Hermann Schindelin - Publications

Affiliations: 
Stony Brook University, Stony Brook, NY, United States 
Area:
Biochemistry

103 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Kasaragod VB, Schindelin H. Structural Framework for Metal Incorporation during Molybdenum Cofactor Biosynthesis. Structure (London, England : 1993). PMID 27112598 DOI: 10.1016/j.str.2016.02.023  0.48
2016 Hänzelmann P, Schindelin H. Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions. Structure (London, England : 1993). 24: 140-7. PMID 26712280 DOI: 10.1016/j.str.2015.10.027  0.48
2016 Hänzelmann P, Schindelin H. Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97. Structure (London, England : 1993). 24: 127-39. PMID 26712278 DOI: 10.1016/j.str.2015.10.026  0.48
2015 Atak S, Langlhofer G, Schaefer N, Kessler D, Meiselbach H, Delto C, Schindelin H, Villmann C. Disturbances of Ligand Potency and Enhanced Degradation of the Human Glycine Receptor at Affected Positions G160 and T162 Originally Identified in Patients Suffering from Hyperekplexia. Frontiers in Molecular Neuroscience. 8: 79. PMID 26733802 DOI: 10.3389/fnmol.2015.00079  0.48
2015 Ludolphs M, Schneeberger D, Soykan T, Schäfer J, Papadopoulos T, Brose N, Schindelin H, Steinem C. Specificity of collybistin-phosphoinositide interactions: Impact of the individual protein domains. The Journal of Biological Chemistry. PMID 26546675 DOI: 10.1074/jbc.M115.673400  0.48
2015 Pelz JP, Schindelin H, van Pee K, Kuper J, Kisker C, Diederichs K, Fischer U, Grimm C. Crystallizing the 6S and 8S spliceosomal assembly intermediates: a complex project. Acta Crystallographica. Section D, Biological Crystallography. 71: 2040-53. PMID 26457428 DOI: 10.1107/S1399004715014832  0.48
2015 Buchberger A, Schindelin H, Hänzelmann P. Control of p97 function by cofactor binding. Febs Letters. 589: 2578-89. PMID 26320413 DOI: 10.1016/j.febslet.2015.08.028  0.48
2015 Knobloch G, Jabari N, Stadlbauer S, Schindelin H, Köhn M, Gohla A. Synthesis of hydrolysis-resistant pyridoxal 5'-phosphate analogs and their biochemical and X-ray crystallographic characterization with the pyridoxal phosphatase chronophin. Bioorganic & Medicinal Chemistry. 23: 2819-27. PMID 25783190 DOI: 10.1016/j.bmc.2015.02.049  0.48
2015 Delto CF, Heisler FF, Kuper J, Sander B, Kneussel M, Schindelin H. The LisH motif of muskelin is crucial for oligomerization and governs intracellular localization. Structure (London, England : 1993). 23: 364-73. PMID 25579817 DOI: 10.1016/j.str.2014.11.016  0.48
2015 Maric HM, Kasaragod VB, Haugaard-Kedström L, Hausrat TJ, Kneussel M, Schindelin H, Strømgaard K. Design and synthesis of high-affinity dimeric inhibitors targeting the interactions between gephyrin and inhibitory neurotransmitter receptors. Angewandte Chemie (International Ed. in English). 54: 490-4. PMID 25413248 DOI: 10.1002/anie.201409043  0.48
2014 Maric HM, Kasaragod VB, Hausrat TJ, Kneussel M, Tretter V, Strømgaard K, Schindelin H. Molecular basis of the alternative recruitment of GABA(A) versus glycine receptors through gephyrin. Nature Communications. 5: 5767. PMID 25531214 DOI: 10.1038/ncomms6767  0.48
2014 Zhao B, Villhauer EB, Bhuripanyo K, Kiyokawa H, Schindelin H, Yin J. SUMO-mimicking peptides inhibiting protein SUMOylation. Chembiochem : a European Journal of Chemical Biology. 15: 2662-6. PMID 25412743 DOI: 10.1002/cbic.201402472  0.48
2014 Maric HM, Kasaragod VB, Schindelin H. Modulation of gephyrin-glycine receptor affinity by multivalency. Acs Chemical Biology. 9: 2554-62. PMID 25137389 DOI: 10.1021/cb500303a  0.48
2014 Cho JH, Meng W, Sato S, Kim EY, Schindelin H, Raleigh DP. Energetically significant networks of coupled interactions within an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 12079-84. PMID 25099351 DOI: 10.1073/pnas.1402054111  0.48
