Year |
Citation |
Score |
2021 |
Petruseva I, Naumenko N, Kuper J, Anarbaev R, Kappenberger J, Kisker C, Lavrik O. The Interaction Efficiency of XPD-p44 With Bulky DNA Damages Depends on the Structure of the Damage. Frontiers in Cell and Developmental Biology. 9: 617160. PMID 33777931 DOI: 10.3389/fcell.2021.617160 |
0.31 |
|
2021 |
Eltschkner S, Kehrein J, Le TA, Davoodi S, Merget B, Basak S, Weinrich JD, Schiebel J, Tonge PJ, Engels B, Sotriffer C, Kisker C. A Long Residence Time Enoyl-Reductase Inhibitor Explores an Extended Binding Region with Isoenzyme-Dependent Tautomer Adaptation and Differential Substrate-Binding Loop Closure. Acs Infectious Diseases. PMID 33710875 DOI: 10.1021/acsinfecdis.0c00437 |
0.321 |
|
2020 |
Peissert S, Sauer F, Grabarczyk DB, Braun C, Sander G, Poterszman A, Egly JM, Kuper J, Kisker C. In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair. Nature Communications. 11: 1667. PMID 32245994 DOI: 10.1038/S41467-020-15241-9 |
0.784 |
|
2018 |
Nasir N, Kisker C. Mechanistic insights into the enzymatic activity and inhibition of the replicative polymerase exonuclease domain from Mycobacterium tuberculosis. Dna Repair. 74: 17-25. PMID 30641156 DOI: 10.1016/j.dnarep.2018.12.006 |
0.325 |
|
2018 |
Ramirez YA, Adler T, Altmann E, Tiesmeyer C, Klemm T, Sauer F, Kathman S, Statsyuk A, Sotriffer C, Kisker C. Structural basis of substrate recognition and covalent inhibition of Cdu1 from Chlamydia trachomatis. Chemmedchem. PMID 30028574 DOI: 10.1002/Cmdc.201800364 |
0.308 |
|
2018 |
Grabarczyk DB, Silkenat S, Kisker C. Structural Basis for the Recruitment of Ctf18-RFC to the Replisome. Structure (London, England : 1993). 26: 137-144.e3. PMID 29225079 DOI: 10.1016/j.str.2017.11.004 |
0.802 |
|
2017 |
Kaiser S, Sauer F, Kisker C. The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism. Nature Communications. 8: 15907. PMID 28653661 DOI: 10.1038/ncomms15907 |
0.366 |
|
2017 |
Spagnuolo LA, Eltschkner S, Yu W, Daryaee F, Davoodi S, Knudson SE, Allen EK, Merino J, Pschibul A, Moree B, Thivalapill N, Truglio JJ, Salafsky J, Slayden RA, Kisker C, et al. Evaluating the contribution of transition state destabilization to changes in the residence time of triazole-based InhA inhibitors. Journal of the American Chemical Society. PMID 28151657 DOI: 10.1021/Jacs.6B11148 |
0.736 |
|
2015 |
Koch SC, Kuper J, Gasteiger KL, Simon N, Strasser R, Eisen D, Geiger S, Schneider S, Kisker C, Carell T. Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA). Proceedings of the National Academy of Sciences of the United States of America. PMID 26100901 DOI: 10.1073/Pnas.1508509112 |
0.31 |
|
2015 |
Schiebel J, Chang A, Merget B, Bommineni GR, Yu W, Spagnuolo LA, Baxter MV, Tareilus M, Tonge PJ, Kisker C, Sotriffer CA. An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction. Biochemistry. 54: 1943-55. PMID 25706582 DOI: 10.1021/Bi5014358 |
0.306 |
|
2014 |
Khan I, Suhasini AN, Banerjee T, Sommers JA, Kaplan DL, Kuper J, Kisker C, Brosh RM. Impact of age-associated cyclopurine lesions on DNA repair helicases. Plos One. 9: e113293. PMID 25409515 DOI: 10.1371/Journal.Pone.0113293 |
0.318 |
|
2014 |
Kuper J, Braun C, Elias A, Michels G, Sauer F, Schmitt DR, Poterszman A, Egly JM, Kisker C. In TFIIH, XPD helicase is exclusively devoted to DNA repair. Plos Biology. 12: e1001954. PMID 25268380 DOI: 10.1371/Journal.Pbio.1001954 |
0.363 |
|
2014 |
Buechner CN, Heil K, Michels G, Carell T, Kisker C, Tessmer I. Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility. The Journal of Biological Chemistry. 289: 3613-24. PMID 24338567 DOI: 10.1074/Jbc.M113.523001 |
0.341 |
|
2013 |
