Year |
Citation |
Score |
2022 |
Bothe S, Hänzelmann P, Böhler S, Kehrein J, Zehe M, Wiedemann C, Hellmich UA, Brenk R, Schindelin H, Sotriffer C. Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97. Communications Chemistry. 5: 169. PMID 36697690 DOI: 10.1038/s42004-022-00782-5 |
0.321 |
|
2022 |
Imam N, Choudhury S, Hemmen K, Heinze KG, Schindelin H. Deciphering the conformational dynamics of gephyrin-mediated collybistin activation. Biophysical Reports. 2: 100079. PMID 36425671 DOI: 10.1016/j.bpr.2022.100079 |
0.342 |
|
2022 |
Imam N, Choudhury S, Heinze KG, Schindelin H. Differential modulation of collybistin conformational dynamics by the closely related GTPases Cdc42 and TC10. Frontiers in Synaptic Neuroscience. 14: 959875. PMID 35989712 DOI: 10.3389/fnsyn.2022.959875 |
0.302 |
|
2022 |
Truongvan N, Li S, Misra M, Kuhn M, Schindelin H. Structures of UBA6 explain its dual specificity for ubiquitin and FAT10. Nature Communications. 13: 4789. PMID 35970836 DOI: 10.1038/s41467-022-32040-6 |
0.394 |
|
2020 |
Kasaragod VB, Pacios-Michelena A, Schaefer N, Zheng F, Bader N, Alzheimer C, Villmann C, Schindelin H. Pyridoxal kinase inhibition by artemisinins down-regulates inhibitory neurotransmission. Proceedings of the National Academy of Sciences of the United States of America. PMID 33318193 DOI: 10.1073/pnas.2008695117 |
0.302 |
|
2020 |
van der Heden van Noort G, Kim RQ, Misra M, Alexis G, Tomašković I, Shin D, Schindelin H, Filippov DV, Ovaa H, Dikic I. Development of ADPribosyl ubiquitin analogs to study enzymes involved in Legionella infection. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 33075184 DOI: 10.1002/chem.202004590 |
0.32 |
|
2020 |
Green JL, Wu Y, Encheva V, Lasonder E, Prommaban A, Kunzelmann S, Christodoulou E, Grainger M, Truongvan N, Bothe S, Sharma V, Song W, Pinzuti I, Uthaipibull C, Srichairatanakool S, ... ... Schindelin H, et al. Ubiquitin activation is essential for schizont maturation in Plasmodium falciparum blood-stage development. Plos Pathogens. 16: e1008640. PMID 32569299 DOI: 10.1371/Journal.Ppat.1008640 |
0.38 |
|
2020 |
Jeanclos E, Knobloch G, Hoffmann A, Fedorchenko O, Odersky A, Lamprecht AK, Schindelin H, Gohla A. Ca functions as a molecular switch that controls the mutually exclusive complex formation of pyridoxal phosphatase with CIB1 or Calmodulin. Febs Letters. PMID 32324254 DOI: 10.1002/1873-3468.13795 |
0.365 |
|
2020 |
Dietschreit J, Wagner A, Le TA, Klein P, Schindelin H, Opatz T, Engels B, Hellmich U, Ochsenfeld C. Predicting 19 F NMR chemical shifts: A combined computational and experimental study of a trypasonomal oxidoreductase-inhibitor complex. Angewandte Chemie (International Ed. in English). PMID 32239740 DOI: 10.1002/Anie.202000539 |
0.316 |
|
2020 |
Green JL, Wu Y, Encheva V, Lasonder E, Prommaban A, Kunzelmann S, Christodoulou E, Grainger M, Truongvan N, Bothe S, Sharma V, Song W, Pinzuti I, Uthaipibull C, Srichairatanakool S, ... ... Schindelin H, et al. Proteins of the parasite pellicle identified as ubiquitylated. Plos Pathogens. DOI: 10.1371/Journal.Ppat.1008640.S006 |
0.306 |
|
2019 |
Hänzelmann P, Galgenmüller C, Schindelin H. Structure and Function of the AAA+ ATPase p97, a Key Player in Protein Homeostasis. Sub-Cellular Biochemistry. 93: 221-272. PMID 31939153 DOI: 10.1007/978-3-030-28151-9_7 |
0.417 |
|
2019 |
Sereikaite V, Fritzius T, Kasaragod V, Bader N, Maric H, Schindelin H, Bettler B, Strømgaard K. Targeting the γ-aminobutyric acid type B (GABAB) receptor complex: Development of inhibitors targeting the K+ channel tetramerization domain (KCTD) containing proteins/GABAB receptor protein-protein interaction. Journal of Medicinal Chemistry. PMID 31509708 DOI: 10.1021/Acs.Jmedchem.9B01087 |
0.383 |
|
2019 |
Kasaragod VB, Schindelin H. Structure of Heteropentameric GABA Receptors and Receptor-Anchoring Properties of Gephyrin. Frontiers in Molecular Neuroscience. 12: 191. PMID 31440140 DOI: 10.3389/Fnmol.2019.00191 |
0.373 |
|
2019 |
Kitzenmaier A, Schaefer N, Kasaragod VB, Polster T, Hantschmann R, Schindelin H, Villmann C. The P429L loss of function mutation of the human glycine transporter 2 associated with hyperekplexia. The European Journal of Neuroscience. PMID 31370103 DOI: 10.1111/Ejn.14533 |
0.35 |
|
2019 |
Viet KK, Wagner A, Schwickert K, Hellwig N, Brennich M, Bader N, Schirmeister T, Morgner N, Schindelin H, Hellmich UA. Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain. Structure (London, England : 1993). PMID 31178222 DOI: 10.1016/J.Str.2019.04.016 |
0.334 |
|
2019 |