2014 Soykan T, Schneeberger D, Tria G, Buechner C, Bader N, Svergun D, Tessmer I, Poulopoulos A, Papadopoulos T, Varoqueaux F, Schindelin H, Brose N. A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. The Embo Journal. 33: 2113-33. PMID 25082542 DOI: 10.15252/embj.201488143  0.48
2014 Schäfer A, Kuhn M, Schindelin H. Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules. Acta Crystallographica. Section D, Biological Crystallography. 70: 1311-20. PMID 24816100 DOI: 10.1107/S1399004714002910  0.48
2014 Kestler C, Knobloch G, Tessmer I, Jeanclos E, Schindelin H, Gohla A. Chronophin dimerization is required for proper positioning of its substrate specificity loop. The Journal of Biological Chemistry. 289: 3094-103. PMID 24338687 DOI: 10.1074/jbc.M113.536482  0.48
2014 Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A. Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities. The Journal of Biological Chemistry. 289: 3416-31. PMID 24338473 DOI: 10.1074/jbc.M113.503359  0.48
2013 Sander B, Tria G, Shkumatov AV, Kim EY, Grossmann JG, Tessmer I, Svergun DI, Schindelin H. Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states. Acta Crystallographica. Section D, Biological Crystallography. 69: 2050-60. PMID 24100323 DOI: 10.1107/S0907444913018714  0.48
2013 Zhao B, Zhang K, Bhuripanyo K, Choi CH, Villhauer EB, Li H, Zheng N, Kiyokawa H, Schindelin H, Yin J. Profiling the cross reactivity of ubiquitin with the Nedd8 activating enzyme by phage display. Plos One. 8: e70312. PMID 23936405 DOI: 10.1371/journal.pone.0070312  0.48
2013 Zhao B, Zhang K, Villhauer EB, Bhuripanyo K, Kiyokawa H, Schindelin H, Yin J. Phage display to identify Nedd8-mimicking peptides as inhibitors of the Nedd8 transfer cascade. Chembiochem : a European Journal of Chemical Biology. 14: 1323-30. PMID 23824602 DOI: 10.1002/cbic.201300234  0.48
2013 Grimm C, Chari A, Pelz JP, Kuper J, Kisker C, Diederichs K, Stark H, Schindelin H, Fischer U. Structural basis of assembly chaperone- mediated snRNP formation. Molecular Cell. 49: 692-703. PMID 23333303 DOI: 10.1016/j.molcel.2012.12.009  0.48
2013 Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H. The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities. The Journal of Biological Chemistry. 288: 2029-39. PMID 23192347 DOI: 10.1074/jbc.M112.410522  0.48
2012 Zhao B, Choi CH, Bhuripanyo K, Villhauer EB, Zhang K, Schindelin H, Yin J. Inhibiting the protein ubiquitination cascade by ubiquitin-mimicking short peptides. Organic Letters. 14: 5760-3. PMID 23134251 DOI: 10.1021/ol3027736  0.48
2012 Zhao B, Bhuripanyo K, Zhang K, Kiyokawa H, Schindelin H, Yin J. Orthogonal ubiquitin transfer through engineered E1-E2 cascades for protein ubiquitination. Chemistry & Biology. 19: 1265-77. PMID 23102221 DOI: 10.1016/j.chembiol.2012.07.023  0.48
2012 Zhao B, Bhuripanyo K, Schneider J, Zhang K, Schindelin H, Boone D, Yin J. Specificity of the E1-E2-E3 enzymatic cascade for ubiquitin C-terminal sequences identified by phage display. Acs Chemical Biology. 7: 2027-35. PMID 23003343 DOI: 10.1021/cb300339p  0.48
2012 Tretter V, Mukherjee J, Maric HM, Schindelin H, Sieghart W, Moss SJ. Gephyrin, the enigmatic organizer at GABAergic synapses. Frontiers in Cellular Neuroscience. 6: 23. PMID 22615685 DOI: 10.3389/fncel.2012.00023  0.48
2012 Hänzelmann P, Schäfer A, Völler D, Schindelin H. Structural insights into functional modes of proteins involved in ubiquitin family pathways. Methods in Molecular Biology (Clifton, N.J.). 832: 547-76. PMID 22350912 DOI: 10.1007/978-1-61779-474-2_39  0.48
2011 Maric HM, Mukherjee J, Tretter V, Moss SJ, Schindelin H. Gephyrin-mediated γ-aminobutyric acid type A and glycine receptor clustering relies on a common binding site. The Journal of Biological Chemistry. 286: 42105-14. PMID 22006921 DOI: 10.1074/jbc.M111.303412  0.48
