Budisa N. Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 106: 7756-61. PMID 19416900 DOI: 10.1073/Pnas.0902688106 |
0.309 |
|
| 2009 |
Clerc J, Groll M, Illich DJ, Bachmann AS, Huber R, Schellenberg B, Dudler R, Kaiser M. Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition Proceedings of the National Academy of Sciences of the United States of America. 106: 6507-6512. PMID 19359491 DOI: 10.1073/Pnas.0901982106 |
0.375 |
|
| 2009 |
Sanglas L, Aviles FX, Huber R, Gomis-Rüthe FX, Arolas JL. Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite Proceedings of the National Academy of Sciences of the United States of America. 106: 1743-1747. PMID 19179285 DOI: 10.1073/Pnas.0812623106 |
0.625 |
|
| 2009 |
Groll M, Huber R, Moroder L. The persisting challenge of selective and specific proteasome inhibition Journal of Peptide Science. 15: 58-66. PMID 19109822 DOI: 10.1002/Psc.1107 |
0.326 |
|
| 2008 |
Breithaupt C, Schäfer B, Pellkofer H, Huber R, Linington C, Jacob U. Demyelinating myelin oligodendrocyte glycoprotein-specific autoantibody response is focused on one dominant conformational epitope region in rodents Journal of Immunology. 181: 1255-1263. PMID 18606679 DOI: 10.4049/Jimmunol.181.2.1255 |
0.363 |
|
| 2008 |
Chatwell L, Illarionova V, Illarionov B, Eisenreich W, Huber R, Skerra A, Bacher A, Fischer M. Structure of Lumazine Protein, an Optical Transponder of Luminescent Bacteria Journal of Molecular Biology. 382: 44-55. PMID 18602927 DOI: 10.1016/J.Jmb.2008.06.052 |
0.466 |
|
| 2008 |
Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T. Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins Proceedings of the National Academy of Sciences of the United States of America. 105: 7702-7707. PMID 18505836 DOI: 10.1073/Pnas.0803392105 |
0.807 |
|
| 2008 |
Groll M, Schellenberg B, Bachmann AS, Archer CR, Huber R, Powell TK, Lindow S, Kaiser M, Dudler R. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature. 452: 755-8. PMID 18401409 DOI: 10.1038/Nature06782 |
0.346 |
|
| 2008 |
Borelli C, Ruge E, Jung HL, Schaller M, Vogelsang A, Monod M, Korting HC, Huber R, Maskos K. X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans Proteins: Structure, Function and Genetics. 72: 1308-1319. PMID 18384081 DOI: 10.1002/Prot.22021 |
0.407 |
|
| 2007 |
Debela M, Hess P, Magdolen V, Schechter NM, Steiner T, Huber R, Bode W, Goettig P. Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7. Proceedings of the National Academy of Sciences of the United States of America. 104: 16086-91. PMID 17909180 DOI: 10.1073/Pnas.0707811104 |
0.39 |
|
| 2007 |
Debela M, Goettig P, Magdolen V, Huber R, Schechter NM, Bode W. Structural Basis of the Zinc Inhibition of Human Tissue Kallikrein 5 Journal of Molecular Biology. 373: 1017-1031. PMID 17881000 DOI: 10.1016/J.Jmb.2007.08.042 |
0.402 |
|
| 2007 |
Velarde M, Huber R, Yanagisawa S, Dennison C, Messerschmidt A. Influence of loop shortening on the metal binding site of cupredoxin pseudoazurin Biochemistry. 46: 9981-9991. PMID 17685636 DOI: 10.1021/Bi701113W |
0.382 |
|
| 2007 |
Tochowicz A, Maskos K, Huber R, Oltenfreiter R, Dive V, Yiotakis A, Zanda M, Bode W, Goettig P. Crystal Structures of MMP-9 Complexes with Five Inhibitors: Contribution of the Flexible Arg424 Side-chain to Selectivity Journal of Molecular Biology. 371: 989-1006. PMID 17599356 DOI: 10.1016/J.Jmb.2007.05.068 |
0.378 |
|
| 2007 |
Borelli C, Ruge E, Schaller M, Monod M, Korting HC, Huber R, Maskos K. The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A Proteins: Structure, Function and Genetics. 68: 738-748. PMID 17510964 DOI: 10.1002/Prot.21425 |
0.439 |
|
| 2007 |
Kyrieleis OJP, Huber R, Ong E, Oehler R, Hunter M, Madison EL, Jacob U. Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family Febs Journal. 274: 2148-2160. PMID 17388811 DOI: 10.1111/J.1742-4658.2007.05756.X |
0.406 |
|
| 2007 |
Steiner T, Lamerz AC, Hess P, Breithaupt C, Krapp S, Bourenkov G, Huber R, Gerardy-Schahn R, Jacob U. Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major. The Journal of Biological Chemistry. 282: 13003-10. PMID 17303565 DOI: 10.1074/Jbc.M609984200 |
0.413 |
|
| 2007 |
Keil C, Maskos K, Than M, Hoopes JT, Huber R, Tan F, Deddish PA, Erdös EG, Skidgel RA, Bode W. Crystal Structure of the Human Carboxypeptidase N (Kininase I) Catalytic Domain Journal of Molecular Biology. 366: 504-516. PMID 17157876 DOI: 10.1016/J.Jmb.2006.11.025 |
0.44 |
|
| 2007 |
Groll M, Huber R, Potts BC. Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding. Journal of the American Chemical Society. 128: 5136-41. PMID 16608349 DOI: 10.1021/ja058320b |
0.316 |
|
| 2006 |
Breithaupt C, Kurzbauer R, Lilie H, Schaller A, Strassner J, Huber R, Macheroux P, Clausen T. Crystal structure of 12-oxophytodienoate reductase 3 from tomato: Self-inhibition by dimerization Proceedings of the National Academy of Sciences of the United States of America. 103: 14337-14342. PMID 16983071 DOI: 10.1073/Pnas.0606603103 |
0.669 |
|
| 2006 |
Tamulaitiene G, Jakubauskas A, Urbanke C, Huber R, Grazulis S, Siksnys V. The Crystal Structure of the Rare-Cutting Restriction Enzyme SdaI Reveals Unexpected Domain Architecture Structure. 14: 1389-1400. PMID 16962970 DOI: 10.1016/J.Str.2006.07.002 |
0.416 |
|
| 2006 |
Debela M, Magdolen V, Grimminger V, Sommerhoff C, Messerschmidt A, Huber R, Friedrich R, Bode W, Goettig P. Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. Journal of Molecular Biology. 362: 1094-107. PMID 16950394 DOI: 10.1016/J.Jmb.2006.08.003 |
0.396 |
|
| 2006 |
Sitar T, Popowicz GM, Siwanowicz I, Huber R, Holak TA. Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins. Proceedings of the National Academy of Sciences of the United States of America. 103: 13028-33. PMID 16924115 DOI: 10.1073/Pnas.0605652103 |
0.35 |
|
| 2006 |
Chatwell L, Krojer T, Fidler A, Römisch W, Eisenreich W, Bacher A, Huber R, Fischer M. Biosynthesis of Riboflavin: Structure and Properties of 2,5-Diamino-6-ribosylamino-4(3H)-pyrimidinone 5′-phosphate Reductase of Methanocaldococcus jannaschii Journal of Molecular Biology. 359: 1334-1351. PMID 16730025 DOI: 10.1016/J.Jmb.2006.04.045 |
0.681 |
|
| 2006 |
Groll M, Larionov OV, Huber R, de Meijere A. Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation. Proceedings of the National Academy of Sciences of the United States of America. 103: 4576-9. PMID 16537370 DOI: 10.1073/Pnas.0600647103 |
0.363 |
|
| 2006 |
Engel M, Hoffmann T, Manhart S, Heiser U, Chambre S, Huber R, Demuth HU, Bode W. Rigidity and flexibility of dipeptidyl peptidase IV: Crystal structures of and docking experiments with DPIV Journal of Molecular Biology. 355: 768-783. PMID 16330047 DOI: 10.1016/J.Jmb.2005.11.014 |
0.421 |
|
| 2006 |
Ramsperger A, Augustin M, Schott AK, Gerhardt S, Krojer T, Eisenreich W, Illarionov B, Cushman M, Bacher A, Huber R, Fischer M. Crystal structure of an archaeal pentameric riboflavin synthase in complex with a substrate analog inhibitor: Stereochemical implications Journal of Biological Chemistry. 281: 1224-1232. PMID 16272154 DOI: 10.1074/Jbc.M509440200 |
0.701 |
|
| 2006 |
Engh RA, Huber R. Structure quality and target parameters International Tables For Crystallography. DOI: 10.1107/97809553602060000695 |
0.354 |
|
| 2005 |
Einsle O, Niessen H, Abt DJ, Seiffert G, Schink B, Huber R, Messerschmidt A, Kroneck PMH. Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 61: 299-301. PMID 16511024 DOI: 10.1107/S174430910500374X |
0.58 |
|
| 2005 |
Golbik R, Yu C, Weyher-Stingl E, Huber R, Moroder L, Budisa N, Schiene-Fischer C. Peptidyl prolyl cis/trans-isomerases: Comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates Biochemistry. 44: 16026-16034. PMID 16331962 DOI: 10.1021/Bi051442W |
0.39 |
|
| 2005 |
Groll M, Huber R. Purification, crystallization, and X-ray analysis of the yeast 20S proteasome. Methods in Enzymology. 398: 329-36. PMID 16275340 DOI: 10.1016/S0076-6879(05)98027-0 |
0.413 |
|
| 2005 |
Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V. Structure of the metal-independent restriction enzyme Bfil reveals fusion of a specific DNA-binding domain with a nonspecific nuclease Proceedings of the National Academy of Sciences of the United States of America. 102: 15797-15802. PMID 16247004 DOI: 10.1073/Pnas.0507949102 |
0.657 |
|
| 2005 |
Breitenlechner CB, Kairies NA, Honold K, Scheiblich S, Koll H, Greiter E, Koch S, Schäfer W, Huber R, Engh RA. Crystal structures of active Src kinase domain complexes Journal of Molecular Biology. 353: 222-231. PMID 16168436 DOI: 10.1016/J.Jmb.2005.08.023 |
0.421 |
|
| 2005 |
Arolas JL, Popowicz GM, Bronsoms S, Aviles FX, Huber R, Holak TA, Ventura S. Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: Contribution of the fourth disulfide bond Journal of Molecular Biology. 352: 961-975. PMID 16126224 DOI: 10.1016/J.Jmb.2005.07.065 |
0.614 |
|
| 2005 |
Arolas JL, Popowicz GM, Lorenzo J, Sommerhoff CP, Huber R, Aviles FX, Holak TA. The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode Journal of Molecular Biology. 350: 489-498. PMID 15961103 DOI: 10.1016/J.Jmb.2005.05.015 |
0.661 |
|
| 2005 |
Kyrieleis OJP, Goettig P, Kiefersauer R, Huber R, Brandstetter H. Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations Journal of Molecular Biology. 349: 787-800. PMID 15893768 DOI: 10.1016/J.Jmb.2005.03.070 |
0.393 |
|
| 2005 |
Moissl C, Rachel R, Briegel A, Engelhardt H, Huber R. The unique structure of archaeal 'hami', highly complex cell appendages with nano-grappling hooks. Molecular Microbiology. 56: 361-70. PMID 15813730 DOI: 10.1111/J.1365-2958.2005.04294.X |
0.305 |
|
| 2005 |
Pal PP, Bae JH, Azim MK, Hess P, Friedrich R, Huber R, Moroder L, Budisa N. Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination. Biochemistry. 44: 3663-72. PMID 15751943 DOI: 10.1021/Bi0484825 |
0.359 |
|
| 2005 |
Jauch R, Humm A, Huber R, Wahl MC. Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements Journal of Biological Chemistry. 280: 15131-15140. PMID 15699042 DOI: 10.1074/Jbc.M413195200 |
0.426 |
|
| 2005 |
Groll M, Bochtler M, Brandstetter H, Clausen T, Huber R. Molecular machines for protein degradation. Chembiochem : a European Journal of Chemical Biology. 6: 222-56. PMID 15678420 DOI: 10.1002/Cbic.200400313 |
0.739 |
|
| 2005 |
Theodoratou E, Huber R, Böck A. [NiFe]-hydrogenase maturation endopeptidase: Structure and function Biochemical Society Transactions. 33: 108-111. PMID 15667279 DOI: 10.1042/Bst0330108 |
0.393 |
|
| 2005 |
Siwanowicz I, Popowicz GM, Wisniewska M, Huber R, Kuenkele KP, Lang K, Engh RA, Holak TA. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993). 13: 155-67. PMID 15642270 DOI: 10.1016/J.Str.2004.11.009 |
0.346 |
|
| 2005 |
Breitenlechner CB, Friebe WG, Brunet E, Werner G, Graul K, Thomas U, Künkele KP, Schäfer W, Gassel M, Bossemeyer D, Huber R, Engh RA, Masjost B. Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants. Journal of Medicinal Chemistry. 48: 163-70. PMID 15634010 DOI: 10.1021/Jm049701N |
0.337 |
|
| 2005 |
Yarim M, Moro S, Huber R, Meier PJ, Kaseda C, Kashima T, Hagenbuch B, Folkers G. Application of QSAR analysis to organic anion transporting polypeptide 1a5 (Oatp1a5) substrates Bioorganic and Medicinal Chemistry. 13: 463-471. PMID 15598568 DOI: 10.1016/J.Bmc.2004.10.009 |
0.329 |
|
| 2005 |
Gomis-Rüth FX, Fita I, Kiefersauer R, Huber R, Avilés FX, Navaza J. Determination of hemihedral twinning and initial structural analysis of crystals of the procarboxypeptidase A ternary complex. Acta Crystallographica. Section D, Biological Crystallography. 51: 819-23. PMID 15299814 DOI: 10.1107/S0907444995000643 |
0.575 |
|
| 2004 |
Wenig K, Chatwell L, Von Pawel-Rammingen U, Björck L, Huber R, Sondermann P. Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG Proceedings of the National Academy of Sciences of the United States of America. 101: 17371-17376. PMID 15574492 DOI: 10.1073/Pnas.0407965101 |
0.459 |
|
| 2004 |
Groll M, Huber R. Inhibitors of the eukaryotic 20S proteasome core particle: A structural approach Biochimica Et Biophysica Acta - Molecular Cell Research. 1695: 33-44. PMID 15571807 DOI: 10.1016/J.Bbamcr.2004.09.025 |
0.409 |
|
| 2004 |
Stanitzek S, Augustin MA, Huber R, Kupke T, Steinbacher S. Structural basis of CTP-dependent peptide bond formation in coenzyme a biosynthesis catalyzed by Escherichia coli PPC synthetase Structure. 12: 1977-1988. PMID 15530362 DOI: 10.1016/J.Str.2004.08.007 |
0.44 |
|
| 2004 |
Fischer M, Schott AK, Römisch W, Ramsperger A, Augustin M, Fidler A, Bacher A, Richter G, Huber R, Eisenreich W. Evolution of vitamin B 2 biosynthesis. A novel class of riboflavin synthase in Archaea Journal of Molecular Biology. 343: 267-278. PMID 15381435 DOI: 10.1016/J.Jmb.2004.08.016 |
0.388 |
|
| 2004 |
Kaiser M, Groll M, Siciliano C, Assfalg-Machleidt I, Weyher E, Kohno J, Milbradt AG, Renner C, Huber R, Moroder L. Binding mode of TMC-95A analogues to eukaryotic 20S proteasome Chembiochem. 5: 1256-1266. PMID 15368577 DOI: 10.1002/Cbic.200400096 |
0.419 |
|
| 2004 |
Popowicz GM, Müller R, Noegel AA, Schleicher M, Huber R, Holak TA. Molecular structure of the rod domain of Dictyostelium filamin Journal of Molecular Biology. 342: 1637-1646. PMID 15364587 DOI: 10.1016/J.Jmb.2004.08.017 |
0.371 |
|
| 2004 |
Keil C, Huber R, Bode W, Than ME. Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP Acta Crystallographica Section D: Biological Crystallography. 60: 1614-1617. PMID 15333934 DOI: 10.1107/S0907444904015343 |
0.381 |
|
| 2004 |
Echt S, Bauer S, Steinbacher S, Huber R, Bacher A, Fischer M. Potential anti-infective targets in pathogenic yeasts: Structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans Journal of Molecular Biology. 341: 1085-1096. PMID 15328619 DOI: 10.1016/J.Jmb.2004.06.053 |
0.454 |
|
| 2004 |
Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H. Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase Structure. 12: 1425-1435. PMID 15296736 DOI: 10.1016/J.Str.2004.05.014 |
0.401 |
|
| 2004 |
