Israel Silman - Publications

Affiliations: 
STB Structural Biology Weizmann Institute of Science, Rehovot, Israel 
Area:
Neuroscience Biology, General Biophysics

85 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
2019 Chandar NB, Efremenko I, Silman I, Martin JML, Sussman JL. Molecular dynamics simulations of the interaction of Mouse and Torpedo acetylcholinesterase with covalent inhibitors explain their differential reactivity: Implications for drug design. Chemico-Biological Interactions. PMID 31226285 DOI: 10.1016/j.cbi.2019.06.028  0.68
2019 Novichkova DA, Lushchekina SV, Dym O, Masson P, Silman I, Sussman JL. The four-helix bundle in cholinesterase dimers: Structural and energetic determinants of stability. Chemico-Biological Interactions. PMID 31202688 DOI: 10.1016/j.cbi.2019.06.012  0.68
2019 Oukoloff K, Coquelle N, Bartolini M, Naldi M, Le Guevel R, Bach S, Josselin B, Ruchaud S, Catto M, Pisani L, Denora N, Iacobazzi RM, Silman I, Sussman JL, Buron F, et al. Design, biological evaluation and X-ray crystallography of nanomolar multifunctional ligands targeting simultaneously acetylcholinesterase and glycogen synthase kinase-3. European Journal of Medicinal Chemistry. 168: 58-77. PMID 30798053 DOI: 10.1016/j.ejmech.2018.12.063  0.68
2018 Leung MR, van Bezouwen LS, Schopfer LM, Sussman JL, Silman I, Lockridge O, Zeev-Ben-Mordehai T. Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly. Proceedings of the National Academy of Sciences of the United States of America. PMID 30538207 DOI: 10.1073/pnas.1817009115  0.68
2018 Santoni G, de Sousa J, De la Mora E, Dias J, Jean L, Sussman JL, Silman I, Renard PY, Brown RCD, Weik M, Baati R, Nachon F. Structure-based optimization of non-quaternary reactivators of acetylcholinesterase inhibited by organophosphorus nerve agents. Journal of Medicinal Chemistry. PMID 30125110 DOI: 10.1021/acs.jmedchem.8b00592  0.68
2018 Goldenzweig A, Goldsmith M, Hill SE, Gertman O, Laurino P, Ashani Y, Dym O, Unger T, Albeck S, Prilusky J, Lieberman RL, Aharoni A, Silman I, Sussman JL, Tawfik DS, et al. Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability. Molecular Cell. 70: 380. PMID 29677494 DOI: 10.1016/j.molcel.2018.03.035  0.68
2018 Zorbaz T, Braïki A, Marakovic N, Renou J, de la Mora E, Marek Hrvat N, Katalinic M, Silman I, Sussman JL, Mercey G, Gomez C, Mougeot R, Perez B, Baati R, Nachon F, et al. Potent 3-hydroxy-2-pyridine aldoxime reactivators of organophosphate-inhibited cholinesterases with predicted blood-brain barrier penetration. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29672968 DOI: 10.1002/chem.201801394  0.68
2017 Xu Y, Cheng S, Sussman JL, Silman I, Jiang H. Computational Studies on Acetylcholinesterases. Molecules (Basel, Switzerland). 22. PMID 28796192 DOI: 10.3390/molecules22081324  0.68
2017 Silman I, Sussman JL. Recent developments in structural studies on acetylcholinesterase. Journal of Neurochemistry. PMID 28503857 DOI: 10.1111/jnc.13992  0.68
2016 Goldenzweig A, Goldsmith M, Hill SE, Gertman O, Laurino P, Ashani Y, Dym O, Unger T, Albeck S, Prilusky J, Lieberman RL, Aharoni A, Silman I, Sussman JL, Tawfik DS, et al. Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability. Molecular Cell. PMID 27425410 DOI: 10.1016/j.molcel.2016.06.012  0.64
2016 Ashani Y, Leader H, Aggarwal N, Silman I, Worek F, Sussman JL, Goldsmith M. In vitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for in vivo protection against organophosphate intoxications. Chemico-Biological Interactions. PMID 27163850 DOI: 10.1016/j.cbi.2016.04.039  0.64
2016 Dym O, Song W, Felder C, Roth E, Shnyrov V, Ashani Y, Xu Y, Joosten RP, Weiner L, Sussman JL, Silman I. The Impact of Crystallization Conditions on Structure-Based Drug Design: A Case Study on the Methylene Blue/Acetylcholinesterase Complex. Protein Science : a Publication of the Protein Society. PMID 26990888 DOI: 10.1002/pro.2923  0.64
