Israel Silman - Publications

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

201 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
2021 Silman I, Shnyrov VL, Ashani Y, Roth E, Nicolas A, Sussman JL, Weiner L. Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif. Protein Science : a Publication of the Protein Society. PMID 33686648 DOI: 10.1002/pro.4061  0.84
2020 Viayna E, Coquelle N, Cieslikiewicz-Bouet M, Cisternas P, Oliva CA, Sánchez-López E, Ettcheto M, Bartolini M, De Simone A, Ricchini M, Rendina M, Pons M, Firuzi O, Pérez B, Saso L, ... ... Silman I, et al. Discovery of a Potent Dual Inhibitor of Acetylcholinesterase and Butyrylcholinesterase with Antioxidant Activity that Alleviates Alzheimer-like Pathology in Old APP/PS1 Mice. Journal of Medicinal Chemistry. PMID 33356266 DOI: 10.1021/acs.jmedchem.0c01775  0.48
2020 Sussman JL, Silman I. Computational studies on cholinesterases: Strengthening our understanding of the integration of structure, dynamics and function. Neuropharmacology. 179: 108265. PMID 32795461 DOI: 10.1016/J.Neuropharm.2020.108265  0.84
2020 Nachon F, Rosenberry TL, Silman I, Sussman JL. A Second Look at the Crystal Structures of Acetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and the Design of Specific Insecticides. Molecules (Basel, Switzerland). 25. PMID 32155891 DOI: 10.3390/Molecules25051198  0.84
2020 Toker L, Silman I, Zeev-Ben-Mordehai T, Sussman JL, Schopfer LM, Lockridge O. Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers. Chemico-Biological Interactions. 109007. PMID 32087110 DOI: 10.1016/J.Cbi.2020.109007  0.84
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  0.84
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  0.84
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  0.84
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  0.84
2018 Lalut J, Santoni G, Karila D, Lecoutey C, Davis A, Nachon F, Silman I, Sussman J, Weik M, Maurice T, Dallemagne P, Rochais C. Novel multitarget-directed ligands targeting acetylcholinesterase and σ receptors as lead compounds for treatment of Alzheimer's disease: Synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase. European Journal of Medicinal Chemistry. 162: 234-248. PMID 30447434 DOI: 10.1016/J.Ejmech.2018.10.064  0.48
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  0.84
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  0.84
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  0.84
2018 Bilkis I, Silman I, Weiner L. Generation of Reactive Oxygen Species by Photosensitizers and their Modes of Action on Proteins. Current Medicinal Chemistry. PMID 29303072 DOI: 10.2174/0929867325666180104153848  0.48
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  0.84
2017 Silman I, Sussman JL. Recent developments in structural studies on acetylcholinesterase. Journal of Neurochemistry. PMID 28503857 DOI: 10.1111/Jnc.13992  0.84
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2013 Offman MN, Silman I, Sussman JL, Futerman AH. Crystal structure of the enzyme acid b-glucosidase Advances in Gaucher Disease: Basic and Clinical Perspectives. 125-138. DOI: 10.2217/EBO.12.215  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2011 Weiner L, Roth E, Silman I. Targeted oxidation of Torpedo californica acetylcholinesterase by singlet oxygen. Photochemistry and Photobiology. 87: 308-16. PMID 21155827 DOI: 10.1111/J.1751-1097.2010.00857.X  0.48
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  0.72
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  0.72
2010 Ashani Y, Gupta RD, Goldsmith M, Silman I, Sussman JL, Tawfik DS, Leader H. Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers. Chemico-Biological Interactions. 187: 362-9. PMID 20303930 DOI: 10.1016/J.Cbi.2010.02.039  0.72
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  0.72