Schiebel J, Kapilashrami K, Fekete A, Bommineni GR, Schaefer CM, Mueller MJ, Tonge PJ, Kisker C. Structural basis for the recognition of mycolic acid precursors by KasA, a condensing enzyme and drug target from Mycobacterium tuberculosis. The Journal of Biological Chemistry. 288: 34190-204. PMID 24108128 DOI: 10.1074/Jbc.M113.511436 |
0.309 |
|
2013 |
Kisker C, Kuper J, Van Houten B. Prokaryotic nucleotide excision repair. Cold Spring Harbor Perspectives in Biology. 5: a012591. PMID 23457260 DOI: 10.1101/cshperspect.a012591 |
0.325 |
|
2013 |
Kuper J, Kisker C. DNA Helicases in NER, BER, and MMR. Advances in Experimental Medicine and Biology. 767: 203-24. PMID 23161013 DOI: 10.1007/978-1-4614-5037-5_10 |
0.311 |
|
2012 |
Wu Y, Sommers JA, Loiland JA, Kitao H, Kuper J, Kisker C, Brosh RM. The Q motif of Fanconi anemia group J protein (FANCJ) DNA helicase regulates its dimerization, DNA binding, and DNA repair function. The Journal of Biological Chemistry. 287: 21699-716. PMID 22582397 DOI: 10.1074/jbc.M112.351338 |
0.343 |
|
2012 |
Patsalo V, Yondola MA, Luan B, Shoshani I, Kisker C, Green DF, Raleigh DP, Hearing P. Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies. The Journal of Biological Chemistry. 287: 22573-83. PMID 22573317 DOI: 10.1074/Jbc.M112.344234 |
0.752 |
|
2012 |
Hirschbeck MW, Kuper J, Lu H, Liu N, Neckles C, Shah S, Wagner S, Sotriffer CA, Tonge PJ, Kisker C. Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors. Structure (London, England : 1993). 20: 89-100. PMID 22244758 DOI: 10.1016/J.Str.2011.07.019 |
0.363 |
|
2012 |
Roth HM, Römer J, Grundler V, Van Houten B, Kisker C, Tessmer I. XPB helicase regulates DNA incision by the Thermoplasma acidophilum endonuclease Bax1. Dna Repair. 11: 286-93. PMID 22237014 DOI: 10.1016/j.dnarep.2011.12.002 |
0.32 |
|
2012 |
Kuper J, Wolski SC, Michels G, Kisker C. Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. The Embo Journal. 31: 494-502. PMID 22081108 DOI: 10.1038/emboj.2011.374 |
0.374 |
|
2011 |
Li HJ, Li X, Liu N, Zhang H, Truglio JJ, Mishra S, Kisker C, Garcia-Diaz M, Tonge PJ. Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member. Biochemistry. 50: 9532-44. PMID 21830810 DOI: 10.1021/Bi200877X |
0.766 |
|
2010 |
Machutta CA, Bommineni GR, Luckner SR, Kapilashrami K, Ruzsicska B, Simmerling C, Kisker C, Tonge PJ. Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin. The Journal of Biological Chemistry. 285: 6161-9. PMID 20018879 DOI: 10.1074/Jbc.M109.077909 |
0.303 |
|
2009 |
Roth HM, Tessmer I, Van Houten B, Kisker C. Bax1 is a novel endonuclease: implications for archaeal nucleotide excision repair. The Journal of Biological Chemistry. 284: 32272-8. PMID 19759013 DOI: 10.1074/jbc.M109.055913 |
0.38 |
|
2009 |
Lu H, England K, am Ende C, Truglio JJ, Luckner S, Reddy BG, Marlenee NL, Knudson SE, Knudson DL, Bowen RA, Kisker C, Slayden RA, Tonge PJ. Slow-onset inhibition of the FabI enoyl reductase from francisella tularensis: residence time and in vivo activity. Acs Chemical Biology. 4: 221-31. PMID 19206187 DOI: 10.1021/Cb800306Y |
0.734 |
|
2009 |
Dietzel U, Kuper J, Doebbler JA, Schulte A, Truglio JJ, Leimkühler S, Kisker C. Mechanism of Substrate and Inhibitor Binding of Rhodobacter capsulatus Xanthine Dehydrogenase. The Journal of Biological Chemistry. 284: 8768-76. PMID 19109249 DOI: 10.1074/Jbc.M808114200 |
0.764 |
|
2008 |
Wolski SC, Kuper J, Hänzelmann P, Truglio JJ, Croteau DL, Van Houten B, Kisker C. Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. Plos Biology. 6: e149. PMID 18578568 DOI: 10.1371/Journal.Pbio.0060149 |
0.773 |
|
2008 |
Respicio L, Nair PA, Huang Q, Anil B, Tracz S, Truglio JJ, Kisker C, Raleigh DP, Ojima I, Knudson DL, Tonge PJ, Slayden RA. Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinburgh, Scotland). 88: 420-9. PMID 18479968 DOI: 10.1016/J.Tube.2008.03.001 |