2013 Ben-David M, Wieczorek G, Elias M, Silman I, Sussman JL, Tawfik DS. Catalytic metal ion rearrangements underline promiscuity and evolvability of a metalloenzyme. Journal of Molecular Biology. 425: 1028-38. PMID 23318950 DOI: 10.1016/j.jmb.2013.01.009  0.64
2013 Silman I, Roth E, Paz A, Triquigneaux MM, Ehrenshaft M, Xu Y, Shnyrov VL, Sussman JL, Deterding LJ, Ashani Y, Mason RP, Weiner L. The specific interaction of the photosensitizer methylene blue with acetylcholinesterase provides a model system for studying the molecular consequences of photodynamic therapy. Chemico-Biological Interactions. 203: 63-6. PMID 23159732 DOI: 10.1016/j.cbi.2012.10.021  0.64
2012 Triquigneaux MM, Ehrenshaft M, Roth E, Silman I, Ashani Y, Mason RP, Weiner L, Deterding LJ. Targeted oxidation of Torpedo californica acetylcholinesterase by singlet oxygen: identification of N-formylkynurenine tryptophan derivatives within the active-site gorge of its complex with the photosensitizer methylene blue. The Biochemical Journal. 448: 83-91. PMID 22888904 DOI: 10.1042/BJ20120992  0.64
2012 Paz A, Roth E, Ashani Y, Xu Y, Shnyrov VL, Sussman JL, Silman I, Weiner L. Structural and functional characterization of the interaction of the photosensitizing probe methylene blue with Torpedo californica acetylcholinesterase. Protein Science : a Publication of the Protein Society. 21: 1138-52. PMID 22674800 DOI: 10.1002/pro.2101  0.64
2012 Goldsmith M, Ashani Y, Simo Y, Ben-David M, Leader H, Silman I, Sussman JL, Tawfik DS. Evolved stereoselective hydrolases for broad-spectrum G-type nerve agent detoxification. Chemistry & Biology. 19: 456-66. PMID 22520752 DOI: 10.1016/j.chembiol.2012.01.017  0.64
2012 Ben-David M, Elias M, Filippi JJ, Duñach E, Silman I, Sussman JL, Tawfik DS. Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1. Journal of Molecular Biology. 418: 181-96. PMID 22387469 DOI: 10.1016/j.jmb.2012.02.042  0.64
2012 Khare SD, Kipnis Y, Greisen P, Takeuchi R, Ashani Y, Goldsmith M, Song Y, Gallaher JL, Silman I, Leader H, Sussman JL, Stoddard BL, Tawfik DS, Baker D. Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis. Nature Chemical Biology. 8: 294-300. PMID 22306579 DOI: 10.1038/nchembio.777  0.64
2012 Xu Y, Li MJ, Greenblatt H, Chen W, Paz A, Dym O, Peleg Y, Chen T, Shen X, He J, Jiang H, Silman I, Sussman JL. Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations. Acta Crystallographica. Section D, Biological Crystallography. 68: 13-25. PMID 22194329 DOI: 10.1107/S0907444911047251  0.64
2012 Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomolecular Nmr Assignments. 6: 15-8. PMID 21647611 DOI: 10.1007/s12104-011-9315-4  0.64
2011 Ashani Y, Goldsmith M, Leader H, Silman I, Sussman JL, Tawfik DS. In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases. Toxicology Letters. 206: 24-8. PMID 21807078 DOI: 10.1016/j.toxlet.2011.07.017  0.64
2011 Offman MN, Krol M, Rost B, Silman I, Sussman JL, Futerman AH. Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease. Protein Engineering, Design & Selection : Peds. 24: 773-5. PMID 21724649 DOI: 10.1093/protein/gzr032  0.64
2011 Sanson B, Colletier JP, Xu Y, Lang PT, Jiang H, Silman I, Sussman JL, Weik M. Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations Protein Science. 20: 1114-1118. PMID 21594947 DOI: 10.1002/pro.661  0.64
2011 Suskiewicz MJ, Sussman JL, Silman I, Shaul Y. Context-dependent resistance to proteolysis of intrinsically disordered proteins Protein Science. 20: 1285-1297. PMID 21574196 DOI: 10.1002/pro.657  0.64
2011 Brumshtein B, Aguilar-Moncayo M, Benito JM, García Fernandez JM, Silman I, Shaaltiel Y, Aviezer D, Sussman JL, Futerman AH, Ortiz Mellet C. Cyclodextrin-mediated crystallization of acid β-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues Organic and Biomolecular Chemistry. 9: 4160-4167. PMID 21483943 DOI: 10.1039/c1ob05200d  0.64