Koch M, Breithaupt C, Gerhardt S, Haase I, Weber S, Cushman M, Huber R, Bacher A, Fischer M. Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase European Journal of Biochemistry. 271: 3208-3214. PMID 15265040 DOI: 10.1111/J.1432-1033.2004.04253.X |
0.388 |
|
| 2004 |
Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W. 1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin: Structure of an intact pro-subtilase Structure. 12: 1313-1323. PMID 15242607 DOI: 10.1016/J.Str.2004.04.013 |
0.464 |
|
| 2004 |
Laupitz R, Hecht S, Amslinger S, Zepeck F, Kaiser J, Richter G, Schramek N, Steinbacher S, Huber R, Arigoni D, Bacher A, Eisenreich W, Rohdich F. Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways. European Journal of Biochemistry / Febs. 271: 2658-69. PMID 15206931 DOI: 10.1111/J.1432-1033.2004.04194.X |
0.329 |
|
| 2004 |
Breitenlechner C, Engh RA, Huber R, Kinzel V, Bossemeyer D, Gassel M. The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution Biochemistry. 43: 7743-7749. PMID 15196017 DOI: 10.1021/Bi0362525 |
0.343 |
|
| 2004 |
Bauer S, Schott AK, Illarionova V, Bacher A, Huber R, Fischer M. Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class Journal of Molecular Biology. 339: 967-979. PMID 15165863 DOI: 10.1016/J.Jmb.2004.04.034 |
0.448 |
|
| 2004 |
Bader G, Gomez-Ortiz M, Haussmann C, Bacher A, Huber R, Fischer M. Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli Acta Crystallographica Section D: Biological Crystallography. 60: 1068-1075. PMID 15159566 DOI: 10.1107/S0907444904007164 |
0.423 |
|
| 2004 |
Fritze IM, Linden L, Freigang J, Auerbach G, Huber R, Steinbacher S. The crystal structures of Zea mays and arabidopsis 4-hydroxyphenylpyruvate dioxygenase Plant Physiology. 134: 1388-1400. PMID 15084729 DOI: 10.1104/Pp.103.034082 |
0.436 |
|
| 2004 |
Koch M, Breithaupt C, Kiefersauer R, Freigang J, Huber R, Messerschmidt A. Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis Embo Journal. 23: 1720-1728. PMID 15057273 DOI: 10.1038/Sj.Emboj.7600189 |
0.442 |
|
| 2004 |
Than ME, Helm M, Simpson DJ, Lottspeich F, Huber R, Gietl C. The 2.0 Å Crystal Structure and Substrate Specificity of the KDEL-tailed Cysteine Endopeptidase Functioning in Programmed Cell Death of Ricinus communis Endosperm Journal of Molecular Biology. 336: 1103-1116. PMID 15037072 DOI: 10.1016/J.Jmb.2003.12.075 |
0.456 |
|
| 2004 |
Svetlitchnyi V, Dobbek H, Meyer-Klaucke W, Meins T, Thiele B, Römer P, Huber R, Meyer O. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans Proceedings of the National Academy of Sciences of the United States of America. 101: 446-451. PMID 14699043 DOI: 10.1073/Pnas.0304262101 |
0.314 |
|
| 2004 |
Kim JS, Kluskens LD, De Vos WM, Huber R, Van Der Oost J. Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin Journal of Molecular Biology. 335: 787-797. PMID 14687574 DOI: 10.1016/J.Jmb.2003.11.006 |
0.418 |
|
| 2003 |
Breitenlechner C, Gaßel M, Hidaka H, Kinzel V, Huber R, Engh RA, Bossemeyer D. Protein Kinase a in Complex with Rho-Kinase Inhibitors Y-27632, Fasudil, and H-1152P: Structural Basis of Selectivity Structure. 11: 1595-1607. PMID 14656443 DOI: 10.1016/J.Str.2003.11.002 |
0.313 |
|
| 2003 |
Krapp S, Münster-Kühnel AK, Kaiser JT, Huber R, Tiralongo J, Gerardy-Schahn R, Jacob U. The crystal structure of murine CMP-5-N-acetylneuraminic acid synthetase Journal of Molecular Biology. 334: 625-637. PMID 14636592 DOI: 10.1016/J.Jmb.2003.09.080 |
0.417 |
|
| 2003 |
Friedrich R, Panizzi P, Fuentes-Prior P, Richter K, Verhamme I, Anderson PJ, Kawabata S, Huber R, Bode W, Bock PE. Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation. Nature. 425: 535-9. PMID 14523451 DOI: 10.1038/Nature01962 |
0.416 |
|
| 2003 |
Macieira S, Martins BM, Huber R. Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation. Fems Microbiology Letters. 226: 31-7. PMID 13129604 DOI: 10.1016/S0378-1097(03)00531-7 |
0.359 |
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| 2003 |
Jozic D, Kaiser JT, Huber R, Bode W, Maskos K. X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases. Journal of Molecular Biology. 332: 243-56. PMID 12946361 DOI: 10.1016/S0022-2836(03)00845-3 |
0.416 |
|
| 2003 |
Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M. Structure and Properties of an Engineered Transketolase from Maize Plant Physiology. 132: 1941-1949. PMID 12913150 DOI: 10.1104/Pp.103.020982 |
0.439 |
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| 2003 |
Steinbacher S, Schiffmann S, Richter G, Huber R, Bacher A, Fischer M. Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: Implications for the catalytic mechanism Journal of Biological Chemistry. 278: 42256-42265. PMID 12904291 DOI: 10.1074/Jbc.M307301200 |
0.374 |
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| 2003 |
Blaesse M, Kupke T, Huber R, Steinbacher S. Structure of MrsD, an FAD-binding protein of the HFCD family. Acta Crystallographica. Section D, Biological Crystallography. 59: 1414-21. PMID 12876343 DOI: 10.1107/S0907444903011831 |
0.425 |
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| 2003 |
Breithaupt C, Schubart A, Zander H, Skerra A, Huber R, Linington C, Jacob U. Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein Proceedings of the National Academy of Sciences of the United States of America. 100: 9446-9451. PMID 12874380 DOI: 10.1073/Pnas.1133443100 |
0.352 |
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| 2003 |
Wendt KS, Schall I, Huber R, Buckel W, Jacob U. Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase Embo Journal. 22: 3493-3502. PMID 12853465 DOI: 10.1093/Emboj/Cdg358 |
0.356 |
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| 2003 |
Gassel M, Breitenlechner CB, Rüger P, Jucknischke U, Schneider T, Huber R, Bossemeyer D, Engh RA. Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT). Journal of Molecular Biology. 329: 1021-34. PMID 12798691 DOI: 10.1016/S0022-2836(03)00518-7 |
0.408 |
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| 2003 |
Steinbacher S, Kaiser J, Gerhardt S, Eisenreich W, Huber R, Bacher A, Rohdich F. Crystal structure of the type II isopentenyl diphosphate:dimethylallyl diphosphate isomerase from Bacillus subtilis. Journal of Molecular Biology. 329: 973-82. PMID 12798687 DOI: 10.1016/S0022-2836(03)00527-8 |
0.438 |
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| 2003 |
Henrich S, Cameron A, Bourenkov GP, Kiefersauer R, Huber R, Lindberg I, Bode W, Than ME. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nature Structural Biology. 10: 520-6. PMID 12794637 DOI: 10.1038/Nsb941 |
0.409 |
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| 2003 |
Augustin MA, Reichert AS, Betat H, Huber R, Mörl M, Steegborn C. Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization. Journal of Molecular Biology. 328: 985-94. PMID 12729736 DOI: 10.1016/S0022-2836(03)00381-4 |
0.474 |
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| 2003 |
Messerschmidt A, Worbs M, Steegborn C, Wahl MC, Huber R, Laber B, Clausen T. Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison. Biological Chemistry. 384: 373-86. PMID 12715888 DOI: 10.1515/BC.2003.043 |
0.657 |
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| 2003 |
Engel M, Hoffmann T, Wagner L, Wermann M, Heiser U, Kiefersauer R, Huber R, Bode W, Demuth HU, Brandstetter H. The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proceedings of the National Academy of Sciences of the United States of America. 100: 5063-8. PMID 12690074 DOI: 10.1073/Pnas.0230620100 |
0.476 |
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| 2003 |
Groll M, Huber R. Substrate access and processing by the 20S proteasome core particle. The International Journal of Biochemistry & Cell Biology. 35: 606-16. PMID 12672453 DOI: 10.1016/S1357-2725(02)00390-4 |
0.36 |
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| 2003 |
Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R. Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Biophysical Chemistry. 100: 437-52. PMID 12646382 DOI: 10.1016/S0301-4622(02)00297-1 |
0.803 |
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| 2003 |
Steinbacher S, Kaiser J, Eisenreich W, Huber R, Bacher A, Rohdich F. Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development. The Journal of Biological Chemistry. 278: 18401-7. PMID 12621040 DOI: 10.1074/Jbc.M300993200 |
0.389 |
|
| 2003 |
Cunha CA, Macieira S, Dias JM, Almeida G, Goncalves LL, Costa C, Lampreia J, Huber R, Moura JJ, Moura I, Romão MJ. Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA). The Journal of Biological Chemistry. 278: 17455-65. PMID 12618432 DOI: 10.1074/Jbc.M211777200 |
0.398 |
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| 2003 |
Steinbacher S, Hernández-Acosta P, Bieseler B, Blaesse M, Huber R, Culiáñez-Macià FA, Kupke T. Crystal structure of the plant PPC decarboxylase AtHAL3a complexed with an ene-thiol reaction intermediate. Journal of Molecular Biology. 327: 193-202. PMID 12614618 DOI: 10.1016/S0022-2836(03)00092-5 |
0.395 |
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| 2003 |
Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R. Investigations on the maturation and regulation of archaebacterial proteasomes. Journal of Molecular Biology. 327: 75-83. PMID 12614609 DOI: 10.1016/S0022-2836(03)00080-9 |
0.389 |
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| 2003 |
Bauer S, Kemter K, Bacher A, Huber R, Fischer M, Steinbacher S. Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. Journal of Molecular Biology. 326: 1463-73. PMID 12595258 DOI: 10.1016/S0022-2836(03)00059-7 |
0.432 |
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| 2003 |
Fischer M, Haase I, Kis K, Meining W, Ladenstein R, Cushman M, Schramek N, Huber R, Bacher A. Enzyme catalysis via control of activation entropy: site-directed mutagenesis of 6,7-dimethyl-8-ribityllumazine synthase. Journal of Molecular Biology. 326: 783-793. PMID 12581640 DOI: 10.1016/S0022-2836(02)01473-0 |
0.371 |
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| 2003 |
Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, Hösl C, Schramek N, Kaiser J, Bacher A, Huber R, Fischer M. Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. Journal of Molecular Biology. 326: 503-16. PMID 12559918 DOI: 10.1016/S0022-2836(02)01303-7 |
0.43 |
|
| 2003 |
Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. Journal of Molecular Biology. 325: 979-89. PMID 12527303 DOI: 10.1016/S0022-2836(02)01250-0 |
0.355 |
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| 2003 |
Kim JS, Groll M, Musiol HJ, Behrendt R, Kaiser M, Moroder L, Huber R, Brandstetter H. Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum. Journal of Molecular Biology. 324: 1041-50. PMID 12470958 DOI: 10.1016/S0022-2836(02)01153-1 |
0.409 |
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| 2003 |
Rehm T, Huber R, Holak TA. Application of NMR in structural proteomics: screening for proteins amenable to structural analysis. Structure (London, England : 1993). 10: 1613-8. PMID 12467568 DOI: 10.1016/S0969-2126(02)00894-8 |
0.361 |
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| 2003 |
Brandstetter H, Kim JS, Groll M, Göttig P, Huber R. Structural basis for the processive protein degradation by tricorn protease. Biological Chemistry. 383: 1157-65. PMID 12437101 DOI: 10.1515/Bc.2002.127 |
0.373 |
|
| 2003 |
Gerhardt S, Schott AK, Kairies N, Cushman M, Illarionov B, Eisenreich W, Bacher A, Huber R, Steinbacher S, Fischer M. Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine. Structure (London, England : 1993). 10: 1371-81. PMID 12377123 DOI: 10.1016/S0969-2126(02)00864-X |
0.479 |
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| 2003 |
Cushman M, Yang D, Mihalic JT, Chen J, Gerhardt S, Huber R, Fischer M, Kis K, Bacher A. Incorporation of an amide into 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors results in an unexpected reversal of selectivity for riboflavin synthase vs lumazine synthase. The Journal of Organic Chemistry. 67: 6871-7. PMID 12353976 DOI: 10.1021/Jo020144R |
0.352 |
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| 2003 |
Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K. Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. Structure (London, England : 1993). 10: 1097-106. PMID 12176387 DOI: 10.1016/S0969-2126(02)00805-5 |
0.436 |
|
| 2002 |
Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O. Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution Proceedings of the National Academy of Sciences of the United States of America. 99: 15971-15976. PMID 12475995 DOI: 10.1073/Pnas.212640899 |
0.339 |
|
| 2002 |
Sichler K, Kopetzki E, Huber R, Bode W, Hopfner KP, Brandstetter H. Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop. The Journal of Biological Chemistry. 278: 4121-6. PMID 12444082 DOI: 10.1074/Jbc.M210722200 |
0.399 |
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| 2002 |
Sichler K, Hopfner KP, Kopetzki E, Huber R, Bode W, Brandstetter H. The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved. Febs Letters. 530: 220-4. PMID 12387896 DOI: 10.1016/S0014-5793(02)03495-6 |
0.348 |
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| 2002 |
Kaiser JT, Bruno S, Clausen T, Huber R, Schiaretti F, Mozzarelli A, Kessler D. Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state. The Journal of Biological Chemistry. 278: 357-65. PMID 12386155 DOI: 10.1074/Jbc.M209862200 |
0.678 |
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| 2002 |
Goettig P, Groll M, Kim JS, Huber R, Brandstetter H. Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. The Embo Journal. 21: 5343-52. PMID 12374735 DOI: 10.1093/Emboj/Cdf552 |
0.419 |
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| 2002 |
Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F. Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase. Journal of the American Chemical Society. 124: 11737-45. PMID 12296741 DOI: 10.1021/Ja0206487 |
0.688 |
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| 2002 |
Sichler K, Banner DW, D'Arcy A, Hopfner KP, Huber R, Bode W, Kresse GB, Kopetzki E, Brandstetter H. Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions Journal of Molecular Biology. 322: 591-603. PMID 12225752 DOI: 10.1016/S0022-2836(02)00747-7 |