0.738 |
|
2007 |
Yakubovskaya E, Lukin M, Chen Z, Berriman J, Wall JS, Kobayashi R, Kisker C, Bogenhagen DF. The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits. The Embo Journal. 26: 4283-91. PMID 17762861 DOI: 10.1038/Sj.Emboj.7601843 |
0.647 |
|
2007 |
Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C. Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad. The Embo Journal. 26: 613-22. PMID 17245438 DOI: 10.1038/Sj.Emboj.7601497 |
0.812 |
|
2007 |
Kolappan S, Zwahlen J, Zhou R, Truglio JJ, Tonge PJ, Kisker C. Lysine 190 is the catalytic base in MenF, the menaquinone-specific isochorismate synthase from Escherichia coli: implications for an enzyme family. Biochemistry. 46: 946-53. PMID 17240978 DOI: 10.1021/Bi0608515 |
0.746 |
|
2006 |
Sullivan TJ, Truglio JJ, Boyne ME, Novichenok P, Zhang X, Stratton CF, Li HJ, Kaur T, Amin A, Johnson F, Slayden RA, Kisker C, Tonge PJ. High affinity InhA inhibitors with activity against drug-resistant strains of Mycobacterium tuberculosis. Acs Chemical Biology. 1: 43-53. PMID 17163639 DOI: 10.1021/Cb0500042 |
0.719 |
|
2006 |
Rafi S, Novichenok P, Kolappan S, Zhang X, Stratton CF, Rawat R, Kisker C, Simmerling C, Tonge PJ. Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli. The Journal of Biological Chemistry. 281: 39285-93. PMID 17012233 DOI: 10.1074/Jbc.M608758200 |
0.45 |
|
2006 |
Truglio JJ, Karakas E, Rhau B, Wang H, DellaVecchia MJ, Van Houten B, Kisker C. Structural basis for DNA recognition and processing by UvrB. Nature Structural & Molecular Biology. 13: 360-4. PMID 16532007 DOI: 10.1038/Nsmb1072 |
0.786 |
|
2006 |
Truglio JJ, Croteau DL, Van Houten B, Kisker C. Prokaryotic nucleotide excision repair: the UvrABC system. Chemical Reviews. 106: 233-52. PMID 16464004 DOI: 10.1021/Cr040471U |
0.728 |
|
2006 |
Yakubovskaya E, Chen Z, Carrodeguas JA, Kisker C, Bogenhagen DF. Functional human mitochondrial DNA polymerase gamma forms a heterotrimer. The Journal of Biological Chemistry. 281: 374-82. PMID 16263719 DOI: 10.1074/Jbc.M509730200 |
0.617 |
|
2005 |
Karakas E, Kisker C. Structural analysis of missense mutations causing isolated sulfite oxidase deficiency. Dalton Transactions (Cambridge, England : 2003). 3459-63. PMID 16234925 DOI: 10.1039/B505789M |
0.613 |
|
2005 |
Karakas E, Wilson HL, Graf TN, Xiang S, Jaramillo-Busquets S, Rajagopalan KV, Kisker C. Structural insights into sulfite oxidase deficiency. The Journal of Biological Chemistry. 280: 33506-15. PMID 16048997 DOI: 10.1074/Jbc.M505035200 |
0.614 |
|
2005 |
Van Houten B, Croteau DL, DellaVecchia MJ, Wang H, Kisker C. 'Close-fitting sleeves': DNA damage recognition by the UvrABC nuclease system. Mutation Research. 577: 92-117. PMID 15927210 DOI: 10.1016/J.Mrfmmm.2005.03.013 |
0.383 |
|
2005 |
Truglio JJ, Rhau B, Croteau DL, Wang L, Skorvaga M, Karakas E, DellaVecchia MJ, Wang H, Van Houten B, Kisker C. Structural insights into the first incision reaction during nucleotide excision repair. The Embo Journal. 24: 885-94. PMID 15692561 DOI: 10.1038/Sj.Emboj.7600568 |
0.796 |
|
2004 |
Skorvaga M, DellaVecchia MJ, Croteau DL, Theis K, Truglio JJ, Mandavilli BS, Kisker C, Van Houten B. Identification of residues within UvrB that are important for efficient DNA binding and damage processing. The Journal of Biological Chemistry. 279: 51574-80. PMID 15456749 DOI: 10.1074/Jbc.M409266200 |
0.779 |
|
2004 |
Truglio JJ, Croteau DL, Skorvaga M, DellaVecchia MJ, Theis K, Mandavilli BS, Van Houten B, Kisker C. Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair. The Embo Journal. 23: 2498-509. PMID 15192705 DOI: 10.1038/Sj.Emboj.7600263 |