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  0.72
2010 Paz A, Zeev-Ben-Mordehai T, Sussman JL, Silman I. Purification of Intrinsically Disordered Proteins Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation. 695-704. DOI: 10.1002/9780470602614.ch24  0.72
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 Sharabi O, Peleg Y, Mashiach E, Vardy E, Ashani Y, Simian I, Sussman JL, Shifman JM. Design, expression and characterization of mutants of fasciculin optimized for interaction with its target, acetylcholinesterase Protein Engineering, Design and Selection. 22: 641-648. PMID 19643977 DOI: 10.1093/Protein/Gzp045  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  0.72
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  0.72
2009 Weiner L, Shnyrov VL, Konstantinovskii L, Roth E, Ashani Y, Silman I. Stabilization of Torpedo californica acetylcholinesterase by reversible inhibitors. Biochemistry. 48: 563-74. PMID 19115961 DOI: 10.1021/Bi801196Y  0.48
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  0.84
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2008 Tompa P, Prilusky J, Silman I, Sussman JL. Structural disorder serves as a weak signal for intracellular protein degradation Proteins: Structure, Function and Genetics. 71: 903-909. PMID 18004785 DOI: 10.1002/Prot.21773  0.72
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  0.72
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. DOI: 10.1107/S0021889808024667  0.72
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  0.72
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  0.72
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  0.72
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  0.84
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  0.84
2007 Haviv H, Wong DM, Silman I, Sussman JL. Bivalent ligands derived from Huperzine A as acetylcholinesterase inhibitors Current Topics in Medicinal Chemistry. 7: 375-387. PMID 17305579 DOI: 10.2174/156802607779941215  0.72
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  0.72
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: 579-590. DOI: 10.1111/j.1467-7652.2007.00263.x  0.72
2007 Felder CE, Prilusky J, Silman I, Sussman JL. A server and database for dipole moments of proteins Nucleic Acids Research. 35: W512-W521. DOI: 10.1093/nar/gkm307  0.72
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  0.72
2006 Esnouf RM, Hamer R, Sussman JL, Silman I, Trudgian D, Yang ZR, Prilusky J. Honing the in silico toolkit for detecting protein disorder Acta Crystallographica Section D: Biological Crystallography. 62: 1260-1266. PMID 17001103 DOI: 10.1107/S0907444906033580  0.72
2006 Banci L, Bertini I, Cusack S, de Jong RN, Heinemann U, Jones EY, Kozielski F, Maskos K, Messerschmidt A, Owens R, Perrakis A, Poterszman A, Schneider G, Siebold C, Silman I, et al. First steps towards effective methods in exploiting high-throughput technologies for the determination of human protein structures of high biomedical value. Acta Crystallographica. Section D, Biological Crystallography. 62: 1208-17. PMID 17001097 DOI: 10.1107/S0907444906029350  0.72
2006 Albeck S, Alzari P, Andreini C, Banci L, Berry IM, Bertini I, Cambillau C, Canard B, Carter L, Cohen SX, Diprose JM, Dym O, Esnouf RM, Felder C, Ferron F, ... ... Silman I, et al. SPINE bioinformatics and data-management aspects of high-throughput structural biology. Acta Crystallographica. Section D, Biological Crystallography. 62: 1184-95. PMID 17001095 DOI: 10.1107/S090744490602991X  0.72
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  0.72
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  0.72
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  0.72
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  0.84