Bansal A, Karanth NM, Demeler B, Schindelin H, Sarma SP. Crystallographic structures of IlvN●Val / Ile complexes: Conformational selectivity for feedback inhibition of AHASs. Biochemistry. PMID 30887800 DOI: 10.1021/Acs.Biochem.9B00050 |
0.43 |
|
2019 |
Kasaragod VB, Hausrat TJ, Schaefer N, Kuhn M, Christensen NR, Tessmer I, Maric HM, Madsen KL, Sotriffer C, Villmann C, Kneussel M, Schindelin H. Elucidating the Molecular Basis for Inhibitory Neurotransmission Regulation by Artemisinins. Neuron. PMID 30704910 DOI: 10.2210/Pdb6Fgd/Pdb |
0.357 |
|
2019 |
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA. Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angewandte Chemie (International Ed. in English). PMID 30605929 DOI: 10.2210/Pdb6Gxy/Pdb |
0.378 |
|
2018 |
Kasaragod VB, Schindelin H. Structure-Function Relationships of Glycine and GABA Receptors and Their Interplay With the Scaffolding Protein Gephyrin. Frontiers in Molecular Neuroscience. 11: 317. PMID 30258351 DOI: 10.3389/Fnmol.2018.00317 |
0.376 |
|
2018 |
Hines RM, Maric HM, Hines DJ, Modgil A, Panzanelli P, Nakamura Y, Nathanson AJ, Cross A, Deeb T, Brandon NJ, Davies P, Fritschy JM, Schindelin H, Moss SJ. Developmental seizures and mortality result from reducing GABA receptor α2-subunit interaction with collybistin. Nature Communications. 9: 3130. PMID 30087324 DOI: 10.1038/S41467-018-05481-1 |
0.3 |
|
2017 |
Skinner JJ, Wang S, Lee J, Ong C, Sommese R, Sivaramakrishnan S, Koelmel W, Hirschbeck M, Schindelin H, Kisker C, Lorenz K, Sosnick TR, Rosner MR. Conserved salt-bridge competition triggered by phosphorylation regulates the protein interactome. Proceedings of the National Academy of Sciences of the United States of America. PMID 29208709 DOI: 10.1073/Pnas.1711543114 |
0.409 |
|
2017 |
Janzen D, Schaefer N, Delto C, Schindelin H, Villmann C. The GlyR Extracellular β8-β9 Loop - A Functional Determinant of Agonist Potency. Frontiers in Molecular Neuroscience. 10: 322. PMID 29062270 DOI: 10.3389/Fnmol.2017.00322 |
0.32 |
|
2017 |
Misra M, Kuhn M, Löbel M, An H, Statsyuk AV, Sotriffer C, Schindelin H. Dissecting the Specificity of Adenosyl Sulfamate Inhibitors Targeting the Ubiquitin-Activating Enzyme. Structure (London, England : 1993). PMID 28578874 DOI: 10.1016/J.Str.2017.05.001 |
0.417 |
|
2017 |
Hänzelmann P, Schindelin H. The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97. Frontiers in Molecular Biosciences. 4: 21. PMID 28451587 DOI: 10.3389/Fmolb.2017.00021 |
0.44 |
|
2017 |
Sosnick TR, Skinner JJ, Wang S, Lee J, Sommese R, Sivaramakrishnan S, Kölmel W, Hirschbeck M, Schindelin H, Kisker C, Lorenz K, Rosner MR. A Phospho-Induced Theft of a Salt Bridge in RKIP Links Map Kinase and G Protein-Mediated Signaling Biophysical Journal. 112: 63a-64a. DOI: 10.1016/J.Bpj.2016.11.382 |
0.385 |
|
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 |
0.481 |
|
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 |
0.429 |
|
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 |
0.414 |
|
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 |
0.409 |
|
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 |
0.396 |
|
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 |
0.367 |
|
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 |
0.384 |
|
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 |
0.332 |
|
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 |
0.427 |
|
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 |
0.384 |
|
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 |
0.341 |
|
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 |
0.387 |
|
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 |
0.417 |
|
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 |
0.408 |
|
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 |
0.391 |
|
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 |
0.479 |
|
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 |
0.485 |
|
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 |
0.466 |
|
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 |
0.321 |
|
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 |
0.45 |
|
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 |
0.392 |
|
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 |
0.43 |
|
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 |
0.459 |
|
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 |
0.353 |
|
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 |
0.358 |
|
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 |
0.391 |
|
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 |
0.341 |
|