0.797 |
|
2004 |
Freisinger E, Grollman AP, Miller H, Kisker C. Lesion (in)tolerance reveals insights into DNA replication fidelity. The Embo Journal. 23: 1494-505. PMID 15057282 DOI: 10.1038/Sj.Emboj.7600158 |
0.428 |
|
2003 |
Guo C, Fischhaber PL, Luk-Paszyc MJ, Masuda Y, Zhou J, Kamiya K, Kisker C, Friedberg EC. Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. The Embo Journal. 22: 6621-30. PMID 14657033 DOI: 10.1093/Emboj/Cdg626 |
0.428 |
|
2003 |
Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C. The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals. Structure (London, England : 1993). 11: 1251-63. PMID 14527393 DOI: 10.1016/J.Str.2003.09.001 |
0.398 |
|
2003 |
Truglio JJ, Theis K, Feng Y, Gajda R, Machutta C, Tonge PJ, Kisker C. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. The Journal of Biological Chemistry. 278: 42352-60. PMID 12909628 DOI: 10.1074/Jbc.M307399200 |
0.767 |
|
2003 |
Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C. The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain. Acta Crystallographica. Section D, Biological Crystallography. 59: 1183-91. PMID 12832761 DOI: 10.1107/S0907444903009934 |
0.361 |
|
2003 |
Freisinger E, Fernandes A, Grollman AP, Kisker C. Crystallographic characterization of an exocyclic DNA adduct: 3,N4-etheno-2'-deoxycytidine in the dodecamer 5'-CGCGAATTepsilonCGCG-3'. Journal of Molecular Biology. 329: 685-97. PMID 12787670 DOI: 10.1016/S0022-2836(03)00445-5 |
0.371 |
|
2002 |
Bell AF, Feng Y, Hofstein HA, Parikh S, Wu J, Rudolph MJ, Kisker C, Whitty A, Tonge PJ. Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers. Chemistry & Biology. 9: 1247-55. PMID 12445775 DOI: 10.1016/S1074-5521(02)00263-6 |
0.341 |
|
2002 |
Truglio JJ, Theis K, Leimkühler S, Rappa R, Rajagopalan KV, Kisker C. Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure (London, England : 1993). 10: 115-25. PMID 11796116 DOI: 10.1016/S0969-2126(01)00697-9 |
0.769 |
|
2002 |
Skorvaga M, Theis K, Mandavilli BS, Kisker C, Van Houten B. The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. The Journal of Biological Chemistry. 277: 1553-9. PMID 11687584 DOI: 10.1074/Jbc.M108847200 |
0.453 |
|
2001 |
Schindelin H, Kisker C, Rajagopalan KV. Molybdopterin from molybdenum and tungsten enzymes. Advances in Protein Chemistry. 58: 47-94. PMID 11665493 DOI: 10.1016/S0065-3233(01)58002-X |
0.409 |
|
2001 |
Friedberg EC, Fischhaber PL, Kisker C. Error-prone DNA polymerases: Novel structures and the benefits of infidelity Cell. 107: 9-12. PMID 11595180 DOI: 10.1016/S0092-8674(01)00509-8 |
0.419 |
|
2001 |
Carrodeguas JA, Theis K, Bogenhagen DF, Kisker C. Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase γ, PolγB, functions as a homodimer Molecular Cell. 7: 43-54. PMID 11172710 DOI: 10.1016/S1097-2765(01)00153-8 |
0.699 |
|
2000 |
Theis K, Skorvaga M, MacHius M, Nakagawa N, Van Houten B, Kisker C. The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch Mutation Research - Dna Repair. 460: 277-300. PMID 10946234 DOI: 10.1016/S0921-8777(00)00032-X |
0.483 |
|
2000 |
Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry. 39: 9222-31. PMID 10924115 DOI: 10.1021/Bi000204S |
0.685 |
|
2000 |
Saenger W, Orth P, Kisker C, Hillen W, Hinrichs W. Der Tetracyclin-Repressor – das Musterbeispiel für einen biologischen Schalter Angewandte Chemie. 112: 2122-2133. DOI: 10.1002/1521-3757(20000616)112:12<2122::Aid-Ange2122>3.0.Co;2-8 |
0.384 |
|
1999 |
Theis K, Chen PJ, Skorvaga M, Van Houten B, Kisker C. Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair Embo Journal. 18: 6899-6907. PMID 10601012 DOI: 10.1093/Emboj/18.24.6899 |
0.473 |
|
1999 |