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2005 Parnas H, Slutsky I, Rashkovan G, Silman I, Wess J, Parnas I. Depolarization initiates phasic acetylcholine release by relief of a tonic block imposed by presynaptic M2 muscarinic receptors. Journal of Neurophysiology. 93: 3257-69. PMID 15703226 DOI: 10.1152/jn.01131.2004  0.72
2005 Niu C, 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 Journal of Physical Chemistry B. 109: 23730-23738. DOI: 10.1021/jp0552877  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2004 Liu T, Zhu W, Gu J, Shen J, Luo X, Chen G, Puah CM, Silman I, Chen K, Sussman JL, Jiang H. Additivity of cation-π interactions: An ab initio computational study on π- Cation-π sandwich complexes Journal of Physical Chemistry A. 108: 9400-9405. DOI: 10.1021/jp0476850  0.72
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  0.72
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  0.72
2003 Millard CB, Shnyrov VL, Newstead S, Shin I, Roth E, Silman I, Weiner L. Stabilization of a metastable state of Torpedo californica acetylcholinesterase by chemical chaperones. Protein Science : a Publication of the Protein Society. 12: 2337-47. PMID 14500892 DOI: 10.1110/Ps.03110703  0.48
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  0.72
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  0.72
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  0.72
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  0.72
2002 Dvir H, Jiang HL, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL. X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement. Biochemistry. 41: 10810-8. PMID 12196020 DOI: 10.1021/Bi020151+  0.72
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  0.72
2002 Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I. Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine Biochemistry. 41: 3555-3564. PMID 11888271 DOI: 10.1021/Bi020016X  0.72
2002 Dvir H, Wong DM, Harel M, Barril X, Orozco M, Luque FJ, Muñoz-Torrero D, Camps P, Rosenberry TL, Silman I, Sussman JL. 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates. Biochemistry. 41: 2970-81. PMID 11863435 DOI: 10.1021/Bi011652I  0.72
2002 Liu T, Sussman JL, Gu J, Tan XJ, Zhu WL, Luo XM, Jiang HL, Ji RY, Chen KX, Silman I. The relationship between binding models of TMA with furan and imidazole and the molecular electrostatic potentials: DFT and MP2 computational studies Journal of Physical Chemistry A. 106: 157-164. DOI: 10.1021/Jp0113275  0.72
2001 Slutsky I, Silman I, Parnas I, Parnas H. Presynaptic M(2) muscarinic receptors are involved in controlling the kinetics of ACh release at the frog neuromuscular junction. The Journal of Physiology. 536: 717-25. PMID 11691867 DOI: 10.1111/j.1469-7793.2001.00717.x  0.72
2001 Weik M, Ravelli RB, Silman I, Sussman JL, Gros P, Kroon J. Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes. Protein Science : a Publication of the Protein Society. 10: 1953-61. PMID 11567086 DOI: 10.1110/Ps.09801  0.72
2001 Doucet-Personeni C, Bentley PD, Fletcher RJ, Kinkaid A, Kryger G, Pirard B, Taylor A, Taylor R, Taylor J, Viner R, Silman I, Sussman JL, Greenblatt HM, Lewis T. A structure-based design approach to the development of novel, reversible AChE inhibitors Journal of Medicinal Chemistry. 44: 3203-3215. PMID 11563919 DOI: 10.1021/Jm010826R  0.72
2001 De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry. 40: 10447-57. PMID 11523986 DOI: 10.1021/Bi0101392  0.72
2001 Weik M, Kryger G, Schreurs AM, Bouma B, Silman I, Sussman JL, Gros P, Kroon J. Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures. Acta Crystallographica. Section D, Biological Crystallography. 57: 566-73. PMID 11264586 DOI: 10.1107/S0907444901001196  0.72
2001 Jian Tan X, Liang Zhu W, Cui M, Min Luo X, De Gu J, Silman I, Sussman JL, Liang Jiang H, Yun Ji R, Xian Chen K. Noncovalent interaction or chemical bonding between alkaline earth cations and benzene? a quantum chemistry study using MP2 and density-functional theory methods Chemical Physics Letters. 349: 113-122. DOI: 10.1016/S0009-2614(01)01176-9  0.72