0.37 |
|
| 2002 |
Raaijmakers H, Macieira S, Dias JM, Teixeira S, Bursakov S, Huber R, Moura JJ, Moura I, Romão MJ. Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure (London, England : 1993). 10: 1261-72. PMID 12220497 DOI: 10.1016/S0969-2126(02)00826-2 |
0.396 |
|
| 2002 |
Garrido-Franco M, Laber B, Huber R, Clausen T. Enzyme-ligand complexes of pyridoxine 5'-phosphate synthase: implications for substrate binding and catalysis. Journal of Molecular Biology. 321: 601-12. PMID 12206776 DOI: 10.1016/S0022-2836(02)00695-2 |
0.682 |
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| 2002 |
Fischer M, Romisch W, Schiffmann S, Kelly M, Oschkinat H, Steinbacher S, Huber R, Eisenreich W, Richter G, Bacher A. Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii. The Journal of Biological Chemistry. 277: 41410-6. PMID 12200440 DOI: 10.1074/Jbc.M206863200 |
0.368 |
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| 2002 |
Steiner T, Kaiser JT, Marinkoviç S, Huber R, Wahl MC. Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities. The Embo Journal. 21: 4641-53. PMID 12198166 DOI: 10.1093/Emboj/Cdf455 |
0.413 |
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| 2002 |
Atzenhofer W, Regelsberger G, Jacob U, Peschek G, Furtmüller P, Huber R, Obinger C. The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase. Journal of Molecular Biology. 321: 479-89. PMID 12162960 DOI: 10.1016/S0022-2836(02)00624-1 |
0.404 |
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| 2002 |
Cushman M, Yang D, Gerhardt S, Huber R, Fischer M, Kis K, Bacher A. Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase. The Journal of Organic Chemistry. 67: 5807-16. PMID 12153285 DOI: 10.1021/Jo0201631 |
0.364 |
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| 2002 |
Braun N, Meining W, Hars U, Fischer M, Ladenstein R, Huber R, Bacher A, Weinkauf S, Bachmann L. Formation of metal nanoclusters on specific surface sites of protein molecules. Journal of Molecular Biology. 321: 341-53. PMID 12144790 DOI: 10.1016/S0022-2836(02)00622-8 |
0.36 |
|
| 2002 |
Cha H, Kopetzki E, Huber R, Lanzendörfer M, Brandstetter H. Structural basis of the adaptive molecular recognition by MMP9. Journal of Molecular Biology. 320: 1065-79. PMID 12126625 DOI: 10.1016/S0022-2836(02)00558-2 |
0.387 |
|
| 2002 |
Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W. The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase. Structure (London, England : 1993). 10: 865-76. PMID 12057200 DOI: 10.1016/S0969-2126(02)00772-4 |
0.413 |
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| 2002 |
Ramachandran R, Hartmann C, Song HK, Huber R, Bochtler M. Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY). Proceedings of the National Academy of Sciences of the United States of America. 99: 7396-401. PMID 12032294 DOI: 10.1073/Pnas.102188799 |
0.795 |
|
| 2002 |
Groll M, Nazif T, Huber R, Bogyo M. Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome. Chemistry & Biology. 9: 655-62. PMID 12031672 DOI: 10.1016/S1074-5521(02)00144-8 |
0.425 |
|
| 2002 |
Than ME, Henrich S, Huber R, Ries A, Mann K, Kühn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W. The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proceedings of the National Academy of Sciences of the United States of America. 99: 6607-12. PMID 12011424 DOI: 10.1073/Pnas.062183499 |
0.381 |
|
| 2002 |
Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine Nature. 416: 455-459. PMID 11919638 DOI: 10.1038/416455A |
0.821 |
|
| 2002 |
Schramek N, Bracher A, Fischer M, Auerbach G, Nar H, Huber R, Bacher A. Reaction mechanism of GTP cyclohydrolase I: single turnover experiments using a kinetically competent reaction intermediate. Journal of Molecular Biology. 316: 829-37. PMID 11866535 DOI: 10.1006/Jmbi.2001.5339 |
0.311 |
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| 2002 |
Fischer M, Haase I, Feicht R, Richter G, Gerhardt S, Changeux JP, Huber R, Bacher A. Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. European Journal of Biochemistry / Febs. 269: 519-26. PMID 11856310 DOI: 10.1046/J.0014-2956.2001.02674.X |
0.384 |
|
| 2002 |
Grazulis S, Deibert M, Rimseliene R, Skirgaila R, Sasnauskas G, Lagunavicius A, Repin V, Urbanke C, Huber R, Siksnys V. Crystal structure of the Bse634I restriction endonuclease: comparison of two enzymes recognizing the same DNA sequence. Nucleic Acids Research. 30: 876-85. PMID 11842098 DOI: 10.1093/Nar/30.4.876 |
0.445 |
|
| 2002 |
Rebelo JM, Dias JM, Huber R, Moura JJ, Romão MJ. Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 791-800. PMID 11713686 DOI: 10.1007/S007750100255 |
0.364 |
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| 2002 |
Steegborn C, Danot O, Huber R, Clausen T. Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization. Structure (London, England : 1993). 9: 1051-60. PMID 11709169 DOI: 10.1016/S0969-2126(01)00665-7 |
0.637 |
|
| 2002 |
Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. The Journal of Biological Chemistry. 277: 2160-8. PMID 11696548 DOI: 10.1074/Jbc.M109830200 |
0.432 |
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| 2002 |
Augustin MA, Huber R, Kaiser JT. Structural implications for substrate binding byPyrococcus furiosusDNA primase Acta Crystallographica Section a Foundations of Crystallography. 58: c273-c273. DOI: 10.1107/S0108767302095909 |
0.378 |
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| 2002 |
Breithaupt C, Macheroux P, Schaller A, Huber R, Clausen T. Crystallographic studies of 12-oxophytodienoate reductases from tomato Acta Crystallographica Section a Foundations of Crystallography. 58: c96-c96. DOI: 10.1107/S0108767302088876 |
0.596 |
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| 2002 |
Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. Erratum: corrigendum: Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine Nature. 417: 102-102. DOI: 10.1038/417102c |
0.787 |
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| 2001 |
Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. The Journal of Biological Chemistry. 277: 12396-405. PMID 11756443 DOI: 10.1074/Jbc.M108734200 |
0.712 |
|
| 2001 |
Riedl SJ, Fuentes-Prior P, Renatus M, Kairies N, Krapp S, Huber R, Salvesen GS, Bode W. Structural basis for the activation of human procaspase-7 Proceedings of the National Academy of Sciences of the United States of America. 98: 14790-14795. PMID 11752425 DOI: 10.1073/Pnas.221580098 |
0.398 |
|
| 2001 |
Bochtler M, Song HK, Hartmann C, Ramachandran R, Huber R. The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale. Journal of Structural Biology. 135: 281-93. PMID 11722168 DOI: 10.1006/Jsbi.2001.4413 |
0.709 |
|
| 2001 |
Brandstetter H, Kim JS, Groll M, Huber R. Crystal structure of the tricorn protease reveals a protein disassembly line. Nature. 414: 466-70. PMID 11719810 DOI: 10.1038/35106609 |
0.45 |
|
| 2001 |
Kairies N, Beisel HG, Fuentes-Prior P, Tsuda R, Muta T, Iwanaga S, Bode W, Huber R, Kawabata S. The 2.0-A crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. Proceedings of the National Academy of Sciences of the United States of America. 98: 13519-24. PMID 11707569 DOI: 10.1073/Pnas.201523798 |
0.309 |
|
| 2001 |
Ullrich TC, Huber R. The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle. Journal of Molecular Biology. 313: 1117-25. PMID 11700067 DOI: 10.1006/Jmbi.2001.5098 |
0.401 |
|
| 2001 |
Macedo-Ribeiro S, Martins BM, Pereira PB, Buse G, Huber R, Soulimane T. New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus Journal of Biological Inorganic Chemistry. 6: 663-674. PMID 11681700 DOI: 10.1007/S007750100243 |
0.347 |
|
| 2001 |
Estébanez-Perpiñá E, Bayés A, Vendrell J, Jongsma MA, Bown DP, Gatehouse JA, Huber R, Bode W, Avilés FX, Reverter D. Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera. Journal of Molecular Biology. 313: 629-38. PMID 11676544 DOI: 10.1006/Jmbi.2001.5076 |
0.655 |
|
| 2001 |
Song HK, Mulrooney SB, Huber R, Hausinger RP. Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation. The Journal of Biological Chemistry. 276: 49359-64. PMID 11591723 DOI: 10.1074/Jbc.M108619200 |
0.575 |
|
| 2001 |
Bader G, Schiffmann S, Herrmann A, Fischer M, Gütlich M, Auerbach G, Ploom T, Bacher A, Huber R, Lemm T. Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP. Journal of Molecular Biology. 312: 1051-7. PMID 11580249 DOI: 10.1006/Jmbi.2001.5011 |
0.384 |
|
| 2001 |
Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K. Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure. Journal of Molecular Biology. 312: 731-42. PMID 11575928 DOI: 10.1006/Jmbi.2001.4954 |
0.347 |
|
| 2001 |
Wendt KS, Vodermaier HC, Jacob U, Gieffers C, Gmachl M, Peters JM, Huber R, Sondermann P. Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex. Nature Structural Biology. 8: 784-8. PMID 11524682 DOI: 10.1038/nsb0901-784 |
0.354 |
|
| 2001 |
Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A. Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism. The Journal of Biological Chemistry. 276: 44108-16. PMID 11524417 DOI: 10.1074/jbc.M104759200 |
0.359 |
|
| 2001 |
Steegborn C, Laber B, Messerschmidt A, Huber R, Clausen T. Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor. Journal of Molecular Biology. 311: 789-801. PMID 11518531 DOI: 10.1006/jmbi.2001.4880 |
0.646 |
|
| 2001 |
Zesławski W, Beisel HG, Kamionka M, Kalus W, Engh RA, Huber R, Lang K, Holak TA. The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5. The Embo Journal. 20: 3638-44. PMID 11447105 DOI: 10.1093/Emboj/20.14.3638 |
0.306 |
|
| 2001 |
Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Molecular Cell. 7: 1177-89. PMID 11430821 DOI: 10.1016/S1097-2765(01)00262-3 |
0.366 |
|
| 2001 |
Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A. The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity. Plant Physiology. 126: 631-42. PMID 11402193 DOI: 10.1104/pp.126.2.631 |
0.648 |
|
| 2001 |
Breithaupt C, Strassner J, Breitinger U, Huber R, Macheroux P, Schaller A, Clausen T. X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure (London, England : 1993). 9: 419-29. PMID 11377202 DOI: 10.1016/S0969-2126(01)00602-5 |
0.639 |
|
| 2001 |
Köhler A, Bajorek M, Groll M, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D. The substrate translocation channel of the proteasome Biochimie. 83: 325-332. PMID 11295493 DOI: 10.1016/S0300-9084(01)01242-1 |
0.317 |
|
| 2001 |
Franco MG, Laber B, Huber R, Clausen T. Structural basis for the function of pyridoxine 5'-phosphate synthase. Structure (London, England : 1993). 9: 245-53. PMID 11286891 DOI: 10.1016/S0969-2126(01)00584-6 |
0.62 |
|
| 2001 |
Brandstetter H, Grams F, Glitz D, Lang A, Huber R, Bode W, Krell HW, Engh RA. The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. The Journal of Biological Chemistry. 276: 17405-12. PMID 11278347 DOI: 10.1074/Jbc.M007475200 |
0.396 |
|
| 2001 |
Estébanez-Perpiña E, Fuentes-Prior P, Belorgey D, Braun M, Kiefersauer R, Maskos K, Huber R, Rubin H, Bode W. Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue. Biological Chemistry. 381: 1203-14. PMID 11209755 DOI: 10.1515/Bc.2000.148 |
0.395 |
|
| 2001 |
Ullrich TC, Blaesse M, Huber R. Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation. The Embo Journal. 20: 316-29. PMID 11157739 DOI: 10.1093/Emboj/20.3.316 |
0.444 |
|
| 2001 |
Augustin MA, Huber R, Kaiser JT. Crystal structure of a DNA-dependent RNA polymerase (DNA primase). Nature Structural & Molecular Biology. 8: 57-61. PMID 11135672 DOI: 10.1038/83060 |
0.365 |
|
| 2001 |
Garbuglia M, Verzini M, Hofmann A, Huber R, Donato R. S100A1 and S100B interactions with annexins. Biochimica Et Biophysica Acta. 1498: 192-206. PMID 11108963 DOI: 10.1016/S0167-4889(00)00096-3 |
0.347 |
|
| 2001 |
Blaesse M, Kupke T, Huber R, Steinbacher S. Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate. The Embo Journal. 19: 6299-310. PMID 11101502 DOI: 10.1093/Emboj/19.23.6299 |
0.431 |
|
| 2001 |
Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A. Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proceedings of the National Academy of Sciences of the United States of America. 97: 13567-72. PMID 11087827 DOI: 10.1073/Pnas.240463497 |
0.378 |
|
| 2001 |
Dorowski A, Hofmann A, Steegborn C, Boicu M, Huber R. Crystal structure of paprika ferredoxin-NADP+ reductase. Implications for the electron transfer pathway. The Journal of Biological Chemistry. 276: 9253-63. PMID 11053431 DOI: 10.1074/jbc.M004576200 |
0.359 |
|
| 2001 |
Einsle O, Stach P, Messerschmidt A, Simon J, Kröger A, Huber R, Kroneck PM. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs. The Journal of Biological Chemistry. 275: 39608-16. PMID 10984487 DOI: 10.1074/Jbc.M006188200 |
0.731 |
|
| 2000 |
Soulimane T, Than ME, Dewor M, Huber R, Buse G. Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus. Protein Science : a Publication of the Protein Society. 9: 2068-73. PMID 11152118 DOI: 10.1110/Ps.9.11.2068 |
0.4 |
|
| 2000 |
Song HK, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, Huber R. Mutational studies on HslU and its docking mode with HslV. Proceedings of the National Academy of Sciences of the United States of America. 97: 14103-8. PMID 11114186 DOI: 10.1073/Pnas.250491797 |
0.737 |
|
| 2000 |
Meyer O, Gremer L, Ferner R, Ferner M, Dobbek H, Gnida M, Meyer-Klaucke W, Huber R. The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase. Biological Chemistry. 381: 865-76. PMID 11076018 DOI: 10.1515/Bc.2000.108 |
0.404 |
|
| 2000 |
Groll M, Bajorek M, Köhler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D. A gated channel into the proteasome core particle Nature Structural Biology. 7: 1062-1067. PMID 11062564 DOI: 10.1038/80992 |
0.305 |
|
| 2000 |
Hänzelmann P, Dobbek H, Gremer L, Huber R, Meyer O. The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase. Journal of Molecular Biology. 301: 1221-35. PMID 10966817 DOI: 10.1006/Jmbi.2000.4023 |
0.411 |
|
| 2000 |