Stewart MJ, Parikh S, Xiao G, Tonge PJ, Kisker C. Structural basis and mechanism of enoyl reductase inhibition by triclosan. Journal of Molecular Biology. 290: 859-65. PMID 10398587 DOI: 10.1006/Jmbi.1999.2907 |
0.377 |
|
1999 |
Grossmann JG, Hasnain SS, Yousafzai FK, Smith BE, Eady RR, Schindelin H, Kisker C, Howard JB, Tsuruta H, Muller J, Rees DC. Comparing crystallographic and solution structures of nitrogenase complexes Acta Crystallographica Section D: Biological Crystallography. 55: 727-728. PMID 10336305 DOI: 10.1107/S0907444999003856 |
0.633 |
|
1998 |
Kisker C, Schindelin H, Baas D, Rétey J, Meckenstock RU, Kroneck PM. A structural comparison of molybdenum cofactor-containing enzymes. Fems Microbiology Reviews. 22: 503-21. PMID 9990727 DOI: 10.1111/J.1574-6976.1998.Tb00384.X |
0.408 |
|
1997 |
Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 91: 973-83. PMID 9428520 DOI: 10.1016/S0092-8674(00)80488-2 |
0.617 |
|
1997 |
Kisker C, Schindelin H, Rees DC. Molybdenum-cofactor-containing enzymes: Structure and mechanism Annual Review of Biochemistry. 66: 233-267. PMID 9242907 DOI: 10.1146/Annurev.Biochem.66.1.233 |
0.588 |
|
1997 |
Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC. Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature. 387: 370-6. PMID 9163420 DOI: 10.1038/387370A0 |
0.663 |
|
1997 |
Rees DC, Hu Y, Kisker C, Schindelin H. A crystallographic view of the molybdenum cofactor Journal of the Chemical Society - Dalton Transactions. 3909-3914. DOI: 10.1039/A704048B |
0.513 |
|
1997 |
Schindelin H, Kisker C, Rees DC. The molybdenum-cofactor: A crystallographic perspective Journal of Biological Inorganic Chemistry. 2: 773-781. DOI: 10.1007/S007750050194 |
0.461 |
|
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 |
0.363 |
|
1996 |
Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-handed β-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila Embo Journal. 15: 2323-2330. PMID 8665839 |
0.525 |
|
1996 |
Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC. Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science (New York, N.Y.). 272: 1615-21. PMID 8658134 DOI: 10.1126/Science.272.5268.1615 |
0.574 |
|
1996 |
Stowell MHB, Soltis SM, Kisker C, Peters JW, Schindelin H, Rees DC, Cascio D, Beamer L, Hart PJ, Wiener MC, Whitby FG. A simple device for studying macromolecular crystals under moderate gas pressures (0.1-10 MPa) Journal of Applied Crystallography. 29: 608-613. DOI: 10.1107/S0021889896004712 |
0.438 |
|
1996 |
Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. The Embo Journal. 15: 2323-2330. DOI: 10.1002/J.1460-2075.1996.Tb00588.X |
0.584 |
|
1995 |
Kisker C, Hinrichs W, Tovar K, Hillen W, Saenger W. The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance. Journal of Molecular Biology. 247: 260-80. PMID 7707374 DOI: 10.1006/Jmbi.1994.0138 |
0.509 |
|
1994 |
Hinrichs W, Kisker C, Düvel M, Müller A, Tovar K, Hillen W, Saenger W. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science (New York, N.Y.). 264: 418-20. PMID 8153629 DOI: 10.1126/Science.8153629 |
0.512 |
|
1994 |
Schubert WD, Schluckebier G, Backmann J, Granzin J, Kisker C, Choe HW, Hahn U, Pfeil W, Saenger W. X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. European Journal of Biochemistry / Febs. 220: 527-34. PMID 8125111 DOI: 10.1111/J.1432-1033.1994.Tb18652.X |
0.399 |
|
1993 |
Heydenreich A, Koellner G, Choe HW, Cordes F, Kisker C, Schindelin H, Adamiak R, Hahn U, Saenger W. The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study. European Journal of Biochemistry / Febs. 218: 1005-12. PMID 8281918 DOI: 10.1111/J.1432-1033.1993.Tb18459.X |
0.403 |
|
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