2000 Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL. Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors Protein Science. 9: 1063-1072. PMID 10892800 DOI: 10.1110/Ps.9.6.1063  0.72
2000 Koellner G, Kryger G, Millard CB, Silman I, Sussman JL, Steiner T. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica Journal of Molecular Biology. 296: 713-735. PMID 10669619 DOI: 10.1006/Jmbi.1999.3468  0.72
2000 Weik M, Ravelli RBG, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL. Specific chemical and structural damage to proteins produced by synchrotron radiation Proceedings of the National Academy of Sciences of the United States of America. 97: 623-628. PMID 10639129 DOI: 10.1073/Pnas.97.2.623  0.72
2000 Zhu WL, Tan XJ, Puah CM, Gu JD, Jiang HL, Chen KX, Felder CE, Silman I, Sussman JL. How does ammonium interact with aromatic groups? A density functional theory (DFT/B3LYP) investigation Journal of Physical Chemistry A. 104: 9573-9580. DOI: 10.1021/Jp001306V  0.72
1999 Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 Å resolution Febs Letters. 463: 321-326. PMID 10606746 DOI: 10.1016/S0014-5793(99)01637-3  0.72
1999 Botti SA, Felder CE, Lifson S, Sussman JL, Silman I. A modular treatment of molecular traffic through the active site of cholinesterase. Biophysical Journal. 77: 2430-50. PMID 10545346 DOI: 10.1016/S0006-3495(99)77080-3  0.72
1999 Silman I, Millard CB, Ordentlich A, Greenblatt HM, Harel M, Barak D, Shafferman A, Sussman JL. A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase Chemico-Biological Interactions. 119: 43-52. PMID 10421437 DOI: 10.1016/S0009-2797(99)00012-5  0.72
1999 Kryger G, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with E2020 (Ariceptρ): Implications for the design of new anti-Alzheimer drugs Structure. 7: 297-307. PMID 10368299 DOI: 10.1016/S0969-2126(99)80040-9  0.72
1999 Millard CB, Kryger G, Ordentlich A, Greenblatt HM, Harel M, Raves ML, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL. Crystal structures of aged phosphonylated acetylcholinesterase: Nerve agent reaction products at the atomic level Biochemistry. 38: 7032-7039. PMID 10353814 DOI: 10.1021/Bi982678L  0.72
1999 Morel N, Bon S, Greenblatt HM, Van Belle D, Wodak SJ, Sussman JL, Massoulié J, Silman I. Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase. Molecular Pharmacology. 55: 982-92. PMID 10347238 DOI: 10.1124/mol.55.6.982  0.72
1999 Millard CB, Koellner G, Ordentlich A, Shafferman A, Silman I, Sussman JL. Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad [7] Journal of the American Chemical Society. 121: 9883-9884. DOI: 10.1021/Ja992704I  0.72
1998 Ravelli RBG, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL. Static Laue diffraction studies on acetylcholinesterase Acta Crystallographica Section D: Biological Crystallography. 54: 1359-1366. PMID 10089512 DOI: 10.1107/S0907444998005277  0.72
1998 Kryger G, Silman I, Sussman JL. Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica Journal of Physiology Paris. 92: 191-194. PMID 9789806 DOI: 10.1016/S0928-4257(98)80008-9  0.72
1998 Botti SA, Felder CE, Sussman JL, Silman I. Electrotactins: A class of adhesion proteins with conserved electrostatic and structural motifs Protein Engineering. 11: 415-420. PMID 9725619 DOI: 10.1093/Protein/11.6.415  0.72
1997 Felder CE, Botti SA, Lifson S, Silman I, Sussman JL. External and internal electrostatic potentials of cholinesterase models. Journal of Molecular Graphics & Modelling. 15: 318-27, 335-7. PMID 9640563 DOI: 10.1016/S1093-3263(98)00005-9  0.72