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 |
0.484 |
|
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 |
0.378 |
|
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 |
0.502 |
|
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 |
0.334 |
|
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 |
0.442 |
|
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 |
0.475 |
|
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 |
0.377 |
|
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 |
0.514 |
|
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 |
0.492 |
|
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 |
0.342 |
|
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 |
0.462 |
|
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 |
0.47 |
|
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 |
0.466 |
|
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 |
0.395 |
|
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 |
0.456 |
|
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 |
0.476 |
|
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 |
0.466 |
|
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 |
0.362 |
|
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 |
0.446 |
|
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 |
0.349 |
|
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 |
0.447 |
|
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 |
0.646 |
|
2007 |
Schindelin H. Evolutionary Origin of the Activation Step During Ubiquitin-dependent Protein Degradation Protein Degradation. 1: 21-43. DOI: 10.1002/9783527619320.ch3 |
0.438 |
|
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 |
0.45 |
|
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 |
0.393 |
|
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 |
0.419 |
|
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 |
0.415 |
|
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 |
0.395 |
|
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 |
0.602 |
|
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 |
0.406 |
|
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 |
0.433 |
|
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 |
0.489 |
|
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 |
0.651 |
|
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 |
0.421 |
|
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 |
0.397 |
|
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 |
0.4 |
|
2004 |
Hänzelmann P, Hernández HL, Menzel C, GarcÃa-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 |
0.308 |
|
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 |
0.469 |
|
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 |
0.447 |
|
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 DOI: 10.1523/Jneurosci.23-23-08330.2003 |
0.382 |
|
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 |
0.503 |
|
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 |
0.396 |
|
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 |
0.745 |
|
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 |
0.417 |
|
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 |
0.431 |
|
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 |
0.66 |
|
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 |
0.494 |
|
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 |
0.756 |
|
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 |
0.513 |
|
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 |
0.409 |
|
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 |
0.329 |
|
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 |
0.41 |
|
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 |
0.372 |
|
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 |
0.418 |
|
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 |
0.312 |
|
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 |
0.396 |
|
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 |
0.329 |
|
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 |
0.308 |
|
1996 |
Schindelin H, Kisker C, Rees DC. Crystal structure of dimethylsulfoxide reductase defines a new familty of oxotransferases containing the molybdenum cofactor Acta Crystallographica Section a Foundations of Crystallography. 52: C128-C128. DOI: 10.1107/S0108767396094068 |
0.358 |
|
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 |
0.345 |
|
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 |
0.463 |
|
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 DOI: 10.1038/364164A0 |
0.337 |
|
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