2011 Gupta RD, Goldsmith M, Ashani Y, Simo Y, Mullokandov G, Bar H, Ben-David M, Leader H, Margalit R, Silman I, Sussman JL, Tawfik DS. Directed evolution of hydrolases for prevention of G-type nerve agent intoxication. Nature Chemical Biology. 7: 120-5. PMID 21217689 DOI: 10.1038/nchembio.510  0.64
2010 Xu Y, Colletier JP, Weik M, Qin G, Jiang H, Silman I, Sussman JL. Long route or shortcut? A molecular dynamics study of traffic of thiocholine within the active-site gorge of acetylcholinesterase Biophysical Journal. 99: 4003-4011. PMID 21156143 DOI: 10.1016/j.bpj.2010.10.047  0.64
2010 Offman MN, Krol M, Silman I, Sussman JL, Futerman AH. Molecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370S Journal of Biological Chemistry. 285: 42105-42114. PMID 20980259 DOI: 10.1074/jbc.M110.172098  0.64
2010 Dvir H, Silman I, Harel M, Rosenberry TL, Sussman JL. Acetylcholinesterase: From 3D structure to function Chemico-Biological Interactions. 187: 10-22. PMID 20138030 DOI: 10.1016/j.cbi.2010.01.042  0.64
2010 Brumshtein B, Salinas P, Peterson B, Chan V, Silman I, Sussman JL, Savickas PJ, Robinson GS, Futerman AH. Characterization of gene-activated human acid-β-glucosidase: Crystal structure, glycan composition, and internalization into macrophages Glycobiology. 20: 24-32. PMID 19741058 DOI: 10.1093/glycob/cwp138  0.64
2009 Zeev-Ben-Mordehai T, Mylonas E, Paz A, Peleg Y, Toker L, Silman I, Svergun DI, Sussman JL. The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties. Biophysical Journal. 97: 2316-26. PMID 19843464 DOI: 10.1016/j.bpj.2009.07.045  0.36
2009 Sanson B, Nachon F, Colletier JP, Froment MT, Toker L, Greenblatt HM, Sussman JL, Ashani Y, Masson P, Silman I, Weik M. Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime Journal of Medicinal Chemistry. 52: 7593-7603. PMID 19642642 DOI: 10.1021/jm900433t  0.36
2009 Khersonsky O, Rosenblat M, Toker L, Yacobson S, Hugenmatter A, Silman I, Sussman JL, Aviram M, Tawfik DS. Directed evolution of serum paraoxonase PON3 by family shuffling and ancestor/consensus mutagenesis, and its biochemical characterization Biochemistry. 48: 6644-6654. PMID 19492856 DOI: 10.1021/bi900583y  0.36
2009 Brumshtein B, Aguilar-Moncayo M, García-Moreno IM, Mellet CO, Fernández JGM, Silman I, Shaaltiel Y, Aviezer D, Sussman JL, Futerman AH. 6-Amino-6-deoxy-5,6-di-N-(N′-octyliminomethylidene) nojirimycin: Synthesis, biological evaluation, and crystal structure in complex with acid β-glucosidase Chembiochem. 10: 1480-1485. PMID 19437524 DOI: 10.1002/cbic.200900142  0.64
2009 Paz A, Xie Q, Greenblatt HM, Fu W, Tang Y, Silman I, Qiu Z, Sussman JL. The crystal structure of a complex of acetylcholinesterase with a bis-(-)-nor-meptazinol derivative reveals disruption of the catalytic triad. Journal of Medicinal Chemistry. 52: 2543-9. PMID 19326912 DOI: 10.1021/jm801657v  0.64
2009 Zeev-Ben-Mordehai T, Paz A, Peleg Y, Toker L, Wolf SG, Rydberg EH, Sussman JL, Silman I. Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: over-expression, purification and biophysical characterization. Protein Expression and Purification. 63: 147-57. PMID 18938249 DOI: 10.1016/j.pep.2008.09.019  0.36
2008 Brumshtein B, Greenblatt HM, Futerman AH, Silman I, Sussman JL. Control of the rate of evaporation in protein crystallization by the 'microbatch under oil' method. Journal of Applied Crystallography. 41: 969-971. PMID 19461852 DOI: 10.1107/S0021889808024667  0.68
2008 Dunker AK, Silman I, Uversky VN, Sussman JL. Function and structure of inherently disordered proteins Current Opinion in Structural Biology. 18: 756-764. PMID 18952168 DOI: 10.1016/j.sbi.2008.10.002  0.64