1997 Shin I, Kreimer D, Silman I, Weiner L. Membrane-promoted unfolding of acetylcholinesterase: a possible mechanism for insertion into the lipid bilayer. Proceedings of the National Academy of Sciences of the United States of America. 94: 2848-52. PMID 9096309 DOI: 10.1073/Pnas.94.7.2848  0.48
1997 Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL. Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A Nature Structural Biology. 4: 57-63. PMID 8989325 DOI: 10.1038/Nsb0197-57  0.72
1996 Kreimer DI, Shin I, Shnyrov VL, Villar E, Silman I, Weiner L. Two partially unfolded states of Torpedo californica acetylcholinesterase. Protein Science : a Publication of the Protein Society. 5: 1852-64. PMID 8880909 DOI: 10.1002/Pro.5560050911  0.48
1996 Shin I, Silman I, Weiner LM. Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes Protein Science. 5: 42-51. PMID 8771195 DOI: 10.1002/Pro.5560050106  0.72
1996 Peng L, Silman I, Sussman J, Goeldner M. Biochemical evaluation of photolabile precursors of choline and of carbamylcholine for potential time-resolved crystallographic studies on cholinesterases. Biochemistry. 35: 10854-61. PMID 8718877 DOI: 10.1021/Bi9529014  0.72
1996 Faerman C, Ripoll D, Bon S, Le Feuvre Y, Morel N, Massoulié J, Sussman JL, Silman I. Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function. Febs Letters. 386: 65-71. PMID 8635606 DOI: 10.1016/0014-5793(96)00374-2  0.72
1996 Harel M, Quinn DM, Nair HK, Silman I, Sussman JL. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase Journal of the American Chemical Society. 118: 2340-2346. DOI: 10.1021/Ja952232H  0.72
1995 Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL. Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Structure (London, England : 1993). 3: 1355-66. PMID 8747462 DOI: 10.1016/S0969-2126(01)00273-8  0.72
1995 Kreimer DI, Shnyrov VL, Villar E, Silman I, Weiner L. Irreversible thermal denaturation of Torpedo californica acetylcholinesterase. Protein Science : a Publication of the Protein Society. 4: 2349-57. PMID 8563632 DOI: 10.1002/Pro.5560041113  0.48
1994 Gilson MK, Straatsma TP, McCammon JA, Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL. Open 'back door' in a molecular dynamics simulation of acetylcholinesterase Science. 263: 1276-1278. PMID 8122110 DOI: 10.1126/science.8122110  0.72
1994 Weiner L, Kreimer D, Roth E, Silman I. Oxidative stress transforms acetylcholinesterase to a molten-globule-like state. Biochemical and Biophysical Research Communications. 198: 915-22. PMID 8117296 DOI: 10.1006/Bbrc.1994.1130  0.48
1994 Axelsen PH, Harel M, Silman I, Sussman JL. Structure and dynamics of the active site gorge of acetylcholinesterase: Synergistic use of molecular dynamics simulation and X-ray crystallography Protein Science. 3: 188-197. PMID 8003956 DOI: 10.1002/Pro.5560030204  0.72
1994 Kreimer DI, Szosenfogel R, Goldfarb D, Silman I, Weiner L. Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 91: 12145-9. PMID 7991597 DOI: 10.1073/Pnas.91.25.12145  0.48
1994 Kreimer DI, Dolginova EA, Raves M, Sussman JL, Silman I, Weiner L. A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials. Biochemistry. 33: 14407-18. PMID 7981200 DOI: 10.1021/Bi00252A006  0.84
1994 Silman I, Harel M, Axelsen P, Raves M, Sussman JL. Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents Biochemical Society Transactions. 22: 745-749. PMID 7821677 DOI: 10.1042/Bst0220745  0.72
1993 Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL. An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proceedings of the National Academy of Sciences of the United States of America. 90: 5128-32. PMID 8506359 DOI: 10.1073/Pnas.90.11.5128  0.4
1993 Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Science : a Publication of the Protein Society. 2: 366-82. PMID 8453375 DOI: 10.1002/Pro.5560020309  0.84
1993 Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proceedings of the National Academy of Sciences of the United States of America. 90: 9031-5. PMID 8415649 DOI: 10.1073/Pnas.90.19.9031  0.72