2011 Mukherjee J, Kretschmannova K, Gouzer G, Maric HM, Ramsden S, Tretter V, Harvey K, Davies PA, Triller A, Schindelin H, Moss SJ. The residence time of GABA(A)Rs at inhibitory synapses is determined by direct binding of the receptor α1 subunit to gephyrin. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 31: 14677-87. PMID 21994384 DOI: 10.1523/JNEUROSCI.2001-11.2011  0.48
2011 Hänzelmann P, Schindelin H. The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97. The Journal of Biological Chemistry. 286: 38679-90. PMID 21914798 DOI: 10.1074/jbc.M111.274506  0.48
2011 Tretter V, Kerschner B, Milenkovic I, Ramsden SL, Ramerstorfer J, Saiepour L, Maric HM, Moss SJ, Schindelin H, Harvey RJ, Sieghart W, Harvey K. Molecular basis of the γ-aminobutyric acid A receptor α3 subunit interaction with the clustering protein gephyrin. The Journal of Biological Chemistry. 286: 37702-11. PMID 21880742 DOI: 10.1074/jbc.M111.291336  0.48
2011 Hänzelmann P, Buchberger A, Schindelin H. Hierarchical binding of cofactors to the AAA ATPase p97. Structure (London, England : 1993). 19: 833-43. PMID 21645854 DOI: 10.1016/j.str.2011.03.018  0.48
2010 Hänzelmann P, Stingele J, Hofmann K, Schindelin H, Raasi S. The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain. The Journal of Biological Chemistry. 285: 20390-8. PMID 20427284 DOI: 10.1074/jbc.M110.112532  0.48
2010 Völler D, Schindelin H. And yet it moves: active site remodeling in the SUMO E1. Structure (London, England : 1993). 18: 419-21. PMID 20399179 DOI: 10.1016/j.str.2010.03.005  0.48
2009 Zhao G, Li G, Schindelin H, Lennarz WJ. An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation. Proceedings of the National Academy of Sciences of the United States of America. 106: 16197-202. PMID 19805280 DOI: 10.1073/pnas.0908321106  0.48
2009 Hänzelmann P, Dahl JU, Kuper J, Urban A, Müller-Theissen U, Leimkühler S, Schindelin H. Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Science : a Publication of the Protein Society. 18: 2480-91. PMID 19798741 DOI: 10.1002/pro.260  0.48
2009 Lees NS, Hänzelmann P, Hernandez HL, Subramanian S, Schindelin H, Johnson MK, Hoffman BM. ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications. Journal of the American Chemical Society. 131: 9184-5. PMID 19566093 DOI: 10.1021/ja903978u  0.48
2009 Zürn A, Zabel U, Vilardaga JP, Schindelin H, Lohse MJ, Hoffmann C. Fluorescence resonance energy transfer analysis of alpha 2a-adrenergic receptor activation reveals distinct agonist-specific conformational changes. Molecular Pharmacology. 75: 534-41. PMID 19106230 DOI: 10.1124/mol.108.052399  0.48
2009 Luther KB, Schindelin H, Haltiwanger RS. Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants. The Journal of Biological Chemistry. 284: 3294-305. PMID 19028689 DOI: 10.1074/jbc.M805502200  0.48
2009 Zhao G, Li G, Zhou X, Matsuo I, Ito Y, Suzuki T, Lennarz WJ, Schindelin H. Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase. Glycobiology. 19: 118-25. PMID 18854368 DOI: 10.1093/glycob/cwn108  0.48
2008 Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ, Schindelin H. The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule. The Journal of Biological Chemistry. 283: 33630-40. PMID 18815132 DOI: 10.1074/jbc.M806026200  0.48
2008 Li G, Zhao G, Schindelin H, Lennarz WJ. Tyrosine phosphorylation of ATPase p97 regulates its activity during ERAD. Biochemical and Biophysical Research Communications. 375: 247-51. PMID 18706391 DOI: 10.1016/j.bbrc.2008.08.018  0.48
2008 Lee I, Schindelin H. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell. 134: 268-78. PMID 18662542 DOI: 10.1016/j.cell.2008.05.046  0.48