2008 Kacher Y, Brumshtein B, Boldin-Adamsky S, Toker L, Shainskaya A, Silman I, Sussman JL, Futerman AH. Acid β-glucosidase: Insights from structural analysis and relevance to Gaucher disease therapy Biological Chemistry. 389: 1361-1369. PMID 18783340 DOI: 10.1515/BC.2008.163  0.36
2008 Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M. Shoot-and-trap: Use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography Proceedings of the National Academy of Sciences of the United States of America. 105: 11742-11747. PMID 18701720 DOI: 10.1073/pnas.0804828105  0.64
2008 Hodis E, Prilusky J, Martz E, Silman I, Moult J, Sussman JL. Proteopedia - A scientific 'wiki' bridging the rift between three-dimensional structure and function of biomacromolecules Genome Biology. 9. PMID 18673581 DOI: 10.1186/gb-2008-9-8-r121  0.64
2008 Silman I, Sussman JL. Acetylcholinesterase: How is structure related to function? Chemico-Biological Interactions. 175: 3-10. PMID 18586019 DOI: 10.1016/j.cbi.2008.05.035  0.64
2008 Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL. Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site Journal of the American Chemical Society. 130: 7856-7861. PMID 18512913 DOI: 10.1021/ja7109822  0.64
2008 Xu Y, Colletier JP, Weik M, Jiang H, Moult J, Silman I, Sussman JL. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics Biophysical Journal. 95: 2500-2511. PMID 18502801 DOI: 10.1529/biophysj.108.129601  0.64
2008 Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal. 95: 1928-44. PMID 18456828 DOI: 10.1529/biophysj.107.126995  0.64
2008 Xu Y, Colletier JP, Jiang H, Silman I, Sussman JL, Weik M. Induced-fit or preexisting equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase and implications for structure-based drug design Protein Science. 17: 601-605. PMID 18359854 DOI: 10.1110/ps.083453808  0.64
2008 Tsvetkov P, Asher G, Paz A, Reuven N, Sussman JL, Silman I, Shaul Y. Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome Proteins: Structure, Function and Genetics. 70: 1357-1366. PMID 17879262 DOI: 10.1002/prot.21614  0.64
2007 Colletier JP, Royant A, Specht A, Sanson B, Nachon F, Masson P, Zaccai G, Sussman JL, Goeldner M, Silman I, Bourgeois D, Weik M. Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography. Acta Crystallographica. Section D, Biological Crystallography. 63: 1115-28. PMID 18007027 DOI: 10.1107/S0907444907044472  0.64
2007 Banci L, Baumeister W, Heinemann U, Schneider G, Silman I, Stuart DI, Sussman JL. An idea whose time has come. Genome Biology. 8: 408. PMID 18001498 DOI: 10.1186/gb-2007-8-11-408  0.64
2007 Harel M, Brumshtein B, Meged R, Dvir H, Ravelli RBG, McCarthy A, Toker L, Silman I, Sussman JL. 3-D structure of serum paraoxonase 1 sheds light on its activity, stability, solubility and crystallizability Arhiv Za Higijenu Rada I Toksikologiju. 58: 347-353. PMID 17913690 DOI: 10.2478/v10004-007-0028-0  0.36
2007 Brumshtein B, Greenblatt HM, Butters TD, Shaaltiel Y, Aviezer D, Silman I, Futerman AH, Sussman JL. Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid β-glucosidase: Insights into the mechanism of chemical chaperone action in Gaucher disease Journal of Biological Chemistry. 282: 29052-29058. PMID 17666401 DOI: 10.1074/jbc.M705005200  0.64
2007 Felder CE, Prilusky J, Silman I, Sussman JL. A server and database for dipole moments of proteins. Nucleic Acids Research. 35: W512-21. PMID 17526523 DOI: 10.1093/nar/gkm307  0.68
2007 Shaaltiel Y, Bartfeld D, Hashmueli S, Baum G, Brill-Almon E, Galili G, Dym O, Boldin-Adamsky SA, Silman I, Sussman JL, Futerman AH, Aviezer D. Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system. Plant Biotechnology Journal. 5: 579-90. PMID 17524049 DOI: 10.1111/j.1467-7652.2007.00263.x  0.68
2007 Banci L, Baumeister W, Enfedaque J, Heinemann U, Schneider G, Silman I, Sussman JL. Structural proteomics: from the molecule to the system. Nature Structural & Molecular Biology. 14: 3-4. PMID 17203065 DOI: 10.1038/nsmb0107-3  0.64