Deibert M, Grazulis S, Sasnauskas G, Siksnys V, Huber R. Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA. Nature Structural Biology. 7: 792-9. PMID 10966652 DOI: 10.1038/79032 |
0.362 |
|
| 2000 |
Garrido Franco M, Huber R, Schmidt FS, Laber B, Clausen T. Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzyme. Acta Crystallographica. Section D, Biological Crystallography. 56: 1045-8. PMID 10944349 DOI: 10.1107/S0907444900007368 |
0.667 |
|
| 2000 |
Minks C, Huber R, Moroder L, Budisa N. Noninvasive tracing of recombinant proteins with "fluorophenylalanine-fingers". Analytical Biochemistry. 284: 29-34. PMID 10933852 DOI: 10.1006/Abio.2000.4667 |
0.336 |
|
| 2000 |
Krupka HI, Huber R, Holt SC, Clausen T. Crystal structure of cystalysin from Treponema denticola: A pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme Embo Journal. 19: 3168-3178. PMID 10880431 DOI: 10.1093/Emboj/19.13.3168 |
0.698 |
|
| 2000 |
Hofmann A, Raguénès-Nicol C, Favier-Perron B, Mesonero J, Huber R, Russo-Marie F, Lewit-Bentley A. The annexin A3-membrane interaction is modulated by an N-terminal tryptophan. Biochemistry. 39: 7712-21. PMID 10869176 DOI: 10.1021/Bi992359+ |
0.358 |
|
| 2000 |
Sperl S, Jacob U, Arroyo de Prada N, Stürzebecher J, Wilhelm OG, Bode W, Magdolen V, Huber R, Moroder L. (4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase. Proceedings of the National Academy of Sciences of the United States of America. 97: 5113-8. PMID 10805774 DOI: 10.1073/Pnas.97.10.5113 |
0.427 |
|
| 2000 |
Wahl MC, Huber R, Marinkoviç S, Weyher-Stingl E, Ehlert S. Structural investigations of the highly flexible recombinant ribosomal protein L12 from Thermotoga maritima. Biological Chemistry. 381: 221-9. PMID 10782993 DOI: 10.1515/Bc.2000.029 |
0.334 |
|
| 2000 |
Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME. Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus. The Embo Journal. 19: 1766-76. PMID 10775261 DOI: 10.1093/Emboj/19.8.1766 |
0.383 |
|
| 2000 |
Rester U, Moser M, Huber R, Bode W. L-Isoaspartate 115 of porcine beta-trypsin promotes crystallization of its complex with bdellastasin. Acta Crystallographica. Section D, Biological Crystallography. 56: 581-8. PMID 10771427 DOI: 10.1107/S0907444900003048 |
0.303 |
|
| 2000 |
Fuentes-Prior P, Iwanaga Y, Huber R, Pagila R, Rumennik G, Seto M, Morser J, Light DR, Bode W. Structural basis for the anticoagulant activity of the thrombin–thrombomodulin complex Nature. 404: 518-525. PMID 10761923 DOI: 10.1038/35006683 |
0.418 |
|
| 2000 |
Clausen T, Kaiser JT, Steegborn C, Huber R, Kessler D. Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 97: 3856-61. PMID 10760256 DOI: 10.1073/Pnas.97.8.3856 |
0.624 |
|
| 2000 |
Reverter D, Fernández-Catalán C, Baumgartner R, Pfänder R, Huber R, Bode W, Vendrell J, Holak TA, Avilés FX. Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. Nature Structural Biology. 7: 322-8. PMID 10742178 DOI: 10.1038/74092 |
0.625 |
|
| 2000 |
Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R, Jaenicke R. The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability Journal of Molecular Biology. 297: 659-672. PMID 10731419 DOI: 10.1006/Jmbi.2000.3570 |
0.453 |
|
| 2000 |
Theodoratou E, Paschos A, Magalon A, Fritsche E, Huber R, Böck A. Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation. European Journal of Biochemistry. 267: 1995-9. PMID 10727938 DOI: 10.1046/J.1432-1327.2000.01202.X |
0.42 |
|
| 2000 |
Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R. Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. Journal of Molecular Biology. 297: 451-64. PMID 10715213 DOI: 10.1006/Jmbi.2000.3581 |
0.708 |
|
| 2000 |
Hofmann A, Proust J, Dorowski A, Schantz R, Huber R. Annexin 24 from Capsicum annuum. X-ray structure and biochemical characterization. The Journal of Biological Chemistry. 275: 8072-82. PMID 10713128 DOI: 10.1074/jbc.275.11.8072 |
0.321 |
|
| 2000 |
Bode W, Huber R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochimica Et Biophysica Acta. 1477: 241-52. PMID 10708861 DOI: 10.1016/S0167-4838(99)00276-9 |
0.418 |
|
| 2000 |
Rebelo J, Macieira S, Dias JM, Huber R, Ascenso CS, Rusnak F, Moura JJ, Moura I, Romão MJ. Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774. Journal of Molecular Biology. 297: 135-46. PMID 10704312 DOI: 10.1006/Jmbi.2000.3552 |
0.437 |
|
| 2000 |
Worbs M, Huber R, Wahl MC. Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon. The Embo Journal. 19: 807-18. PMID 10698923 DOI: 10.1093/Emboj/19.5.807 |
0.385 |
|
| 2000 |
Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature. 403: 800-5. PMID 10693812 DOI: 10.1038/35001629 |
0.726 |
|
| 2000 |
Loidl G, Musiol HJ, Groll M, Huber R, Moroder L. Synthesis of bivalent inhibitors of eucaryotic proteasomes. Journal of Peptide Science : An Official Publication of the European Peptide Society. 6: 36-46. PMID 10674718 DOI: 10.1002/(Sici)1099-1387(200001)6:1<36::Aid-Psc232>3.0.Co;2-2 |
0.365 |
|
| 2000 |
Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proceedings of the National Academy of Sciences of the United States of America. 97: 588-92. PMID 10639123 DOI: 10.1073/Pnas.97.2.588 |
0.366 |
|
| 2000 |
Wahl MC, Bourenkov GP, Bartunik HD, Huber R. Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12. The Embo Journal. 19: 174-86. PMID 10637222 DOI: 10.1093/Emboj/19.2.174 |
0.394 |
|
| 2000 |
Groll M, Kim KB, Kairies N, Huber R, Crews CM. Crystal Structure of Epoxomicin:20S Proteasome reveals a molecular basis for selectivity of alpha,beta-Epoxyketone Proteasome Inhibitors Journal of the American Chemical Society. 122: 1237-1238. DOI: 10.2210/Pdb1G65/Pdb |
0.353 |
|
| 2000 |
Kiefersauer R, Than ME, Dobbek H, Gremer L, Melero M, Strobl S, Dias JM, Soulimane T, Huber R. A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes Journal of Applied Crystallography. 33: 1223-1230. DOI: 10.1107/S010876730002907X |
0.322 |
|
| 1999 |
Macedo-Ribeiro S, Bode W, Huber R, Quinn-Allen MA, Kim SW, Ortel TL, Bourenkov GP, Bartunik HD, Stubbs MT, Kane WH, Fuentes-Prior P. Crystal structures of the membrane-binding C2 domain of human coagulation factor V. Nature. 402: 434-9. PMID 10586886 DOI: 10.1038/46594 |
0.388 |
|
| 1999 |
Deibert M, Grazulis S, Janulaitis A, Siksnys V, Huber R. Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 A resolution. The Embo Journal. 18: 5805-16. PMID 10545092 DOI: 10.1093/Emboj/18.21.5805 |
0.365 |
|
| 1999 |
Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R. Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity. Journal of Molecular Biology. 293: 693-701. PMID 10543960 DOI: 10.1006/Jmbi.1999.3165 |
0.354 |
|
| 1999 |
Eichinger A, Beisel HG, Jacob U, Huber R, Medrano FJ, Banbula A, Potempa J, Travis J, Bode W. Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. The Embo Journal. 18: 5453-62. PMID 10523290 DOI: 10.1093/Emboj/18.20.5453 |
0.441 |
|
| 1999 |
Siksnys V, Skirgaila R, Sasnauskas G, Urbanke C, Cherny D, Grazulis S, Huber R. The Cfr10I restriction enzyme is functional as a tetramer. Journal of Molecular Biology. 291: 1105-18. PMID 10518946 DOI: 10.1006/Jmbi.1999.2977 |
0.41 |
|
| 1999 |
Rester U, Bode W, Moser M, Parry MA, Huber R, Auerswald E. Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmin system. Journal of Molecular Biology. 293: 93-106. PMID 10512718 DOI: 10.1006/Jmbi.1999.3162 |
0.442 |
|
| 1999 |
Groll M, Heinemeyer W, Jäger S, Ullrich T, Bochtler M, Wolf DH, Huber R. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proceedings of the National Academy of Sciences of the United States of America. 96: 10976-83. PMID 10500111 DOI: 10.1073/Pnas.96.20.10976 |
0.602 |
|
| 1999 |
Hopfner KP, Lang A, Karcher A, Sichler K, Kopetzki E, Brandstetter H, Huber R, Bode W, Engh RA. Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding. Structure (London, England : 1993). 7: 989-96. PMID 10467148 DOI: 10.1016/S0969-2126(99)80125-7 |
0.41 |
|
| 1999 |
Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM. Structure of cytochrome c nitrite reductase. Nature. 400: 476-80. PMID 10440380 DOI: 10.1038/22802 |
0.745 |
|
| 1999 |
Schnackenberg J, Than ME, Mann K, Wiegand G, Huber R, Reuter W. Amino acid sequence, crystallization and structure determination of reduced and oxidized cytochrome c6 from the green alga Scenedesmus obliquus. Journal of Molecular Biology. 290: 1019-30. PMID 10438600 DOI: 10.1006/Jmbi.1999.2944 |
0.391 |
|
| 1999 |
Steegborn C, Messerschmidt A, Laber B, Streber W, Huber R, Clausen T. The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity. Journal of Molecular Biology. 290: 983-96. PMID 10438597 DOI: 10.1006/jmbi.1999.2935 |
0.653 |
|
| 1999 |
Dobbek H, Gremer L, Meyer O, Huber R. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proceedings of the National Academy of Sciences of the United States of America. 96: 8884-9. PMID 10430865 DOI: 10.1073/Pnas.96.16.8884 |
0.381 |
|
| 1999 |
Bochtler M, Ditzel L, Groll M, Hartmann C, Huber R. The proteasome. Annual Review of Biophysics and Biomolecular Structure. 28: 295-317. PMID 10410804 DOI: 10.1146/annurev.biophys.28.1.295 |
0.675 |
|
| 1999 |
Ploom T, Haussmann C, Hof P, Steinbacher S, Bacher A, Richardson J, Huber R. Crystal structure of 7,8-dihydroneopterin triphosphate epimerase. Structure (London, England : 1993). 7: 509-16. PMID 10378270 DOI: 10.1016/S0969-2126(99)80067-7 |
0.34 |
|
| 1999 |
Dias JM, Than ME, Humm A, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Calvete J, Caldeira J, Carneiro C, Moura JJ, Moura I, Romão MJ. Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods. Structure (London, England : 1993). 7: 65-79. PMID 10368307 DOI: 10.1016/S0969-2126(99)80010-0 |
0.397 |
|
| 1999 |
Bracher A, Fischer M, Eisenreich W, Ritz H, Schramek N, Boyle P, Gentili P, Huber R, Nar H, Auerbach G, Bacher A. Histidine 179 mutants of GTP cyclohydrolase I catalyze the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate. The Journal of Biological Chemistry. 274: 16727-35. PMID 10358012 DOI: 10.1074/Jbc.274.24.16727 |
0.344 |
|
| 1999 |
Steinbacher S, Hof P, Eichinger L, Schleicher M, Gettemans J, Vandekerckhove J, Huber R, Benz J. The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain. The Embo Journal. 18: 2923-9. PMID 10357805 DOI: 10.1093/Emboj/18.11.2923 |
0.382 |
|
| 1999 |
Fritsche E, Paschos A, Beisel HG, Böck A, Huber R. Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli. Journal of Molecular Biology. 288: 989-98. PMID 10331925 DOI: 10.1006/Jmbi.1999.2719 |
0.445 |
|
| 1999 |
Loidl G, Groll M, Musiol HJ, Huber R, Moroder L. Bivalency as a principle for proteasome inhibition. Proceedings of the National Academy of Sciences of the United States of America. 96: 5418-22. PMID 10318898 DOI: 10.1073/Pnas.96.10.5418 |
0.401 |
|
| 1999 |
Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W. Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. The Embo Journal. 18: 2313-22. PMID 10228146 DOI: 10.1093/Emboj/18.9.2313 |
0.381 |
|
| 1999 |
Steegborn C, Clausen T, Sondermann P, Jacob U, Worbs M, Marinkovic S, Huber R, Wahl MC. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration. The Journal of Biological Chemistry. 274: 12675-84. PMID 10212249 DOI: 10.1074/jbc.274.18.12675 |
0.592 |
|
| 1999 |
Pereira PJ, Wang ZM, Rubin H, Huber R, Bode W, Schechter NM, Strobl S. The 2.2 A Crystal Structure of Human Chymase in Complex with Succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural Explanation for its Dipeptidyl Carboxypeptidase Specificity. Journal of Molecular Biology. 286: 817. PMID 10208809 DOI: 10.1006/Jmbi.1999.2691 |
0.449 |
|
| 1999 |
Loidl G, Groll M, Musiol HJ, Ditzel L, Huber R, Moroder L. Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes. Chemistry & Biology. 6: 197-204. PMID 10099130 DOI: 10.1016/S1074-5521(99)80036-2 |
0.336 |
|
| 1999 |
Hopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B. Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius. Proceedings of the National Academy of Sciences of the United States of America. 96: 3600-5. PMID 10097083 DOI: 10.1073/Pnas.96.7.3600 |
0.352 |
|
| 1999 |
Ploom T, Thöny B, Yim J, Lee S, Nar H, Leimbacher W, Richardson J, Huber R, Auerbach G. Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase. Journal of Molecular Biology. 286: 851-60. PMID 10024455 DOI: 10.1006/Jmbi.1998.2511 |
0.38 |
|
| 1999 |
Reuter W, Wiegand G, Huber R, Than ME. Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus. Proceedings of the National Academy of Sciences of the United States of America. 96: 1363-8. PMID 9990029 DOI: 10.1073/Pnas.96.4.1363 |
0.402 |
|
| 1999 |
Renatus M, Bode W, Huber R, Stürzebecher J, Stubbs MT. Structural and functional analyses of benzamidine-based inhibitors in complex with trypsin: implications for the inhibition of factor Xa, tPA, and urokinase. Journal of Medicinal Chemistry. 41: 5445-56. PMID 9876114 DOI: 10.1021/Jm981068G |
0.385 |
|
| 1999 |
Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A. Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution. The Embo Journal. 17: 6827-38. PMID 9843488 DOI: 10.1093/emboj/17.23.6827 |
0.684 |
|
| 1999 |
Prade L, Huber R, Bieseler B. Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants. Structure (London, England : 1993). 6: 1445-52. PMID 9817846 DOI: 10.1016/S0969-2126(98)00143-9 |
0.317 |
|
| 1998 |
Fritsche E, Bergner A, Humm A, Piepersberg W, Huber R. Crystal structure of L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis. Biochemistry. 37: 17664-72. PMID 9922132 DOI: 10.1021/Bi981949P |
0.468 |
|
| 1998 |
Parry MA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Gührs KH, Bode W. The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action. Nature Structural Biology. 5: 917-23. PMID 9783753 DOI: 10.1038/2359 |
0.414 |
|
| 1998 |
Parry MA, Jacob U, Huber R, Wisner A, Bon C, Bode W. The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases. Structure (London, England : 1993). 6: 1195-206. PMID 9753698 DOI: 10.1016/S0969-2126(98)00119-1 |
0.405 |
|
| 1998 |
Banbula A, Potempa J, Travis J, Fernandez-Catalán C, Mann K, Huber R, Bode W, Medrano F. Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution. Structure (London, England : 1993). 6: 1185-93. PMID 9753696 DOI: 10.1016/S0969-2126(98)00118-X |