1993 Sussman JL, Harel M, Silman I. Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs Chemico-Biological Interactions. 87: 187-197. PMID 8343975 DOI: 10.1016/0009-2797(93)90042-W  0.72
1992 Harel M, Sussman JL, Krejci E, Bon S, Chanal P, Massoulié J, Silman I. Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis. Proceedings of the National Academy of Sciences of the United States of America. 89: 10827-31. PMID 1438284 DOI: 10.1073/Pnas.89.22.10827  0.72
1992 Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J. The alpha/beta hydrolase fold. Protein Engineering. 5: 197-211. PMID 1409539 DOI: 10.1093/Protein/5.3.197  0.72
1992 Duval N, Bon S, Silman I, Sussman J, Massoulié J. Site-directed mutagenesis of active-site-related residues in Torpedo acetylcholinesterase. Presence of a glutamic acid in the catalytic triad. Febs Letters. 309: 421-3. PMID 1355448 DOI: 10.1016/0014-5793(92)80821-W  0.72
1992 Eichler J, Silman I, Anglister L. G2-acetylcholinesterase is presynaptically localized in Torpedo electric organ. Journal of Neurocytology. 21: 707-16. PMID 1331340 DOI: 10.1007/BF01181586  0.72
1991 Harel M, Su CT, Frolow F, Silman I, Sussman JL. Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products. Biochemistry. 30: 5217-25. PMID 2036388 DOI: 10.1021/Bi00235A015  0.84
1991 Harel M, Su CT, Frolow F, Ashani Y, Silman I, Sussman JL. Refined crystal structures of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin. Journal of Molecular Biology. 221: 909-18. PMID 1942036 DOI: 10.1016/0022-2836(91)80183-U  0.84
1990 Eichler J, Silman I, Gentry MK, Anglister L. Immunocytochemical localization of phosphatidylinositol-anchored acetylcholinesterase in excitable membranes of Torpedo ocellata. Brain Research. Molecular Brain Research. 8: 213-8. PMID 2170799 DOI: 10.1016/0169-328X(90)90019-A  0.72
1988 Inestrosa NC, Fuentes ME, Anglister L, Futerman AH, Silman I. A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C. Neuroscience Letters. 90: 186-90. PMID 3412641 DOI: 10.1016/0304-3940(88)90809-9  0.72
1988 SILMAN I, FUTERMAN AH. Modes of attachment of acetylcholinesterase to the surface membrane European Journal of Biochemistry. 170: 11-22. PMID 3319614  0.72
1988 Eghbali M, Silman I, Robinson TF, Seifter S. Visualization of collagenase-sensitive acetylcholinesterase in isolated cardiomyocytes and in heart tissue. Cell and Tissue Research. 253: 281-6. PMID 2842053 DOI: 10.1007/Bf00222282  0.72
1987 Low MG, Futerman AH, Ackermann KE, Sherman WR, Silman I. Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure Biochemical Journal. 241: 615-619. PMID 3593210  0.72
1987 Silman I, Futerman AH. Posttranslational modification as a means of anchoring acetylcholinesterase to the cell surface Biopolymers - Peptide Science Section. 26. PMID 3555636  0.72
1987 Futerman AH, Raviv D, Michaelson DM, Silman I. Differential susceptibility to phosphatidylinositol-specific phospholipase C of acetylcholinesterase in excitable tissues of embryonic and adult Torpedo ocellata Brain Research. 388: 105-112. PMID 3040164 DOI: 10.1016/0169-328X(87)90003-9  0.72
1986 Low MG, Ferguson MAJ, Futerman AH, Silman I. Covalently attached phosphatidylinositol as a hydrophobic anchor for membrane proteins Trends in Biochemical Sciences. 11: 212-215. DOI: 10.1016/0968-0004(86)90009-5  0.72
1985 Futerman AH, Low MG, Michaelson DM, Silman I. Solubilization of Membrane‐Bound Acetyicholinesterase by a Phosphatidylinositol‐Specific Phospholipase C Journal of Neurochemistry. 45: 1487-1494. PMID 4045459 DOI: 10.1111/j.1471-4159.1985.tb07217.x  0.72
1985 Futerman AH, Low MG, Ackermann KE, Sherman WR, Silman I. Identification of covalently bound inositol in the hydrophobic membrane-anchoring domain of Torpedo acetylcholinesterase Biochemical and Biophysical Research Communications. 129: 312-317. PMID 4004881 DOI: 10.1016/0006-291X(85)91439-1  0.72