2008 Schmitz J, Chowdhury MM, Hänzelmann P, Nimtz M, Lee EY, Schindelin H, Leimkühler S. The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry. 47: 6479-89. PMID 18491921 DOI: 10.1021/bi800477u  0.48
2008 Li H, Chavan M, Schindelin H, Lennarz WJ, Li H. Structure of the oligosaccharyl transferase complex at 12 A resolution. Structure (London, England : 1993). 16: 432-40. PMID 18334218 DOI: 10.1016/j.str.2007.12.013  0.48
2008 Kadurin I, Golubovic A, Leisle L, Schindelin H, Gründer S. Differential effects of N-glycans on surface expression suggest structural differences between the acid-sensing ion channel (ASIC) 1a and ASIC1b. The Biochemical Journal. 412: 469-75. PMID 18307415 DOI: 10.1042/BJ20071614  0.48
2008 Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency. Biochemistry. 47: 615-26. PMID 18092812 DOI: 10.1021/bi701734g  0.48
2008 Paukert M, Chen X, Polleichtner G, Schindelin H, Gründer S. Candidate amino acids involved in H+ gating of acid-sensing ion channel 1a. The Journal of Biological Chemistry. 283: 572-81. PMID 17981796 DOI: 10.1074/jbc.M706811200  0.48
2008 Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of a molybdopterin synthase-precursor Z complex: Insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency (Biochemistry (2008) 47, 2, (615-626)) Biochemistry. 47: 3315. DOI: 10.1021/bi8001117  0.48
2007 Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry. 46: 7497-505. PMID 17536785 DOI: 10.1021/bi6026314  0.48
2007 Zhao G, Zhou X, Wang L, Li G, Schindelin H, Lennarz WJ. Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation. Proceedings of the National Academy of Sciences of the United States of America. 104: 8785-90. PMID 17496150 DOI: 10.1073/pnas.0702966104  0.48
2007 Nichols JD, Xiang S, Schindelin H, Rajagopalan KV. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Biochemistry. 46: 78-86. PMID 17198377 DOI: 10.1021/bi061551q  0.48
2007 Schindelin H. Evolutionary Origin of the Activation Step During Ubiquitin-dependent Protein Degradation Protein Degradation. 1: 21-43. DOI: 10.1002/9783527619320.ch3  0.48
2006 Zhou X, Zhao G, Truglio JJ, Wang L, Li G, Lennarz WJ, Schindelin H. Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module. Proceedings of the National Academy of Sciences of the United States of America. 103: 17214-9. PMID 17088551 DOI: 10.1073/pnas.0602954103  0.48
2006 Chavan M, Chen Z, Li G, Schindelin H, Lennarz WJ, Li H. Dimeric organization of the yeast oligosaccharyl transferase complex. Proceedings of the National Academy of Sciences of the United States of America. 103: 8947-52. PMID 16754853 DOI: 10.1073/pnas.0603262103  0.48
2006 Suzuki T, Hara I, Nakano M, Zhao G, Lennarz WJ, Schindelin H, Taniguchi N, Totani K, Matsuo I, Ito Y. Site-specific labeling of cytoplasmic peptide:N-glycanase by N,N'-diacetylchitobiose-related compounds. The Journal of Biological Chemistry. 281: 22152-60. PMID 16740630 DOI: 10.1074/jbc.M603236200  0.48
2006 Li G, Zhao G, Zhou X, Schindelin H, Lennarz WJ. The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. Proceedings of the National Academy of Sciences of the United States of America. 103: 8348-53. PMID 16709668 DOI: 10.1073/pnas.0602747103  0.48
2006 Hänzelmann P, Schindelin H. Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. Proceedings of the National Academy of Sciences of the United States of America. 103: 6829-34. PMID 16632608 DOI: 10.1073/pnas.0510711103  0.48
2006 Xiang S, Kim EY, Connelly JJ, Nassar N, Kirsch J, Winking J, Schwarz G, Schindelin H. The crystal structure of Cdc42 in complex with collybistin II, a gephyrin-interacting guanine nucleotide exchange factor. Journal of Molecular Biology. 359: 35-46. PMID 16616186 DOI: 10.1016/j.jmb.2006.03.019  0.48