0.434 |
|
| 1998 |
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K. Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. The Embo Journal. 17: 5238-48. PMID 9724659 DOI: 10.1093/Emboj/17.17.5238 |
0.301 |
|
| 1998 |
Hopfner KP, Kopetzki E, Kresse GB, Bode W, Huber R, Engh RA. New enzyme lineages by subdomain shuffling. Proceedings of the National Academy of Sciences of the United States of America. 95: 9813-8. PMID 9707558 DOI: 10.1073/Pnas.95.17.9813 |
0.422 |
|
| 1998 |
Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F. Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data. Protein Science : a Publication of the Protein Society. 7: 1303-9. PMID 9655333 DOI: 10.1002/Pro.5560070605 |
0.384 |
|
| 1998 |
Ditzel L, Huber R, Mann K, Heinemeyer W, Wolf DH, Groll M. Conformational constraints for protein self-cleavage in the proteasome Journal of Molecular Biology. 279: 1187-1191. PMID 9642094 DOI: 10.1006/Jmbi.1998.1818 |
0.448 |
|
| 1998 |
Skirgaila R, Grazulis S, Bozic D, Huber R, Siksnys V. Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues. Journal of Molecular Biology. 279: 473-81. PMID 9642051 DOI: 10.1006/Jmbi.1998.1803 |
0.397 |
|
| 1998 |
Budisa N, Huber R, Golbik R, Minks C, Weyher E, Moroder L. Atomic mutations in annexin V--thermodynamic studies of isomorphous protein variants. European Journal of Biochemistry. 253: 1-9. PMID 9578454 DOI: 10.1046/J.1432-1327.1998.2530001.X |
0.315 |
|
| 1998 |
Glatigny A, Hof P, Romão MJ, Huber R, Scazzocchio C. Altered specificity mutations define residues essential for substrate positioning in xanthine dehydrogenase. Journal of Molecular Biology. 278: 431-8. PMID 9571062 DOI: 10.1006/Jmbi.1998.1707 |
0.348 |
|
| 1998 |
Ditzel L, Löwe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 93: 125-38. PMID 9546398 DOI: 10.1016/S0092-8674(00)81152-6 |
0.66 |
|
| 1998 |
Becker M, Stubbs MT, Huber R. Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives. Protein Science : a Publication of the Protein Society. 7: 580-6. PMID 9541389 DOI: 10.1002/Pro.5560070306 |
0.342 |
|
| 1998 |
Messerschmidt A, Prade L, Kroes SJ, Sanders-Loehr J, Huber R, Canters GW. Rack-induced metal binding vs. flexibility: Met121His azurin crystal structures at different pH. Proceedings of the National Academy of Sciences of the United States of America. 95: 3443-8. PMID 9520385 DOI: 10.1073/Pnas.95.7.3443 |
0.37 |
|
| 1998 |
Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, Reddy P, Wolfson MF, Rauch CT, Castner BJ, Davis R, Clarke HR, Petersen M, Fitzner JN, Cerretti DP, et al. Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proceedings of the National Academy of Sciences of the United States of America. 95: 3408-12. PMID 9520379 DOI: 10.1073/pnas.95.7.3408 |
0.306 |
|
| 1998 |
Molitor M, Dahl C, Molitor I, Schäfer U, Speich N, Huber R, Deutzmann R, Trüper HG. A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum. Microbiology (Reading, England). 529-41. PMID 9493389 DOI: 10.1099/00221287-144-2-529 |
0.351 |
|
| 1998 |
Gomis-Rüth FX, Gómez-Ortiz M, Vendrell J, Ventura S, Bode W, Huber R, Avilés FX. Cutting at the right place--the importance of selective limited proteolysis in the activation of proproteinase E. European Journal of Biochemistry. 251: 839-44. PMID 9490059 DOI: 10.1046/j.1432-1327.1998.2510839.x |
0.591 |
|
| 1998 |
Hofmann A, Escherich A, Lewit-Bentley A, Benz J, Raguenes-Nicol C, Russo-Marie F, Gerke V, Moroder L, Huber R. Interactions of benzodiazepine derivatives with annexins. The Journal of Biological Chemistry. 273: 2885-94. PMID 9446599 DOI: 10.1074/Jbc.273.5.2885 |
0.376 |
|
| 1998 |
Blickling S, Beisel HG, Bozic D, Knäblein J, Laber B, Huber R. Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure. Journal of Molecular Biology. 274: 608-21. PMID 9417939 DOI: 10.1006/Jmbi.1997.1393 |
0.423 |
|
| 1998 |
Neuefeind T, Huber R, Reinemer P, Knäblein J, Prade L, Mann K, Bieseler B. Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides. Journal of Molecular Biology. 274: 577-87. PMID 9417936 DOI: 10.1006/Jmbi.1997.1401 |
0.419 |
|
| 1998 |
Neuefeind T, Huber R, Dasenbrock H, Prade L, Bieseler B. Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism. Journal of Molecular Biology. 274: 446-53. PMID 9417926 DOI: 10.1006/Jmbi.1997.1402 |
0.457 |
|
| 1998 |
Auerbach G, Herrmann A, Gütlich M, Fischer M, Jacob U, Bacher A, Huber R. The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. The Embo Journal. 16: 7219-30. PMID 9405351 DOI: 10.1093/Emboj/16.24.7219 |
0.461 |
|
| 1998 |
Romão MJ, Huber R. Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas. Biochemical Society Transactions. 25: 755-7. PMID 9388539 DOI: 10.1042/Bst0250755 |
0.364 |
|
| 1998 |
Hopfner KP, Brandstetter H, Karcher A, Kopetzki E, Huber R, Engh RA, Bode W. Converting blood coagulation factor IXa into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants. The Embo Journal. 16: 6626-35. PMID 9362477 DOI: 10.1093/Emboj/16.22.6626 |
0.403 |
|
| 1998 |
Voityuk AA, Albert K, Romão MJ, Huber R, Rösch N. Substrate Oxidation in the Active Site of Xanthine Oxidase and Related Enzymes. A Model Density Functional Study Inorganic Chemistry. 37: 176-180. DOI: 10.1021/Ic9707570 |
0.317 |
|
| 1997 |
Romão MJ, Knäblein J, Huber R, Moura JJG. Structure and function of molybdopterin containing enzymes. Progress in Biophysics & Molecular Biology. 68: 121-144. PMID 9652170 DOI: 10.1016/S0079-6107(97)00022-9 |
0.407 |
|
| 1997 |
Auerbach G, Huber R, Grättinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure (London, England : 1993). 5: 1475-83. PMID 9384563 DOI: 10.1016/S0969-2126(97)00297-9 |
0.424 |
|
| 1997 |
Escherich A, Ditzel L, Musiol HJ, Groll M, Huber R, Moroder L. Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae. Biological Chemistry. 378: 893-8. PMID 9377486 DOI: 10.1515/Bchm.1997.378.8.893 |
0.304 |
|
| 1997 |
Clausen T, Huber R, Messerschmidt A, Pohlenz HD, Laber B. Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study. Biochemistry. 36: 12633-43. PMID 9376370 DOI: 10.1021/bi970630m |
0.642 |
|
| 1997 |
Renatus M, Stubbs MT, Huber R, Bringmann P, Donner P, Schleuning WD, Bode W. Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage. Biochemistry. 36: 13483-93. PMID 9354616 DOI: 10.1021/Bi971129X |
0.422 |
|
| 1997 |
Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W. Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor. Structure (London, England : 1993). 5: 1287-95. PMID 9351803 DOI: 10.1016/S0969-2126(97)00281-5 |
0.41 |
|
| 1997 |
Fuentes-Prior P, Noeske-Jungblut C, Donner P, Schleuning WD, Huber R, Bode W. Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proceedings of the National Academy of Sciences of the United States of America. 94: 11845-50. PMID 9342325 DOI: 10.1073/pnas.94.22.11845 |
0.349 |
|
| 1997 |
Wahl MC, Huber R, Prade L, Marinkovic S, Messerschmidt A, Clausen T. Cloning, purification, crystallization, and preliminary X-ray diffraction analysis of cystathionine gamma-synthase from E. coli. Febs Letters. 414: 492-6. PMID 9323022 DOI: 10.1016/S0014-5793(97)01057-0 |
0.614 |
|
| 1997 |
Renatus M, Engh RA, Stubbs MT, Huber R, Fischer S, Kohnert U, Bode W. Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA. The Embo Journal. 16: 4797-805. PMID 9305622 DOI: 10.1093/Emboj/16.16.4797 |
0.399 |
|
| 1997 |
Than ME, Hof P, Huber R, Bourenkov GP, Bartunik HD, Buse G, Soulimane T. Thermus thermophilus cytochrome-c552: A new highly thermostable cytochrome-c structure obtained by MAD phasing. Journal of Molecular Biology. 271: 629-44. PMID 9281430 DOI: 10.1006/Jmbi.1997.1181 |
0.39 |
|
| 1997 |
Renatus M, Bode W, Huber R, Stürzebecher J, Prasa D, Fischer S, Kohnert U, Stubbs MT. Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors. The Journal of Biological Chemistry. 272: 21713-9. PMID 9268299 DOI: 10.1074/Jbc.272.35.21713 |
0.428 |
|
| 1997 |
Fritsche E, Humm A, Huber R. Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study. European Journal of Biochemistry. 247: 483-90. PMID 9266688 DOI: 10.1111/J.1432-1033.1997.00483.X |
0.416 |
|
| 1997 |
Budisa N, Karnbrock W, Steinbacher S, Humm A, Prade L, Neuefeind T, Moroder L, Huber R. Bioincorporation of telluromethionine into proteins: a promising new approach for X-ray structure analysis of proteins. Journal of Molecular Biology. 270: 616-23. PMID 9245591 DOI: 10.1006/Jmbi.1997.1132 |
0.366 |
|
| 1997 |
Stubbs MT, Morenweiser R, Stürzebecher J, Bauer M, Bode W, Huber R, Piechottka GP, Matschiner G, Sommerhoff CP, Fritz H, Auerswald EA. The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition. The Journal of Biological Chemistry. 272: 19931-7. PMID 9242660 DOI: 10.1074/Jbc.272.32.19931 |
0.432 |
|
| 1997 |
Avaeva S, Kurilova S, Nazarova T, Rodina E, Vorobyeva N, Sklyankina V, Grigorjeva O, Harutyunyan E, Oganessyan V, Wilson K, Dauter Z, Huber R, Mather T. Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4(2-). Ligand-induced molecular asymmetry. Febs Letters. 410: 502-8. PMID 9237692 DOI: 10.1016/S0014-5793(97)00650-9 |
0.441 |
|
| 1997 |
Liemann S, Bringemeier I, Benz J, Göttig P, Hofmann A, Huber R, Noegel AA, Jacob U. Crystal structure of the C-terminal tetrad repeat from synexin (annexin VII) of Dictyostelium discoideum. Journal of Molecular Biology. 270: 79-88. PMID 9231902 DOI: 10.1006/Jmbi.1997.1091 |
0.408 |
|
| 1997 |
Liemann S, Huber R. Three-dimensional structure of annexins. Cellular and Molecular Life Sciences. 53: 516-521. PMID 9230929 DOI: 10.1007/S000180050065 |
0.394 |
|
| 1997 |
Gomis-Rüth FX, Gómez-Ortiz M, Vendrell J, Ventura S, Bode W, Huber R, Avilés FX. Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation. Journal of Molecular Biology. 269: 861-80. PMID 9223647 DOI: 10.1006/Jmbi.1997.1040 |
0.655 |
|
| 1997 |
Humm A, Fritsche E, Steinbacher S, Huber R. Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. The Embo Journal. 16: 3373-85. PMID 9218780 DOI: 10.1093/Emboj/16.12.3373 |
0.456 |
|
| 1997 |
van de Locht A, Bode W, Huber R, Le Bonniec BF, Stone SR, Esmon CT, Stubbs MT. The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. The Embo Journal. 16: 2977-84. PMID 9214615 DOI: 10.1093/Emboj/16.11.2977 |
0.448 |
|
| 1997 |
Harutyunyan EH, Oganessyan VY, Oganessyan NN, Avaeva SM, Nazarova TI, Vorobyeva NN, Kurilova SA, Huber R, Mather T. Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis. Biochemistry. 36: 7754-60. PMID 9201917 DOI: 10.1021/Bi962637U |
0.386 |
|
| 1997 |
Bochtler M, Ditzel L, Groll M, Huber R. Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 94: 6070-4. PMID 9177170 DOI: 10.1073/Pnas.94.12.6070 |
0.671 |
|
| 1997 |
Humm A, Fritsche E, Mann K, Göhl M, Huber R. Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue. The Biochemical Journal. 771-6. PMID 9148748 DOI: 10.1042/Bj3220771 |
0.367 |
|
| 1997 |
Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage. Journal of Molecular Biology. 267: 865-80. PMID 9135118 DOI: 10.1006/Jmbi.1997.0922 |
0.307 |
|
| 1997 |
Groll M, Ditzel L, Löwe J, Stock D, Bochtler M, Bartunik HD, Huber R. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature. 386: 463-71. PMID 9087403 DOI: 10.1038/386463A0 |
0.726 |
|
| 1997 |
Jacob U, Mack M, Clausen T, Huber R, Buckel W, Messerschmidt A. Glutaconate CoA-transferase from Acidaminococcus fermentans: The crystal structure reveals homology with other CoA-transferases Structure. 5: 415-426. PMID 9083111 DOI: 10.1016/S0969-2126(97)00198-6 |
0.673 |
|
| 1997 |
Hammann C, Van Pouderoyen G, Nar H, Rüth FXG, Messerschmidt A, Huber R, Den Blaauwen T, Canters GW. Crystal structures of modified Apo-His117Gly and Apo-His46Gly mutants of Pseudomonas aeruginosa azurin Journal of Molecular Biology. 266: 357-366. PMID 9047369 DOI: 10.1006/Jmbi.1996.0764 |
0.419 |
|
| 1997 |
Gomez-Ortiz M, Gomis-Rüth FX, Huber R, Avilés FX. Inhibition of carboxypeptidase A by excess zinc: analysis of the structural determinants by X-ray crystallography. Febs Letters. 400: 336-40. PMID 9009226 DOI: 10.1016/S0014-5793(96)01412-3 |
0.572 |
|
| 1997 |
Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry. 36: 24-33. PMID 8993314 DOI: 10.1021/Bi962272D |
0.381 |
|
| 1997 |
Macedo-Ribeiro S, Darimont B, Sterner R, Huber R. Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima. Structure (London, England : 1993). 4: 1291-301. PMID 8939753 DOI: 10.1016/S0969-2126(96)00137-2 |
0.366 |
|
| 1997 |
Baxa U, Steinbacher S, Miller S, Weintraub A, Huber R, Seckler R. Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide. Biophysical Journal. 71: 2040-8. PMID 8889178 DOI: 10.1016/S0006-3495(96)79402-X |
0.308 |
|
| 1997 |
Stock D, Ditzel L, Baumeister W, Huber R, Löwe J. Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography. Cold Spring Harbor Symposia On Quantitative Biology. 60: 525-32. PMID 8824425 DOI: 10.1101/Sqb.1995.060.01.056 |
0.57 |
|
| 1997 |
Bozic D, Grazulis S, Siksnys V, Huber R. Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 A resolution. Journal of Molecular Biology. 255: 176-186. DOI: 10.2210/Pdb1Cfr/Pdb |
0.432 |
|
| 1997 |
Romão MJ, Rösch N, Huber R. The molybdenum site in the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas and a catalytic mechanism for this class of enzymes Jbic Journal of Biological Inorganic Chemistry. 2: 782-785. DOI: 10.1007/S007750050195 |
0.367 |
|
| 1996 |
Engh RA, Brandstetter H, Sucher G, Eichinger A, Baumann U, Bode W, Huber R, Poll T, Rudolph R, Von Der Saal W. Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: Implications for drug design Structure. 4: 1353-1362. PMID 8939759 DOI: 10.1016/S0969-2126(96)00142-6 |
0.375 |
|
| 1996 |
Zajc A, Romão MJ, Turk B, Huber R. Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. Journal of Molecular Biology. 263: 269-83. PMID 8913306 DOI: 10.1006/Jmbi.1996.0574 |
0.412 |
|
| 1996 |
Schneider F, Löwe J, Huber R, Schindelin H, Kisker C, Knäblein J. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution Journal of Molecular Biology. 263: 53-69. PMID 8890912 DOI: 10.1006/Jmbi.1996.0555 |
0.614 |
|
| 1996 |
Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proceedings of the National Academy of Sciences of the United States of America. 93: 10584-8. PMID 8855221 DOI: 10.1073/Pnas.93.20.10584 |
0.364 |
|
| 1996 |
Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. Journal of Molecular Biology. 262: 202-24. PMID 8831789 DOI: 10.1006/jmbi.1996.0508 |
0.649 |
|
| 1996 |
Huber R, Hof P, Duarte RO, Moura JJ, Moura I, Liu MY, LeGall J, Hille R, Archer M, Romão MJ. A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes. Proceedings of the National Academy of Sciences of the United States of America. 93: 8846-51. PMID 8799115 DOI: 10.1073/Pnas.93.17.8846 |
0.372 |
|
| 1996 |
Stock D, Nederlof PM, Seemüller E, Baumeister W, Huber R, Löwe J. Proteasome: from structure to function. Current Opinion in Biotechnology. 7: 376-85. PMID 8768894 DOI: 10.1016/S0958-1669(96)80111-X |
0.645 |
|
| 1996 |
Benz J, Bergner A, Hofmann A, Demange P, Göttig P, Liemann S, Huber R, Voges D. The structure of recombinant human annexin VI in crystals and membrane-bound. Journal of Molecular Biology. 260: 638-43. PMID 8709144 DOI: 10.1006/Jmbi.1996.0426 |
0.376 |
|
| 1996 |
Liemann S, Benz J, Burger A, Voges D, Hofmann A, Huber R, Göttig P. Structural and functional characterisation of the voltage sensor in the ion channel human annexin V. Journal of Molecular Biology. 258: 555-61. PMID 8636991 DOI: 10.1006/Jmbi.1996.0268 |
0.345 |
|
| 1996 |
Burger A, Berendes R, Liemann S, Benz J, Hofmann A, Göttig P, Huber R, Gerke V, Thiel C, Römisch J, Weber K. The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein. Journal of Molecular Biology. 257: 839-47. PMID 8636985 DOI: 10.1006/Jmbi.1996.0205 |
0.395 |
|
| 1996 |
Lamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W. The 2.3 Å Crystal Structure of the Catalytic Domain of Recombinant Two-chain Human Tissue-type Plasminogen Activator Journal of Molecular Biology. 258: 117-135. PMID 8613982 DOI: 10.1006/Jmbi.1996.0238 |
0.431 |
|
| 1996 |
Engh RA, Huber R, Bode W, Schulze AJ. Divining the serpin inhibition mechanism: a suicide substrate 'springe'? Trends in Biotechnology. 13: 503-10. PMID 8595135 DOI: 10.1016/S0167-7799(00)89013-7 |
0.358 |
|
| 1996 |
Reinemer P, Prade L, Hof P, Neuefeind T, Huber R, Zettl R, Palme K, Schell J, Koelln I, Bartunik HD, Bieseler B. Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. Journal of Molecular Biology. 255: 289-309. PMID 8551521 DOI: 10.1006/jmbi.1996.0024 |
0.312 |
|
| 1996 |
Romão MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R. Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science (New York, N.Y.). 270: 1170-6. PMID 7502041 DOI: 10.1126/Science.270.5239.1170 |
0.434 |
|
| 1996 |
Stubbs MT, Huber R, Bode W. Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin. Febs Letters. 375: 103-7. PMID 7498454 DOI: 10.1016/0014-5793(95)01190-P |
0.393 |
|
| 1996 |
Oppliger T, Thöny B, Nar H, Bürgisser D, Huber R, Heizmann CW, Blau N. Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity. The Journal of Biological Chemistry. 270: 29498-506. PMID 7493990 DOI: 10.1074/Jbc.270.49.29498 |
0.379 |
|
| 1996 |
Bode W, Lollar P, Bauer M, Huber R, Brandstetter H. Crystal Structure of the Antihaemophilic Clotting Factor IXa Japanese Journal of Thrombosis and Hemostasis. 7: 165-175. DOI: 10.2491/Jjsth.7.165 |
0.454 |
|
| 1996 |
Kiefersauer R, Stetefeld J, Gomis-Rüth FX, Romão MJ, Lottspeich F, Huber R. Protein-Crystal Density by Volume Measurement and Amino-Acid Analysis Journal of Applied Crystallography. 29: 311-317. DOI: 10.1107/S0021889895014932 |
0.331 |
|
| 1996 |
Schmidtke G, Kraft R, Kostka S, Henklein P, Frömmel C, Löwe J, Huber R, Kloetzel PM, Schmidt M. Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis. The Embo Journal. 15: 6887-6898. DOI: 10.1002/J.1460-2075.1996.Tb01081.X |
0.572 |
|
| 1996 |
Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W. The 2.8 A crystal structure of Gla-domainless activated protein C. The Embo Journal. 15: 6822-6831. DOI: 10.1002/J.1460-2075.1996.Tb01073.X |
0.431 |
|
| 1996 |
van de Locht A, Stubbs MT, Bode W, Friedrich T, Bollschweiler C, Höffken W, Huber R. The ornithodorin-thrombin crystal structure, a key to the TAP enigma? The Embo Journal. 15: 6011-6017. DOI: 10.1002/J.1460-2075.1996.Tb00989.X |
0.457 |
|
| 1996 |
Hof P, Mayr I, Huber R, Korzus E, Potempa J, Travis J, Powers JC, Bode W. The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. The Embo Journal. 15: 5481-5491. DOI: 10.1002/J.1460-2075.1996.Tb00933.X |
0.364 |
|
| 1995 |
Nar H, Huber R, Auerbach G, Fischer M, Hösl C, Ritz H, Bracher A, Meining W, Eberhardt S, Bacher A. Active site topology and reaction mechanism of GTP cyclohydrolase I. Proceedings of the National Academy of Sciences of the United States of America. 92: 12120-5. PMID 8618856 DOI: 10.1073/Pnas.92.26.12120 |
0.411 |
|
| 1995 |
Wiegand G, Epp O, Huber R. The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat. Journal of Molecular Biology. 247: 99-110. PMID 7897663 DOI: 10.1006/jmbi.1994.0125 |
0.304 |
|
| 1995 |
Machius M, Wiegand G, Huber R. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. Journal of Molecular Biology. 246: 545-59. PMID 7877175 DOI: 10.1006/jmbi.1994.0106 |
0.303 |
|
| 1995 |
Korndörfer I, Steipe B, Huber R, Tomschy A, Jaenicke R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution. Journal of Molecular Biology. 246: 511-21. PMID 7877172 DOI: 10.1006/Jmbi.1994.0103 |
0.337 |
|
| 1995 |
Mirwaldt C, Korndörfer I, Huber R. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. Journal of Molecular Biology. 246: 227-39. PMID 7853400 DOI: 10.1006/Jmbi.1994.0078 |
0.427 |
|
| 1995 |
Beissinger M, Lee SC, Steinbacher S, Reinemer P, Huber R, Yu MH, Seckler R. Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context. Journal of Molecular Biology. 249: 185-94. PMID 7776371 DOI: 10.1006/Jmbi.1995.0288 |
0.339 |
|
| 1995 |
Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. European Journal of Biochemistry. 228: 830-41. PMID 7737183 DOI: 10.1111/j.1432-1033.1995.tb20329.x |
0.302 |
|
| 1995 |
Seemüller E, Lupas A, Stock D, Löwe J, Huber R, Baumeister W. Proteasome from Thermoplasma acidophilum: a threonine protease. Science (New York, N.Y.). 268: 579-82. PMID 7725107 DOI: 10.1126/Science.7725107 |
0.651 |
|
| 1995 |
Löwe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science (New York, N.Y.). 268: 533-9. PMID 7725097 DOI: 10.1126/Science.7725097 |
0.609 |
|
| 1995 |
Turk D, Podobnik M, Popovic T, Katunuma N, Bode W, Huber R, Turk V. Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors. Biochemistry. 34: 4791-7. PMID 7718586 DOI: 10.1021/Bi00014A037 |
0.379 |
|
| 1995 |
Archer M, Huber R, Tavares P, Moura I, Moura JJ, Carrondo MA, Sieker LC, LeGall J, Romão MJ. Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure. Journal of Molecular Biology. 251: 690-702. PMID 7666420 DOI: 10.1006/Jmbi.1995.0465 |
0.4 |
|
| 1995 |
Nar H, Huber R, Meining W, Schmid C, Weinkauf S, Bacher A. Atomic structure of GTP cyclohydrolase I. Structure (London, England : 1993). 3: 459-66. PMID 7663943 DOI: 10.1016/S0969-2126(01)00179-4 |
0.332 |
|
| 1995 |
Soulimane T, Gohlke U, Huber R, Buse G. Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 A resolution. Febs Letters. 368: 132-4. PMID 7615066 DOI: 10.1016/0014-5793(95)00623-H |
0.346 |
|
| 1995 |
Brandstetter H, Bauer M, Huber R, Lollar P, Bode W. X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. Proceedings of the National Academy of Sciences of the United States of America. 92: 9796-800. PMID 7568220 DOI: 10.1073/Pnas.92.21.9796 |
0.428 |
|
| 1995 |
Bürgisser DM, Thöny B, Redweik U, Hess D, Heizmann CW, Huber R, Nar H. 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding. Journal of Molecular Biology. 253: 358-69. PMID 7563095 DOI: 10.1006/Jmbi.1995.0558 |
0.403 |
|
| 1995 |
Budisa N, Steipe B, Demange P, Eckerskorn C, Kellermann J, Huber R. High‐level Biosynthetic Substitution of Methionine in Proteins by its Analogs 2‐Aminohexanoic Acid, Selenomethionine, Telluromethionine and Ethionine in Escherichia coli Febs Journal. 230: 788-796. DOI: 10.1111/J.1432-1033.1995.0788H.X |
0.358 |
|
| 1995 |
van de Locht A, Lamba D, Bauer M, Huber R, Friedrich T, Kröger B, Höffken W, Bode W. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. The Embo Journal. 14: 5149-5157. DOI: 10.1002/J.1460-2075.1995.Tb00199.X |
0.436 |
|
| 1995 |
Gomis-Rüth FX, Gómez M, Bode W, Huber R, Avilés FX. The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C. The Embo Journal. 14: 4387-4394. DOI: 10.1002/J.1460-2075.1995.Tb00117.X |
0.43 |
|
| 1994 |
Jap B, Pühler G, Lücke H, Typke D, Löwe J, Stock D, Huber R, Baumeister W. Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum. Journal of Molecular Biology. 234: 881-4. PMID 8254679 DOI: 10.1006/Jmbi.1993.1633 |
0.617 |
|
| 1994 |
Schulze AJ, Huber R, Bode W, Engh RA. Structural aspects of serpin inhibition. Febs Letters. 344: 117-24. PMID 8187869 DOI: 10.1016/0014-5793(94)00369-6 |
0.377 |
|
| 1994 |
Voges D, Berendes R, Burger A, Demange P, Baumeister W, Huber R. Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study. Journal of Molecular Biology. 238: 199-213. PMID 8158649 DOI: 10.1006/Jmbi.1994.1281 |
0.404 |
|
| 1994 |
Burger A, Voges D, Demange P, Perez CR, Huber R, Berendes R. Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter. Journal of Molecular Biology. 237: 479-99. PMID 8151707 DOI: 10.1006/Jmbi.1994.1249 |
0.308 |
|
| 1994 |
Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW. Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold Proceedings of the National Academy of Sciences of the United States of America. 91: 2473-2477. PMID 8146141 DOI: 10.1073/Pnas.91.7.2473 |
0.596 |
|
| 1994 |
Dirr H, Reinemer P, Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. European Journal of Biochemistry. 220: 645-61. PMID 8143720 DOI: 10.1111/J.1432-1033.1994.Tb18666.X |
0.45 |
|
| 1994 |
Hoppe E, Berne PF, Stock D, Rasmussen JS, Møller NP, Ullrich A, Huber R. Expression, purification and crystallization of human phosphotyrosine phosphatase 1B. European Journal of Biochemistry. 223: 1069-77. PMID 8055946 DOI: 10.1111/J.1432-1033.1994.Tb19085.X |
0.437 |
|
| 1994 |
Kungl AJ, Machius M, Huber R, Schwer C, Lam C, Aschauer H, Ehn G, Lindley IJ, Auer M. Purification, crystallization and preliminary X-ray diffraction analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-2). Febs Letters. 347: 300-3. PMID 8034022 DOI: 10.1016/0014-5793(94)00573-7 |
0.368 |
|
| 1994 |
Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science (New York, N.Y.). 265: 383-6. PMID 8023158 DOI: 10.1126/Science.8023158 |
0.413 |
|
| 1994 |
Gomis-Rüth FX, Kress LF, Kellermann J, Mayr I, Lee X, Huber R, Bode W. Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin. Journal of Molecular Biology. 239: 513-44. PMID 8006965 DOI: 10.1006/jmbi.1994.1392 |
0.347 |
|
| 1994 |
Dirr H, Reinemer P, Huber R. Refined crystal structure of porcine class Pi glutathione S-transferase (pGST P1-1) at 2.1 A resolution. Journal of Molecular Biology. 243: 72-92. PMID 7932743 DOI: 10.1006/Jmbi.1994.1631 |
0.484 |
|
| 1994 |
Schiffer CA, Huber R, Wüthrich K, van Gunsteren WF. Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals. Journal of Molecular Biology. 241: 588-99. PMID 7520085 DOI: 10.1006/Jmbi.1994.1533 |
0.35 |
|
| 1994 |
Bode W, Huber R. Proteinase — Protein inhibitor interactions Fibrinolysis and Proteolysis. 8: 161-171. DOI: 10.1016/0268-9499(94)90714-5 |
0.3 |
|
| 1994 |
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H. The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. The Embo Journal. 13: 1263-1269. DOI: 10.1002/J.1460-2075.1994.Tb06378.X |
0.45 |
|
| 1993 |
Bewley MC, Boustead CM, Walker JH, Waller DA, Huber R. Structure of chicken annexin V at 2.25-A resolution. Biochemistry. 32: 3923-9. PMID 8471604 DOI: 10.1021/Bi00066A011 |
0.377 |
|
| 1993 |
Weng X, Luecke H, Song IS, Kang DS, Kim SH, Huber R. Crystal structure of human annexin I at 2.5 A resolution. Protein Science : a Publication of the Protein Society. 2: 448-58. PMID 8453382 DOI: 10.1002/Pro.5560020317 |
0.439 |
|
| 1993 |
Gomis-Rüth FX, Stöcker W, Huber R, Zwilling R, Bode W. Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin. Journal of Molecular Biology. 229: 945-68. PMID 8445658 DOI: 10.1006/jmbi.1993.1098 |
0.357 |
|
| 1993 |
Lin G, Bode W, Huber R, Chi C, Engh RA. The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin. European Journal of Biochemistry. 212: 549-55. PMID 8444191 DOI: 10.1111/J.1432-1033.1993.Tb17692.X |
0.417 |
|
| 1993 |
Avilés FX, Vendrell J, Guasch A, Coll M, Huber R. Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and on the activation process. European Journal of Biochemistry. 211: 381-9. PMID 8436102 DOI: 10.1111/J.1432-1033.1993.Tb17561.X |
0.639 |
|
| 1993 |
Romero A, Hoitink CW, Nar H, Huber R, Messerschmidt A, Canters GW. X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin. Journal of Molecular Biology. 229: 1007-21. PMID 8383207 DOI: 10.1006/Jmbi.1993.1101 |
0.365 |
|
| 1993 |
Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W. Structure of human des(1-45) factor Xa at 2.2 A resolution. Journal of Molecular Biology. 232: 947-66. PMID 8355279 DOI: 10.1006/Jmbi.1993.1441 |
0.441 |
|
| 1993 |
Burger A, Berendes R, Voges D, Huber R, Demange P. A rapid and efficient purification method for recombinant annexin V for biophysical studies. Febs Letters. 329: 25-8. PMID 8354401 DOI: 10.1016/0014-5793(93)80185-W |
0.306 |
|
| 1993 |
Romão MJ, Barata BA, Archer M, Lobeck K, Moura I, Carrondo MA, LeGall J, Lottspeich F, Huber R, Moura JJ. Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers. European Journal of Biochemistry. 215: 729-32. PMID 8354279 DOI: 10.1111/J.1432-1033.1993.Tb18085.X |
0.358 |
|
| 1993 |
Xia C, Meyer DJ, Chen H, Reinemer P, Huber R, Ketterer B. Chemical modification of GSH transferase P1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site Biochemical Journal. 293: 357-362. PMID 8343115 DOI: 10.1042/Bj2930357 |
0.425 |
|
| 1993 |