1985 Barton PL, Futerman AH, Silman I. Arrhenius plots of acetylcholinesterase activity in mammalian erythrocytes and in Torpedo electric organ. Effect of solubilization by proteinases and by a phosphatidylinositol-specific phospholipase C Biochemical Journal. 231: 237-240. PMID 3904734  0.72
1985 Futerman AH, Fiorini RM, Roth E, Low MG, Silman I. Physicochemical behaviour and structural characteristics of membrane-bound acetylcholinesterase from Torpedo electric organ. Effect of phosphatidylinositol-specific phospholipase C Biochemical Journal. 226: 369-377. PMID 2986594  0.72
1984 Jedrzejczyk J, Silman I, Lai J, Barnard EA. Molecular forms of acetylcholinesterase in synaptic and extrasynaptic regions of avian tonic muscle. Neuroscience Letters. 46: 283-9. PMID 6738921 DOI: 10.1016/0304-3940(84)90113-7  0.72
1984 Razon N, Soreq H, Roth E, Bartal A, Silman I. Characterization of activities and forms of cholinesterases in human primary brain tumors. Experimental Neurology. 84: 681-95. PMID 6723888 DOI: 10.1016/0014-4886(84)90215-2  0.72
1983 Futerman AH, Low MG, Silman I. A hydrophobic dimer of acetylcholinesterase from Torpedo californica electric organ is solubilized by phosphatidylinositol-specific phospholipase C Neuroscience Letters. 40: 85-89. PMID 6633970 DOI: 10.1016/0304-3940(83)90097-6  0.72
1982 Amitai G, Ashani Y, Gafni A, Silman I. Novel pyrene-containing organophosphates as fluorescent probes for studying aging-induced conformational changes in organophosphate-inhibited acetylcholinesterase Biochemistry. 21: 2060-2069. PMID 7093230  0.72
1981 Ben-Barak J, Gazit H, Silman I, Dudai Y. In vivo modulation of the number of muscarinic receptors in rat brain by cholinergic ligands. European Journal of Pharmacology. 74: 73-81. PMID 7318895 DOI: 10.1016/0014-2999(81)90325-3  0.72
1980 Lyles JM, Barnard EA, Silman I. Changes in the levels and forms of cholinesterases in the blood plasma of normal and dystrophic chickens. Journal of Neurochemistry. 34: 978-87. PMID 7359144 DOI: 10.1111/j.1471-4159.1980.tb09674.x  0.72
1980 Amitai G, Ashani Y, Shahar A, Gafni A, Silman I. Fluorescent organophosphates: novel probes for studying aging-induced conformational changes in inhibited acetylcholinesterase and for localization of cholinesterase in nervous tissue Monographs in Neural Sciences. 7: 70-84. PMID 7015117  0.72
1980 Silman I, Anglister L. Electric eel acetylcholinesterase: a multisubunit enzyme containing a collagen tail. Monographs in Neural Sciences. 7: 55-69. PMID 6262636 DOI: 10.1159/000388814  0.72
1980 Amitai G, Ashani Y, Gafni A, Silman I. New fluorescent organophosphates as probes for studying aging-induced conformational changes in inhibited acetylcholinesterase Neurochemistry International. 2: 199-204. DOI: 10.1016/0197-0186(80)90025-X  0.72
1979 Gazit H, Silman I, Dudai Y. Administration of an organophosphate causes a decrease in muscarinic receptor levels in rat brain. Brain Research. 174: 351-6. PMID 487134 DOI: 10.1016/0006-8993(79)90861-8  0.72
1979 Lyles JM, Silman I, Barnard EA. Developmental changes in levels and forms of cholinesterases in muscles of normal and dystrophic chickens. Journal of Neurochemistry. 33: 727-38. PMID 479887 DOI: 10.1111/j.1471-4159.1979.tb05218.x  0.72
1979 Anglister L, Tarrab-Hazdai R, Fuchs S, Silman I. Immunological cross-reactivity between electric-eel acetylcholinesterase and rat-tail-tendon collagen. European Journal of Biochemistry / Febs. 94: 25-9. PMID 436842 DOI: 10.1111/j.1432-1033.1979.tb12867.x  0.72
1978 Silman I, Lyles JM, Barnard EA. Intrinsic forms of acetylcholinesterase in skeletal muscle. Febs Letters. 94: 166-70. PMID 700129 DOI: 10.1016/0014-5793(78)80929-6  0.72