2006 Brumshtein B, Wormald MR, Silman I, Futerman AH, Sussman JL. Structural comparison of differently glycosylated forms of acid-β-glucosidase, the defective enzyme in Gaucher disease Acta Crystallographica Section D: Biological Crystallography. 62: 1458-1465. PMID 17139081 DOI: 10.1107/S0907444906038303  0.64
2006 Rydberg EH, Brumshtein B, Greenblatt HM, Wong DM, Shaya D, Williams LD, Carlier PR, Pang YP, Silman I, Sussman JL. Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of Bis5-tacrine produces a dramatic rearrangement in the active-site gorge. Journal of Medicinal Chemistry. 49: 5491-500. PMID 16942022 DOI: 10.1021/jm060164b  0.64
2006 Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M. Structural insights into substrate traffic and inhibition in acetylcholinesterase Embo Journal. 25: 2746-2756. PMID 16763558 DOI: 10.1038/sj.emboj.7601175  0.64
2006 Sussman JL, Silman I. Shedding UV Light on the Phase Problem Structure. 14: 629-630. PMID 16615902 DOI: 10.1016/j.str.2006.03.004  0.64
2005 Niu C, Xu Y, Xu Y, Luo X, Duan W, Silman I, Sussman JL, Zhu W, Chen K, Shen J, Jiang H. Dynamic mechanism of E2020 binding to acetylcholinesterase: a steered molecular dynamics simulation. The Journal of Physical Chemistry. B. 109: 23730-8. PMID 16375354 DOI: 10.1021/jp0552877  0.68
2005 Harel M, Hyatt JL, Brumshtein B, Morton CL, Wadkins RM, Silman I, Sussman JL, Potter PM. The 3D structure of the anticancer prodrug CPT-11 with Torpedo californica acetylcholinesterase rationalizes its inhibitory action on AChE and its hydrolysis by butyrylcholinesterase and carboxylesterase Chemico-Biological Interactions. 157: 153-157. PMID 16289500 DOI: 10.1016/j.cbi.2005.10.016  0.64
2005 Hyatt JL, Tsurkan L, Morton CL, Yoon KJ, Harel M, Brumshtein B, Silman I, Sussman JL, Wadkins RM, Potter PM. Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11. Chemico-Biological Interactions. 157: 247-52. PMID 16257398 DOI: 10.1016/j.cbi.2005.10.033  0.64
2005 Albeck S, Burstein Y, Dym O, Jacobovitch Y, Levi N, Meged R, Michael Y, Peleg Y, Prilusky J, Schreiber G, Silman I, Unger T, Sussman JL. Three-dimensional structure determination of proteins related to human health in their functional context at the Israel Structural Proteomics Center (ISPC) Acta Crystallographica Section D: Biological Crystallography. 61: 1364-1372. PMID 16204888 DOI: 10.1107/S0907444905023565  0.64
2005 Haviv H, Wong DM, Greenblatt HM, Carlier PR, Pang YP, Silman I, Sussman JL. Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase Journal of the American Chemical Society. 127: 11029-11036. PMID 16076210 DOI: 10.1021/ja051765f  0.64
2005 Hasin Y, Avidan N, Bercovich D, Korczyn AD, Silman I, Beckmann JS, Sussman JL. Analysis of genetic polymorphisms in acetylcholinesterase as reflected in different populations. Current Alzheimer Research. 2: 207-18. PMID 15974920 DOI: 10.2174/1567205053585909  0.64
2005 Prilusky J, Felder CE, Zeev-Ben-Mordehai T, Rydberg EH, Man O, Beckmann JS, Silman I, Sussman JL. FoldIndex©: A simple tool to predict whether a given protein sequence is intrinsically unfolded Bioinformatics. 21: 3435-3438. PMID 15955783 DOI: 10.1093/bioinformatics/bti537  0.64
2005 Silman I, Sussman JL. Acetylcholinesterase: 'Classical' and 'non-classical' functions and pharmacology Current Opinion in Pharmacology. 5: 293-302. PMID 15907917 DOI: 10.1016/j.coph.2005.01.014  0.64
2005 Premkumar L, Sawkar AR, Boldin-Adamsky S, Toker L, Silman I, Kelly JW, Futerman AH, Sussman JL. X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease. The Journal of Biological Chemistry. 280: 23815-9. PMID 15817452 DOI: 10.1074/jbc.M502799200  0.36
2005 Harel M, Hyatt JL, Brumshtein B, Morton CL, Yoon KJ, Wadkins RM, Silman I, Sussman JL, Potter PM. The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action. Molecular Pharmacology. 67: 1874-81. PMID 15772291 DOI: 10.1124/mol.104.009944  0.64