Meyer DJ, Xia C, Coles B, Chen H, Reinemer P, Huber R, Ketterer B. Unusual reactivity of Tyr-7 of GSH transferase P1-1. The Biochemical Journal. 293: 351-6. PMID 8343114 DOI: 10.1042/Bj2930351 |
0.383 |
|
| 1993 |
Engh RA, Dieckmann T, Bode W, Auerswald EA, Turk V, Huber R, Oschkinat H. Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy. Journal of Molecular Biology. 234: 1060-9. PMID 8263913 DOI: 10.1006/Jmbi.1993.1659 |
0.42 |
|
| 1993 |
Grams F, Huber R, Kress LF, Moroder L, Bode W. Activation of snake venom metalloproteinases by a cysteine switch-like mechanism. Febs Letters. 335: 76-80. PMID 8243670 DOI: 10.1016/0014-5793(93)80443-X |
0.35 |
|
| 1993 |
Berendes R, Voges D, Demange P, Huber R, Burger A. Structure-function analysis of the ion channel selectivity filter in human annexin V. Science (New York, N.Y.). 262: 427-30. PMID 7692599 DOI: 10.1126/Science.7692599 |
0.332 |
|
| 1993 |
Ficner R, Lobeck K, Schmidt G, Huber R. Isolation, crystallization, crystal structure analysis and refinement of B-phycoerythrin from the red alga Porphyridium sordidum at 2.2 A resolution. Journal of Molecular Biology. 228: 935-50. PMID 1469725 DOI: 10.1016/0022-2836(92)90876-L |
0.339 |
|
| 1993 |
Völkl P, Huber R, Drobner E, Rachel R, Burggraf S, Trincone A, Stetter KO. Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum. Applied and Environmental Microbiology. 59: 2918-2926. DOI: 10.1128/Aem.59.9.2918-2926.1993 |
0.302 |
|
| 1993 |
Bossemeyer D, Engh R, Kinzel V, Ponstingl H, Huber R. Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). The Embo Journal. 12: 849-859. DOI: 10.1002/J.1460-2075.1993.Tb05725.X |
0.456 |
|
| 1992 |
Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW. Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution. Febs Letters. 306: 119-24. PMID 1633865 DOI: 10.1016/0014-5793(92)80981-L |
0.415 |
|
| 1992 |
Bacher A, Weinkauf S, Bachmann L, Ritsert K, Baumeister W, Huber R, Ladenstein R. Electron microscopy of decorated crystals for the determination of crystallographic rotation and translation parameters in large protein complexes. Journal of Molecular Biology. 225: 1065-73. PMID 1613790 DOI: 10.1016/0022-2836(92)90105-S |
0.376 |
|
| 1992 |
Steipe B, Plückthun A, Huber R. Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant. Journal of Molecular Biology. 225: 739-53. PMID 1602480 DOI: 10.1016/0022-2836(92)90398-4 |
0.404 |
|
| 1992 |
Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, Bode W. The interaction of thrombin with fibrinogen. A structural basis for its specificity. European Journal of Biochemistry. 206: 187-95. PMID 1587268 DOI: 10.1111/J.1432-1033.1992.Tb16916.X |
0.309 |
|
| 1992 |
Nar H, Huber R, Messerschmidt A, Filippou AC, Barth M, Jaquinod M, van de Kamp M, Canters GW. Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin. European Journal of Biochemistry / Febs. 205: 1123-9. PMID 1576995 DOI: 10.1111/J.1432-1033.1992.Tb16881.X |
0.355 |
|
| 1992 |
Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agró A. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Journal of Molecular Biology. 224: 179-205. PMID 1548698 DOI: 10.1016/0022-2836(92)90583-6 |
0.358 |
|
| 1992 |
Guasch A, Coll M, Avilés FX, Huber R. Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. Journal of Molecular Biology. 224: 141-157. PMID 1548696 DOI: 10.1016/0022-2836(92)90581-4 |
0.574 |
|
| 1992 |
Bode W, Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. European Journal of Biochemistry. 204: 433-51. PMID 1541261 DOI: 10.1111/J.1432-1033.1992.Tb16654.X |
0.384 |
|
| 1992 |
Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. Journal of Molecular Biology. 227: 214-26. PMID 1522586 DOI: 10.1016/0022-2836(92)90692-D |
0.315 |
|
| 1992 |
Schmid C, Ladenstein R, Luecke H, Huber R, Bacher A. Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli. Journal of Molecular Biology. 226: 1279-81. PMID 1518056 DOI: 10.1016/0022-2836(92)91067-Y |
0.365 |
|
| 1992 |
Baumann U, Bode W, Huber R, Travis J, Potempa J. Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. Journal of Molecular Biology. 226: 1207-18. PMID 1518052 DOI: 10.1016/0022-2836(92)91062-T |
0.413 |
|
| 1992 |
Vendrell J, Guasch A, Coll M, Villegas V, Billeter M, Wider G, Huber R, Wüthrich K, Avilés FX. Pancreatic procarboxypeptidases: their activation processes related to the structural features of the zymogens and activation segments. Biological Chemistry Hoppe-Seyler. 373: 387-92. PMID 1515065 DOI: 10.1515/Bchm3.1992.373.2.387 |
0.571 |
|
| 1992 |
Szyperski T, Güntert P, Stone SR, Tulinsky A, Bode W, Huber R, Wüthrich K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51). Journal of Molecular Biology. 228: 1206-11. PMID 1474586 DOI: 10.1016/0022-2836(92)90326-F |
0.425 |
|
| 1992 |
Laber B, Gomis-Rüth FX, Romão MJ, Huber R. Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization Biochemical Journal. 288: 691-695. PMID 1463470 DOI: 10.1042/Bj2880691 |
0.401 |
|
| 1992 |
Lewit-Bentley A, Morera S, Huber R, Bodo G. The effect of metal binding on the structure of annexin V and implications for membrane binding. European Journal of Biochemistry. 210: 73-7. PMID 1446685 DOI: 10.1111/J.1432-1033.1992.Tb17392.X |
0.33 |
|
| 1992 |
Billeter M, Vendrell J, Wider G, Avilés FX, Coll M, Guasch A, Huber R, Wüthrich K. Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B. Journal of Biomolecular Nmr. 2: 1-10. PMID 1422143 DOI: 10.1007/Bf02192796 |
0.619 |
|
| 1992 |
Messerschmidt A, Steigemann W, Huber R, Lang G, Kroneck PM. X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini. European Journal of Biochemistry. 209: 597-602. PMID 1330552 DOI: 10.1111/J.1432-1033.1992.Tb17325.X |
0.587 |
|
| 1992 |
Bode W, Gomis-Rüth FX, Huber R, Zwilling R, Stöcker W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature. 358: 164-167. PMID 1319561 DOI: 10.1038/358164A0 |
0.441 |
|
| 1992 |
Huber R, Berendes R, Burger A, Schneider M, Karshikov A, Luecke H, Römisch J, Paques E. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. Journal of Molecular Biology. 223: 683-704. PMID 1311770 DOI: 10.1016/0022-2836(92)90984-R |
0.385 |
|
| 1991 |
Huber R, Schneider M, Mayr I, Römisch J, Paques EP. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. Febs Letters. 275: 15-21. PMID 2148156 DOI: 10.1016/0014-5793(90)81428-Q |
0.358 |
|
| 1991 |
Dirr HW, Mann K, Huber R, Ladenstein R, Reinemer P. Class pi glutathione S-transferase from pig lung. Purification, biochemical characterization, primary structure and crystallization. European Journal of Biochemistry. 196: 693-8. PMID 2013291 DOI: 10.1111/j.1432-1033.1991.tb15867.x |
0.307 |
|
| 1991 |
Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. Journal of Molecular Biology. 221: 765-72. PMID 1942029 DOI: 10.1016/0022-2836(91)80173-R |
0.338 |
|
| 1991 |
Weinkauf S, Bacher A, Baumeister W, Ladenstein R, Huber R, Bachmann L. Correlation of metal decoration and topochemistry on protein surfaces. Journal of Molecular Biology. 221: 637-45. PMID 1920438 DOI: 10.1016/0022-2836(91)80078-9 |
0.352 |
|
| 1991 |
Rydel TJ, Tulinsky A, Bode W, Huber R. Refined structure of the hirudin-thrombin complex. Journal of Molecular Biology. 221: 583-601. PMID 1920434 DOI: 10.1016/0022-2836(91)80074-5 |
0.437 |
|
| 1991 |
Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. Journal of Molecular Biology. 218: 427-47. PMID 1901363 DOI: 10.1016/0022-2836(91)90723-J |
0.431 |
|
| 1991 |
Duerring M, Schmidt GB, Huber R. Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 A resolution. Journal of Molecular Biology. 217: 577-92. PMID 1899708 DOI: 10.1016/0022-2836(91)90759-Y |
0.332 |
|
| 1991 |
Musil D, Bode W, Huber R, Laskowski M, Lin TY, Ardelt W. Refined X-ray crystal structures of the reactive site modified ovomucoid inhibitor third domains from silver pheasant (OMSVP3*) and from Japanese quail (OMJPQ3*). Journal of Molecular Biology. 220: 739-55. PMID 1870129 DOI: 10.1016/0022-2836(91)90114-L |
0.43 |
|
| 1991 |
Brisson A, Mosser G, Huber R. Structure of soluble and membrane-bound human annexin V. Journal of Molecular Biology. 220: 199-203. PMID 1830342 DOI: 10.1016/0022-2836(91)90002-N |
0.332 |
|
| 1991 |
Engh RA, Huber R. Accurate bond and angle parameters for X‐ray protein structure refinement Acta Crystallographica Section A. 47: 392-400. DOI: 10.1107/S0108767391001071 |
0.329 |
|
| 1991 |
Bode W, Huber R. Ligand binding: proteinase-protein inhibitor interactions Current Opinion in Structural Biology. 1: 45-52. DOI: 10.1016/0959-440X(91)90010-Q |
0.364 |
|
| 1991 |
Messerschmidt A, Huber R, Kroneck P. X-ray crystallographic characterisation of type-2 depleted ascorbate oxidase from zucchini Journal of Inorganic Biochemistry. 43: 189. DOI: 10.1016/0162-0134(91)84181-8 |
0.52 |
|
| 1991 |
Bode W, Huber R. Proteinase-Protein Inhibitor Interaction Biomedica Biochimica Acta. 50: 103-115. DOI: 10.1007/978-3-642-76412-7_9 |
0.317 |
|
| 1991 |
Coll M, Guasch A, Avilés FX, Huber R. Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. The Embo Journal. 10: 1-9. DOI: 10.1002/J.1460-2075.1991.Tb07914.X |
0.461 |
|
| 1991 |
Musil D, Zucic D, Turk D, Engh RA, Mayr I, Huber R, Popovic T, Turk V, Towatari T, Katunuma N. The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. The Embo Journal. 10: 2321-2330. DOI: 10.1002/J.1460-2075.1991.Tb07771.X |
0.44 |
|
| 1990 |
Messerschmidt A, Huber R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. European Journal of Biochemistry. 187: 341-52. PMID 2404764 DOI: 10.1111/J.1432-1033.1990.Tb15311.X |
0.345 |
|
| 1990 |
Huber R. E. Antonini Plenary lecture. A structural basis of light energy and electron transfer in biology European Journal of Biochemistry. 187: 283-305. PMID 2404762 DOI: 10.1111/J.1432-1033.1990.Tb15305.X |
0.303 |
|
| 1990 |
Wright HT, Qian HX, Huber R. Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin Journal of Molecular Biology. 213: 513-528. PMID 2352279 DOI: 10.1016/S0022-2836(05)80212-8 |
0.417 |
|
| 1990 |
Stubbs M, Summers L, Mayr I, Schneider M, Bode W, Huber R, Ries A, Kühn K. Crystals of the NC1 domain of human type IV collagen. Journal of Molecular Biology. 211: 683-684. PMID 2313693 DOI: 10.1016/0022-2836(90)90066-U |
0.345 |
|
| 1990 |
Glockshuber R, Steipe B, Huber R, Plückthun A. Crystallization and preliminary X-ray studies of the VL domain of the antibody McPC603 produced in Escherichia coli. Journal of Molecular Biology. 213: 613-5. PMID 2113586 DOI: 10.1016/S0022-2836(05)80247-5 |
0.381 |
|
| 1990 |
Duerring M, Huber R, Bode W, Ruembeli R, Zuber H. Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A. Journal of Molecular Biology. 211: 633-44. PMID 2106585 DOI: 10.1016/0022-2836(90)90270-V |
0.336 |
|
| 1990 |
Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Rüssmann L, Schumacher G. Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures. Journal of Molecular Biology. 214: 597-610. PMID 1696320 DOI: 10.1016/0022-2836(90)90201-V |
0.442 |
|
| 1990 |
Rachel R, Engel AM, Huber R, Stetter K, Baumeister W. A porin-type protein is the main constituent of the cell envelope of the ancestral eubacteriumThermotoga maritima Febs Letters. 262: 64-68. DOI: 10.1016/0014-5793(90)80155-C |
0.305 |
|
| 1990 |
Stubbs M, Laber B, Bode W, Huber R, Jerala R, Lenarcic B, Turk V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. The Embo Journal. 9: 1939-1947. DOI: 10.1002/J.1460-2075.1990.Tb08321.X |
0.468 |
|
| 1990 |
Huber R, Römisch J, Paques EP. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. The Embo Journal. 9: 3867-3874. DOI: 10.1002/J.1460-2075.1990.Tb07605.X |
0.397 |
|
| 1989 |
Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T. The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. Febs Letters. 242: 285-92. PMID 2914611 DOI: 10.1016/0014-5793(89)80486-7 |
0.314 |
|
| 1989 |
Laber B, Krieglstein K, Henschen A, Kos J, Turk V, Huber R, Bode W. The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein. Febs Letters. 248: 162-8. PMID 2721673 DOI: 10.1016/0014-5793(89)80453-3 |
0.308 |
|
| 1989 |
Huber R. A structural basis of light energy and electron transfer in biology Bioscience Reports. 9: 635-673. PMID 2692721 DOI: 10.1007/Bf01114805 |
0.301 |
|
| 1989 |
Roth M, Lewit-Bentley A, Michel H, Deisenhofer J, Huber R, Oesterhelt D. Detergent structure in crystals of a bacterial photosynthetic reaction centre Nature. 340: 659-662. DOI: 10.1038/340659A0 |
0.632 |
|
| 1989 |
Huber R. Nobel lecture. A structural basis of light energy and electron transfer in biology. The Embo Journal. 8: 2125-2147. DOI: 10.1002/J.1460-2075.1989.Tb08337.X |
0.301 |
|
| 1989 |
Huber R. A Structural Basis of Light Energy and Electron Transfer in Biology (Nobel Lecture) Angewandte Chemie. 28: 848-869. DOI: 10.1002/Anie.198908481 |
0.301 |
|
| 1988 |
Huber R, Schneider M, Mayr I, Müller R, Deutzmann R, Suter F, Zuber H, Falk H, Kayser H. Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution. Journal of Molecular Biology. 198: 499-513. PMID 3430616 DOI: 10.1016/0022-2836(87)90296-8 |
0.42 |
|
| 1988 |
Hoeffken HW, Knof SH, Bartlett PA, Huber R, Moellering H, Schumacher G. Crystal structure determination, refinement and molecular model of creatine amidinohydrolase from Pseudomonas putida. Journal of Molecular Biology. 204: 417-33. PMID 3221393 DOI: 10.1016/0022-2836(88)90586-4 |
0.327 |
|
| 1988 |
Declercq JP, Tinant B, Parello J, Etienne G, Huber R. Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius). Journal of Molecular Biology. 202: 349-53. PMID 3172221 DOI: 10.1016/0022-2836(88)90464-0 |
0.395 |
|
| 1988 |
Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J, Turk V. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. The Embo Journal. 7: 2593-2599. DOI: 10.1002/J.1460-2075.1988.Tb03109.X |
0.437 |
|
| 1988 |
Huber R. Flexibility and Rigidity of Proteins and Protein–Pigment Complexes Angewandte Chemie International Edition in English. 27: 79-88. DOI: 10.1002/Anie.198800791 |
0.385 |
|
| 1987 |
Brünger AT, Huber R, Karplus M. Trypsinogen-trypsin transition: a molecular dynamics study of induced conformational change in the activation domain. Biochemistry. 26: 5153-62. PMID 3663651 DOI: 10.1021/Bi00390A039 |