1978 Anglister L, Silman I. Molecular structure of elongated forms of electric eel acetylcholinesterase. Journal of Molecular Biology. 125: 293-311. PMID 215774 DOI: 10.1016/0022-2836(78)90404-7  0.72
1977 Silman I, Dudai Y. Acetylcholinesterase: structure and activity of a membrane-bound enzyme. Advances in Biological and Medical Physics. 16: 223-34. PMID 45171 DOI: 10.1016/B978-0-12-005216-5.50019-0  0.72
1977 Wilson IB, Silman I. Effects of quaternary ligands on the inhibition of acetylcholinesterase by arsenite Biochemistry. 16: 2701-2708. PMID 19036 DOI: 10.1021/bi00631a018  0.72
1976 Anglister L, Rogozinski S, Silman I. Detection of hydroxyproline in preparations of acetylcholinesterase from the electric organ of the electric eel. Febs Letters. 69: 129-32. PMID 992021 DOI: 10.1016/0014-5793(76)80668-0  0.72
1976 Prives J, Silman I, Amsterdam A. Appearance and disappearance of acetycholine receptor during differentiation of chick skeletal muscle in vitro Cell. 7: 543-550. PMID 954086 DOI: 10.1016/0092-8674(76)90204-X  0.72
1975 Teichberg VI, Silman I, Beitsch DD, Resheff G. A beta-D-galactoside binding protein from electric organ tissue of Electrophorus electricus. Proceedings of the National Academy of Sciences of the United States of America. 72: 1383-7. PMID 1055413 DOI: 10.1073/Pnas.72.4.1383  0.72
1974 Dudai Y, Silman I. The molecular weight and subunit structure of acetylcholinesterase preparations from the electric organ of the electric eel. Biochemical and Biophysical Research Communications. 59: 117-24. PMID 4842295 DOI: 10.1016/S0006-291X(74)80182-8  0.72
1974 Dudai Y, Silman I. The effects of solubilization procedures on the release and molecular state of acetylcholinesterase from electric organ tissue. Journal of Neurochemistry. 23: 1177-87. PMID 4375706 DOI: 10.1111/j.1471-4159.1974.tb12215.x  0.72
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  0.72
1973 Ben-Haim D, Landau EM, Silman I. The role of a reactive disulphide bond in the function of the acetylcholine receptor at the frog neuromuscular junction. The Journal of Physiology. 234: 305-25. PMID 4767050 DOI: 10.1113/jphysiol.1973.sp010347  0.72
1973 Dudai Y, Herzberg M, Silman I. Molecular structures of acetylcholinesterase from electric organ tissue of the electric eel. Proceedings of the National Academy of Sciences of the United States of America. 70: 2473-6. PMID 4517659 DOI: 10.1073/pnas.70.9.2473  0.72
1973 Dudai Y, Silman I. The effect of Ca2+ on interaction of acetylcholinesterase with subcellular fractions of electric organ tissue from the electric eel Febs Letters. 30: 49-52. DOI: 10.1016/0014-5793(73)80616-7  0.72
1972 Dudai Y, Silman I, Kalderon N, Blumberg S. Purification by affinity chromatography of acetylcholinesterase from electric organ tissue of the electric eel subsequent to tryptic treatment. Biochimica Et Biophysica Acta. 268: 138-57. PMID 5018273 DOI: 10.1016/0005-2744(72)90208-2  0.72
1972 Dudai Y, Silman I, Shinitzky M, Blumberg S. Purification by affinity chromatography of the molecular forms of acetylcholinesterase present in fresh electric-organ tissue of electric eel. Proceedings of the National Academy of Sciences of the United States of America. 69: 2400-3. PMID 4506759 DOI: 10.1073/pnas.69.9.2400  0.72
1971 Dudai Y, Silman I. The subunits of an acetylcholinesterase preparation purified from trypsin-treated electric eel tissue. Febs Letters. 16: 324-328. PMID 11945972 DOI: 10.1016/0014-5793(71)80381-2  0.72
1970 Kalderon N, Silman I, Blumberg S, Dudai Y. A method for the purification of acetylcholinesterase by affinity chromatography. Biochimica Et Biophysica Acta. 207: 560-2. PMID 5452681 DOI: 10.1016/S0005-2795(70)80020-4  0.72
1969 Silman I, Karlin A. Acetylcholine receptor: covalent attachment of depolarizing groups at the active site. Science (New York, N.Y.). 164: 1420-1. PMID 5783718 DOI: 10.1126/science.164.3886.1420  0.72
Show low-probability matches.