2004 Greenblatt HM, Guillou C, Guénard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL. The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design. Journal of the American Chemical Society. 126: 15405-11. PMID 15563167 DOI: 10.1021/ja0466154  0.64
2004 Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulié J, Silman I. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. The Embo Journal. 23: 4394-405. PMID 15526038 DOI: 10.1038/sj.emboj.7600425  0.64
2004 Hasin Y, Avidan N, Bercovich D, Korczyn A, Silman I, Beckmann JS, Sussman JL. A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene. Human Mutation. 24: 408-16. PMID 15459952 DOI: 10.1002/humu.20106  0.64
2004 Harel M, Aharoni A, Gaidukov L, Brumshtein B, Khersonsky O, Meged R, Dvir H, Ravelli RB, McCarthy A, Toker L, Silman I, Sussman JL, Tawfik DS. Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes. Nature Structural & Molecular Biology. 11: 412-9. PMID 15098021 DOI: 10.1038/nsmb767  0.36
2004 Futerman AH, Sussman JL, Horowitz M, Silman I, Zimran A. New directions in the treatment of Gaucher disease. Trends in Pharmacological Sciences. 25: 147-51. PMID 15019270 DOI: 10.1016/j.tips.2004.01.004  0.64
2004 Pe'er I, Felder CE, Man O, Silman I, Sussman JL, Beckmann JS. Proteomic signatures: amino acid and oligopeptide compositions differentiate among phyla. Proteins. 54: 20-40. PMID 14705021 DOI: 10.1002/prot.10559  0.64
2003 Xu Y, Shen J, Luo X, Silman I, Sussman JL, Chen K, Jiang H. How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations. Journal of the American Chemical Society. 125: 11340-9. PMID 16220957 DOI: 10.1021/ja029775t  0.64
2003 Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti S, Sussman JL. The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. Proteins. 53: 758-67. PMID 14579366 DOI: 10.1002/prot.10471  0.36
2003 Greenblatt HM, Dvir H, Silman I, Sussman JL. Acetylcholinesterase: a multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease. Journal of Molecular Neuroscience : Mn. 20: 369-83. PMID 14501022 DOI: 10.1385/JMN:20:3:369  0.64
2003 Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JL. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. Embo Reports. 4: 704-9. PMID 12792654 DOI: 10.1038/sj.embor.embor873  0.36
2003 Zeev-Ben-Mordehai T, Silman I, Sussman JL. Acetylcholinesterase in motion: Visualizing conformational changes in crystal structures by a morphing procedure Biopolymers. 68: 395-406. PMID 12601798 DOI: 10.1002/bip.10287  0.64
2003 Wong DM, Greenblatt HM, Dvir H, Carlier PR, Han YF, Pang YP, Silman I, Sussman JL. Acetylcholinesterase complexed with bivalent ligands related to huperzine a: experimental evidence for species-dependent protein-ligand complementarity. Journal of the American Chemical Society. 125: 363-73. PMID 12517147 DOI: 10.1021/ja021111w  0.64
2002 Weik M, Bergès J, Raves ML, Gros P, McSweeney S, Silman I, Sussman JL, Houée-Levin C, Ravelli RB. Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation. Journal of Synchrotron Radiation. 9: 342-6. PMID 12409620 DOI: 10.1107/S0909049502014589  0.64
2002 Felder CE, Harel M, Silman I, Sussman JL. Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase. Acta Crystallographica. Section D, Biological Crystallography. 58: 1765-71. PMID 12351819 DOI: 10.1107/S0907444902011642  0.64
2002 Koellner G, Steiner T, Millard CB, Silman I, Sussman JL. A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica. Journal of Molecular Biology. 320: 721-5. PMID 12095250 DOI: 10.1016/S0022-2836(02)00475-8  0.64
1973 Shinitzky M, Dudai Y, Silman I. Spectral evidence for the presence of tryptophan in the binding site of acetylcholinesterase. Febs Letters. 30: 125-128. PMID 11947075 DOI: 10.1016/0014-5793(73)80633-7  0.64
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