2006 Kim EY, Schrader N, Smolinsky B, Bedet C, Vannier C, Schwarz G, Schindelin H. Deciphering the structural framework of glycine receptor anchoring by gephyrin. The Embo Journal. 25: 1385-95. PMID 16511563 DOI: 10.1038/sj.emboj.7601029  0.48
2006 Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H. Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways. The Journal of Biological Chemistry. 281: 13751-61. PMID 16500903 DOI: 10.1074/jbc.M600137200  0.48
2006 Lawrence SH, Luther KB, Schindelin H, Ferry JG. Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila. Journal of Bacteriology. 188: 1143-54. PMID 16428418 DOI: 10.1128/JB.188.3.1143-1154.2006  0.48
2006 Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell. 124: 61-73. PMID 16413482 DOI: 10.1016/j.cell.2005.10.044  0.48
2005 Li G, Zhou X, Zhao G, Schindelin H, Lennarz WJ. Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome. Proceedings of the National Academy of Sciences of the United States of America. 102: 15809-14. PMID 16249333 DOI: 10.1073/pnas.0507155102  0.48
2004 Biswas S, Katiyar S, Li G, Zhou X, Lennarz WJ, Schindelin H. The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23. Biochemical and Biophysical Research Communications. 323: 149-55. PMID 15351714 DOI: 10.1016/j.bbrc.2004.08.061  0.48
2004 Hänzelmann P, Schindelin H. Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proceedings of the National Academy of Sciences of the United States of America. 101: 12870-5. PMID 15317939 DOI: 10.1073/pnas.0404624101  0.48
2004 Hänzelmann P, Hernández HL, Menzel C, García-Serres R, Huynh BH, Johnson MK, Mendel RR, Schindelin H. Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. The Journal of Biological Chemistry. 279: 34721-32. PMID 15180982 DOI: 10.1074/jbc.M313398200  0.48
2004 Iyer PP, Lawrence SH, Luther KB, Rajashankar KR, Yennawar HP, Ferry JG, Schindelin H. Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila. Structure (London, England : 1993). 12: 559-67. PMID 15062079 DOI: 10.1016/j.str.2004.03.007  0.48
2004 Schrader N, Kim EY, Winking J, Paulukat J, Schindelin H, Schwarz G. Biochemical characterization of the high affinity binding between the glycine receptor and gephyrin. The Journal of Biological Chemistry. 279: 18733-41. PMID 14976213 DOI: 10.1074/jbc.M311245200  0.48
2003 Giesemann T, Schwarz G, Nawrotzki R, Berhörster K, Rothkegel M, Schlüter K, Schrader N, Schindelin H, Mendel RR, Kirsch J, Jockusch BM. Complex formation between the postsynaptic scaffolding protein gephyrin, profilin, and Mena: a possible link to the microfilament system. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 23: 8330-9. PMID 12967995  0.48
2003 Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H. Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. The Journal of Biological Chemistry. 278: 14514-22. PMID 12571227 DOI: 10.1074/jbc.M300449200  0.48
2002 Rizzi M, Schindelin H. Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis. Current Opinion in Structural Biology. 12: 709-20. PMID 12504674 DOI: 10.1016/S0959-440X(02)00385-8  0.48
2001 Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature. 414: 325-9. PMID 11713534 DOI: 10.1038/35104586  0.48
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  0.48
2001 Schwarz G, Schrader N, Mendel RR, Hecht HJ, Schindelin H. Crystal structures of human gephyrin and plant Cnx1 G domains: Comparative analysis and functional implications Journal of Molecular Biology. 312: 405-418. PMID 11554796 DOI: 10.1006/jmbi.2001.4952  0.48
2001 Xiang S, Nichols J, Rajagopalan KV, Schindelin H. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure (London, England : 1993). 9: 299-310. PMID 11525167 DOI: 10.1016/S0969-2126(01)00588-3  0.48
2001 Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nature Structural Biology. 8: 42-6. PMID 11135669 DOI: 10.1038/83034  0.48