0.348 |
|
| 1987 |
Ladenstein R, Bacher A, Huber R. Some observations of a correlation between the symmetry of large heavy-atom complexes and their binding sites on proteins. Journal of Molecular Biology. 195: 751-3. PMID 3656432 DOI: 10.1016/0022-2836(87)90196-3 |
0.369 |
|
| 1987 |
Huber R, Schneider M, Epp O, Mayr I, Messerschmidt A, Pflugrath J, Kayser H. Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. Journal of Molecular Biology. 195: 423-434. PMID 3656419 DOI: 10.1016/0022-2836(87)90661-9 |
0.423 |
|
| 1987 |
Huber R. Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes. Eleventh Keilin memorial lecture Biochemical Society Transactions. 15: 1009-1020. PMID 3502256 DOI: 10.1042/Bst0151009 |
0.418 |
|
| 1987 |
Wlodawer A, Deisenhofer J, Huber R. Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 193: 145-56. PMID 2438420 DOI: 10.1016/0022-2836(87)90633-4 |
0.609 |
|
| 1986 |
Schirmer T, Huber R, Schneider M, Bode W, Miller M, Hackert ML. Crystal structure analysis and refinement at 2.5 A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. The molecular model and its implications for light-harvesting. Journal of Molecular Biology. 188: 651-76. PMID 3090271 DOI: 10.1016/S0022-2836(86)80013-4 |
0.432 |
|
| 1986 |
Ladenstein R, Meyer B, Huber R, Labischinski H, Bartels K, Bartunik HD, Bachmann L, Ludwig HC, Bacher A. Heavy riboflavin synthase from Bacillus subtilis. Particle dimensions, crystal packing and molecular symmetry. Journal of Molecular Biology. 187: 87-100. PMID 3083109 DOI: 10.1016/0022-2836(86)90408-0 |
0.398 |
|
| 1986 |
Allen JP, Feher G, Yeates TO, Rees DC, Deisenhofer J, Michel H, Huber R. Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by x-ray diffraction. Proceedings of the National Academy of Sciences of the United States of America. 83: 8589-93. PMID 3022298 DOI: 10.1073/Pnas.83.22.8589 |
0.662 |
|
| 1986 |
Bode W, Wei A, Huber R, Meyer E, Travis J, Neumann S. X‐ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. The Embo Journal. 5: 2453-2458. DOI: 10.1002/J.1460-2075.1986.Tb04521.X |
0.473 |
|
| 1985 |
Deisenhofer J, Epp O, Miki K, Huber R, Michel H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution. Nature. 318: 618-24. PMID 22439175 DOI: 10.1038/318618A0 |
0.651 |
|
| 1985 |
Wlodawer A, Walter J, Huber R, Sjölin L. Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. Journal of Molecular Biology. 180: 301-29. PMID 6210373 DOI: 10.1016/S0022-2836(84)80006-6 |
0.365 |
|
| 1985 |
Wang D, Bode W, Huber R. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution. Journal of Molecular Biology. 185: 595-624. PMID 4057257 DOI: 10.1016/0022-2836(85)90074-9 |
0.402 |
|
| 1985 |
Bode W, Epp O, Huber R, Laskowski M, Ardelt W. The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). European Journal of Biochemistry. 147: 387-95. PMID 3971987 DOI: 10.1111/J.1432-1033.1985.Tb08762.X |
0.392 |
|
| 1985 |
Huber R, Schneider M. A group refinement procedure in protein crystallography using Fourier transforms Journal of Applied Crystallography. 18: 165-169. DOI: 10.1107/S0021889885010044 |
0.363 |
|
| 1985 |
Deisenhofer J, Michel H, Huber R. The structural basis of photosynthetic light reactions in bacteria Trends in Biochemical Sciences. 10: 243-248. DOI: 10.1016/0968-0004(85)90143-4 |
0.55 |
|
| 1984 |
Wiegand G, Remington S, Deisenhofer J, Huber R. Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A. Journal of Molecular Biology. 174: 205-19. PMID 6716477 DOI: 10.1016/0022-2836(84)90373-5 |
0.761 |
|
| 1984 |
Deisenhofer J, Epp O, Miki K, Huber R, Michel H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. Journal of Molecular Biology. 180: 385-98. PMID 6392571 DOI: 10.1016/S0022-2836(84)80011-X |
0.661 |
|
| 1984 |
Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. Journal of Molecular Biology. 177: 531-57. PMID 6332197 |
0.58 |
|
| 1984 |
Bode W, Walter J, Huber R, Wenzel HR, Tschesche H. The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor. European Journal of Biochemistry. 144: 185-90. PMID 6207021 DOI: 10.1111/J.1432-1033.1984.Tb08447.X |
0.418 |
|
| 1984 |
Walter J, Huber R, Sjölin; L, Wlodawer A. Structure of bovine pancreatic trypsin inhibitor: joint refinement with high-resolution X-ray and neutron data Acta Crystallographica Section a Foundations of Crystallography. 40: C19-C19. DOI: 10.1107/S0108767384099268 |
0.313 |
|
| 1983 |
Bolognesi M, Gatti G, Menagatti E, Guarneri M, Marquart M, Papamokos E, Huber R. Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation. Journal of Molecular Biology. 162: 839-68. PMID 7169635 DOI: 10.1016/0022-2836(82)90550-2 |
0.412 |
|
| 1983 |
Marquart M, Walter J, Deisenhofer J, Bode W, Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors Acta Crystallographica Section B Structural Science. 39: 480-490. DOI: 10.1107/S010876818300275X |
0.533 |
|
| 1982 |
Weber E, Papamokos E, Bode W, Huber R, Kato I, Laskowski M. Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor. Journal of Molecular Biology. 149: 109-23. PMID 7310876 DOI: 10.1016/0022-2836(81)90263-1 |
0.43 |
|
| 1982 |
Remington S, Wiegand G, Huber R. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. Journal of Molecular Biology. 158: 111-52. PMID 7120407 DOI: 10.1016/0022-2836(82)90452-1 |
0.667 |
|
| 1982 |
Papamokos E, Weber E, Bode W, Huber R, Empie MW, Kato I, Laskowski M. Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases. Journal of Molecular Biology. 158: 515-37. PMID 6752426 DOI: 10.1016/0022-2836(82)90212-1 |
0.381 |
|
| 1980 |
Marquart M, Deisenhofer J, Huber R, Palm W. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.0 A resolution. Journal of Molecular Biology. 141: 369-91. PMID 7441755 DOI: 10.1016/0022-2836(80)90252-1 |
0.519 |
|
| 1980 |
Huber R, Scholze H, Pâques EP, Deisenhofer J. Crystal structure analysis and molecular model of human C3a anaphylatoxin. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 361: 1389-99. PMID 7439885 DOI: 10.1515/Bchm2.1980.361.2.1389 |
0.608 |
|
| 1980 |
Huber R. Spatial structure of immunoglobulin molecules Klinische Wochenschrift. 58: 1217-1231. PMID 6780722 DOI: 10.1007/Bf01478928 |
0.328 |
|
| 1980 |
Ladenstein R, Epp O, Bartels K, Jones A, Huber R, Wendel A. Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 A resolution. Journal of Molecular Biology. 134: 199-218. PMID 537063 DOI: 10.1016/0022-2836(79)90032-9 |
0.42 |
|
| 1979 |
Huber R. Conformational flexibility in protein molecules Nature. 280: 538-539. PMID 460436 DOI: 10.1038/280538A0 |
0.307 |
|
| 1979 |
Wiegand G, Kukla D, Scholze H, Jones TA, Huber R. Crystal structure analysis of the tetragonal crystal form are preliminary molecular model of pig-heart citrate synthase. European Journal of Biochemistry. 93: 41-50. PMID 436830 DOI: 10.1111/J.1432-1033.1979.Tb12792.X |
0.435 |
|
| 1979 |
Huber R. Conformational flexibility and its functional significance in some protein molecules Trends in Biochemical Sciences. 4: 276-277. DOI: 10.1016/0968-0004(79)90298-6 |
0.342 |
|
| 1978 |
Deisenhofer J, Jones TA, Huber R, Sjödahl J, Sjöquist J. Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 359: 975-85. PMID 711157 DOI: 10.1515/Bchm2.1978.359.2.975 |
0.513 |
|
| 1978 |
Matsushima M, Marquart M, Jones TA, Colman PM, Bartels K, Huber R. Crystal structure of the human Fab fragment Kol and its comparison with the intact Kol molecule. Journal of Molecular Biology. 121: 441-59. PMID 671546 DOI: 10.1016/0022-2836(78)90393-5 |
0.375 |
|
| 1978 |
Bode W, Huber R. Crystal structure analysis and refinement of two variants of trigonal trypsinogen: trigonal trypsin and PEG (polyethylene glycol) trypsinogen and their comparison with orthorhombic trypsin and trigonal trypsinogen. Febs Letters. 90: 265-269. PMID 668890 DOI: 10.1016/0014-5793(78)80382-2 |
0.38 |
|
| 1978 |
Weber E, Steigemann W, Jones TA, Huber R. The structure of oxy-erythrocruorin at 1.4 X resolution. Journal of Molecular Biology. 120: 327-36. PMID 642012 DOI: 10.1016/0022-2836(78)90071-2 |
0.349 |
|
| 1978 |
Bode W, Schwager P, Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution. Journal of Molecular Biology. 118: 99-112. PMID 625059 DOI: 10.1016/0022-2836(78)90246-2 |
0.379 |
|
| 1978 |
Huber R, Bode W. Structural basis of the activation and action of trypsin Accounts of Chemical Research. 11: 114-122. DOI: 10.1021/Ar50123A006 |
0.344 |
|
| 1977 |
Fehlhammer H, Bode W, Huber R. Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin. Journal of Molecular Biology. 111: 415-38. PMID 864704 DOI: 10.1016/S0022-2836(77)80062-4 |
0.417 |
|
| 1976 |
Colman PM, Deisenhofer J, Huber R. Structure of the human antibody molecule Kol (immunoglobulin G1): an electron density map at 5 A resolution. Journal of Molecular Biology. 100: 257-78. PMID 1255713 DOI: 10.1016/S0022-2836(76)80062-9 |
0.52 |
|
| 1976 |
Hetzel R, Wüthrich K, Deisenhofer J, Huber R. Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). II. Semi-empirical energy calculations. Biophysics of Structure and Mechanism. 2: 159-80. PMID 1085644 DOI: 10.1007/BF00863707 |
0.514 |
|
| 1976 |
Huber R, Deisenhofer J, Colman PM, Matsushima M, Palm W. Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature. 264: 415-20. PMID 1004567 DOI: 10.1038/264415A0 |
0.554 |
|
| 1976 |
Deisenhofer J, Colman PM, Epp O, Huber R. Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 A resolution. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 357: 1421-34. PMID 992566 DOI: 10.1515/Bchm2.1976.357.2.1421 |
0.504 |
|
| 1976 |
Bode W, Fehlhammer H, Huber R. Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation. Journal of Molecular Biology. 106: 325-35. PMID 978726 DOI: 10.1016/0022-2836(76)90089-9 |
0.399 |
|
| 1976 |
Huber R, Deisenhofer J, Colman PM, Epp O, Fehlhammer H, Palm W. Proceedings: X-ray diffraction analysis of immunoglobulin structure. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 357: 614-5. PMID 964922 |
0.481 |
|
| 1976 |
Deisenhofer J, Colman PM, Huber R, Haupt H, Schwick G. Crystallographic structural studies of a human Fc-fragment. I. An electron-density map at 4 A resolution and a partial model. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 357: 435-45. PMID 955567 DOI: 10.1515/Bchm2.1976.357.1.435 |
0.555 |
|
| 1975 |
Epp O, Lattman EE, Schiffer M, Huber R, Palm W. The molecular structure of a dimer composed of the variable portions of the bence-jones protein REI refined at 2.0-Å resolution Biochemistry. 14: 4943-4952. PMID 1182131 DOI: 10.1021/Bi00693A025 |
0.422 |
|
| 1974 |
Epp O, Colman P, Fehlhammer H, Bode W, Schiffer M, Huber R, Palm W. Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI. European Journal of Biochemistry. 45: 513-24. PMID 4851220 DOI: 10.1111/J.1432-1033.1974.Tb03576.X |
0.41 |
|
| 1974 |
Huber R, Kukla D, Bode W, Schwager P, Bartels K, Deisenhofer J, Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution. Journal of Molecular Biology. 89: 73-101. PMID 4475115 DOI: 10.1016/0022-2836(74)90163-6 |
0.587 |
|
| 1973 |
Rühlmann A, Kukla D, Schwager P, Bartels K, Huber R. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. Journal of Molecular Biology. 77: 417-436. PMID 4737866 DOI: 10.1016/0022-2836(73)90448-8 |
0.405 |
|
| 1973 |
Huber R, Kukla D, Rühlmann A, Steigemann W. Pancreatic trypsin inhibitor (Kunitz). I. Structure and function. Cold Spring Harbor Symposia On Quantitative Biology. 36: 141-8. PMID 4508131 DOI: 10.1101/Sqb.1972.036.01.019 |
0.316 |
|
| 1972 |
Blow DM, Wright CS, Kukla D, Rühlmann A, Steigemann W, Huber R. A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin. Journal of Molecular Biology. 69: 137-44. PMID 4672197 DOI: 10.1016/0022-2836(72)90028-9 |
0.324 |
|
| 1971 |
Huber R, Epp O, Formanek H. Structures of deoxy- and carbonmonoxy-erythrocruorin. Journal of Molecular Biology. 52: 349-54. PMID 5485913 DOI: 10.1016/0022-2836(70)90035-5 |
0.321 |
|
| 1971 |
Huber R, Epp O, Steigemann W, Formanek H. The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin. European Journal of Biochemistry. 19: 42-50. PMID 5102553 DOI: 10.1111/J.1432-1033.1971.Tb01285.X |
0.339 |
|
| 1971 |
Epp O, Steigemann W, Formanek H, Huber R. Crystallographic evidence for the tetrameric subunit structure of L-asparaginase from Escherichia coli. European Journal of Biochemistry. 20: 432-7. PMID 4931953 DOI: 10.1111/J.1432-1033.1971.Tb01410.X |
0.393 |
|
| 1970 |
Huber R, Kukla D, Rühlmann A, Epp O, Formanek H. The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the polypeptide chain. Naturwissenschaften. 57: 389-392. PMID 5447861 DOI: 10.1007/Bf00599976 |
0.35 |
|
| 1969 |
Qasba R, Brandl F, Hoppe W, Huber R. Kristallstrukturanalyse der monoklinen Modifikation des 3,5,8,10-Tetramethylcycloheptazulen Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 25: 1198-1200. DOI: 10.1107/S0567740869003736 |
0.491 |
|
| 1969 |
Huber R, Kopfmann G. Experimental absorption correction: results Acta Crystallographica Section A. 25: 143-152. DOI: 10.1107/S0567739469000246 |
0.323 |
|
| 1968 |
Amit A, Huber R, Hoppe W. Die Röntgenstrukturanalyse des Bullvalens Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 24: 865-869. DOI: 10.1107/S0567740868003298 |
0.488 |
|
| 1967 |
Paulus E, Hoppe W, Huber R. Struktur von Cyclooctatetraen-di-metall-cyclopentadienyl-Komplexen Naturwissenschaften. 54: 67-68. DOI: 10.1007/Bf00592755 |
0.473 |
|
| 1965 |
Huber R, Hoppe W. [On the chemistry of ecdysone. VII. Analysis of the crystal and molecular structure of the molting hormone in insects, ecdysone, using the automized folding molecule method]. Chemische Berichte. 98: 2403-24. PMID 5849856 DOI: 10.1002/Cber.19650980744 |
0.537 |
|
| 1965 |
Hoppe W, Huber R. [On the chemistry of ecdysone. II. Determination of the skeleton of sterin and its orientation by diffuse x-ray diffraction in ecdysone crystals]. Chemische Berichte. 98: 2353-60. PMID 5849852 DOI: 10.1002/Cber.19650980739 |
0.499 |
|
| 1963 |
Karlson P, Hoffmeister H, Hoppe W, Huber R. Zur Chemie Des Ecdysons European Journal of Organic Chemistry. 662: 1-20. DOI: 10.1002/Jlac.19636620102 |
0.489 |
|
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