2000 Lake MW, Temple CA, Rajagopalan KV, Schindelin H. The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. The Journal of Biological Chemistry. 275: 40211-7. PMID 10978347 DOI: 10.1074/jbc.M007406200  0.48
2000 Wuebbens MM, Liu MTW, Rajagopalan KV, Schindelin H. Insight into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC Structure. 8: 709-718. PMID 10903949 DOI: 10.1016/S0969-2126(00)00157-X  0.48
2000 Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli. The Journal of Biological Chemistry. 275: 1814-22. PMID 10636880 DOI: 10.1074/jbc.275.3.1814  0.48
2000 Li HK, Temple C, Rajagopalan KV, Schindelin H. The 1.3 Å Crystal structure of rhodobacter sphaeroides dimethyl sulfoxide reductase reveals two distinct molybdenum coordination environments Journal of the American Chemical Society. 122: 7673-7680. DOI: 10.1021/ja000643e  0.48
1999 Sternglanz R, Schindelin H. Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases Proceedings of the National Academy of Sciences of the United States of America. 96: 8807-8808. PMID 10430845 DOI: 10.1073/pnas.96.16.8807  0.48
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  0.48
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: 10.1016/S0168-6445(98)00040-0  0.48
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  0.48
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  0.48
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  0.48
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  0.48
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.  0.48
1996 Lauble H, Knödler S, Schindelin H, Förster S, Wajant H, Effenberger F. Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.). Acta Crystallographica. Section D, Biological Crystallography. 52: 887-9. PMID 15299660 DOI: 10.1107/S0907444996002399  0.48
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  0.48
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  0.48
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  0.48
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.  0.48
1995 Schindelin H, Zhang M, Bald R, Furste JP, Erdmann VA, Heinemann U. Crystal structure of an RNA dodecamer containing the Escherichia coli Shine-Dalgarno sequence Journal of Molecular Biology. 249: 595-603. PMID 7540215 DOI: 10.1006/jmbi.1995.0321  0.48
1994 Schindelin H, Jiang W, Inouye M, Heinemann U. Crystal structure of CspA, the major cold shock protein of Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 91: 5119-5123. PMID 8197194 DOI: 10.1073/pnas.91.11.5119  0.48
1994 Lauble H, Müller K, Schindelin H, Förster S, Effenberger F. Crystallization and preliminary X-ray diffraction studies of mandelonitrile lyase from almonds. Proteins. 19: 343-7. PMID 7984630 DOI: 10.1002/prot.340190410  0.48
1993 Schindelin H, Marahiel MA, Heinemann U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein Nature. 364: 164-168. PMID 8321288  0.48
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  0.48
1993 Welfle H, Misselwitz R, Welfle K, Schindelin H, Scholtz AS, Heinemann U. Conformations and conformational changes of four Phe-->Trp variants of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis studied by circular dichroism and fluorescence spectroscopy. European Journal of Biochemistry / Febs. 217: 849-56. PMID 8223641 DOI: 10.1111/j.1432-1033.1993.tb18313.x  0.48
1992 Groch N, Schindelin H, Scholtz AS, Hahn U, Heinemann U. Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene. European Journal of Biochemistry / Febs. 207: 677-85. PMID 1633819 DOI: 10.1111/j.1432-1033.1992.tb17095.x  0.48
1992 Schindelin H, Herrler M, Willimsky G, Marahiel MA, Heinemann U. Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB Proteins: Structure, Function and Genetics. 14: 120-124. PMID 1409560 DOI: 10.1002/prot.340140113  0.48
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