| Year |
Citation |
Score |
| 2023 |
Dym O, Aggarwal N, Ashani Y, Leader H, Albeck S, Unger T, Hamer-Rogotner S, Silman I, Tawfik DS, Sussman JL. The impact of molecular variants, crystallization conditions and the space group on ligand-protein complexes: a case study on bacterial phosphotriesterase. Acta Crystallographica. Section D, Structural Biology. 79: 992-1009. PMID 37860961 DOI: 10.1107/S2059798323007672 |
0.507 |
|
| 2023 |
Liu J, Yuan R, Shao W, Wang J, Silman I, Sussman JL. Do "Newly Born" orphan proteins resemble "Never Born" proteins? A study using three deep learning algorithms. Proteins. PMID 37092778 DOI: 10.1002/prot.26496 |
0.49 |
|
| 2023 |
Pokorna S, Khersonsky O, Lipsh-Sokolik R, Goldenzweig A, Nielsen R, Ashani Y, Peleg Y, Unger T, Albeck S, Dym O, Tirosh A, Tarayra R, Hocquemiller M, Laufer R, Ben-Dor S, ... Silman I, et al. Design of a stable human acid-β-glucosidase: towards improved Gaucher disease therapy and mutation classification. The Febs Journal. PMID 36808692 DOI: 10.1111/febs.16758 |
0.435 |
|
| 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 |
0.464 |
|
| 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 |
0.541 |
|
| 2020 |
Catto M, Pisani L, de la Mora E, Belviso BD, Mangiatordi GF, Pinto A, Palma A, Denora N, Caliandro R, Colletier JP, Silman I, Nicolotti O, Altomare CD. Chiral Separation, X-ray Structure, and Biological Evaluation of a Potent and Reversible Dual Binding Site AChE Inhibitor. Acs Medicinal Chemistry Letters. 11: 869-876. PMID 32435398 DOI: 10.1021/Acsmedchemlett.9B00656 |
0.388 |
|
| 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 |
0.587 |
|
| 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 |
0.731 |
|
| 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 |
0.514 |
|
| 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 |
0.562 |
|
| 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 |
0.51 |
|
| 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 |
0.776 |
|
| 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 |
0.524 |
|
| 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 |
0.554 |
|
| 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 |
0.456 |
|
| 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 |
0.526 |
|
| 2018 |
Galdeano C, Coquelle N, Cieslikiewicz-Bouet M, Bartolini M, Pérez B, Clos MV, Silman I, Jean L, Colletier JP, Renard PY, Muñoz-Torrero D. Increasing Polarity in Tacrine and Huprine Derivatives: Potent Anticholinesterase Agents for the Treatment of Myasthenia Gravis. Molecules (Basel, Switzerland). 23. PMID 29534488 DOI: 10.3390/Molecules23030634 |
0.31 |
|
| 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 |
0.561 |
|
| 2017 |
Silman I, Sussman JL. Recent developments in structural studies on acetylcholinesterase. Journal of Neurochemistry. PMID 28503857 DOI: 10.1111/Jnc.13992 |
0.591 |
|
| 2017 |
Sussman JL, Silman I. Recent breakthroughs in the structure/function studies of acetylcholinesterase Acta Crystallographica Section a Foundations and Advances. 73: C275-C275. DOI: 10.1107/S2053273317092981 |
0.53 |
|
| 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 |
0.558 |
|
| 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 |
0.518 |
|
| 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 |
0.562 |
|
| 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 |
0.543 |
|
| 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 |
0.55 |
|
| 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 |
0.476 |
|
| 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 |
0.37 |
|
| 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 |
0.557 |
|
| 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 |
0.494 |
|
| 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 |
0.573 |
|
| 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 |
0.552 |
|
| 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 |
0.612 |
|
| 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 |
0.493 |
|
| 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 |
0.481 |
|
| 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 |
0.546 |
|
| 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 |
0.577 |
|
| 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 |
0.522 |
|
| 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 |
0.527 |
|
| 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 |
0.5 |
|
| 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 |
0.323 |
|
| 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 |
0.541 |
|
| 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 |
0.585 |
|
| 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 |
0.488 |
|
| 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 |
0.602 |
|
| 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 |
0.582 |
|
| 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 |
0.712 |
|
| 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 |
0.764 |
|
| 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 |
0.552 |
|
| 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 |
0.523 |
|
| 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 |
0.512 |
|
| 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 |
0.612 |
|
| 2009 |
Gabel F, Masson P, Froment MT, Doctor BP, Saxena A, Silman I, Zaccai G, Weik M. Direct correlation between molecular dynamics and enzymatic stability: a comparative neutron scattering study of native human butyrylcholinesterase and its "aged" soman conjugate. Biophysical Journal. 96: 1489-94. PMID 19217865 DOI: 10.1016/J.Bpj.2008.10.029 |
0.312 |
|
| 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 |
0.402 |
|
| 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 |
0.756 |
|
| 2009 |
Sussman JL, Hodis E, Silman I, Moult J, Martz E, Prilusky J. Proteopedia: scientific wiki bridging 3D structure-function Acta Crystallographica Section a Foundations of Crystallography. 65: s39-s39. DOI: 10.1107/S0108767309099255 |
0.502 |
|
| 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 |
0.481 |
|
| 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 |
0.572 |
|
| 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 |
0.54 |
|
| 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 |
0.572 |
|
| 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 |
0.531 |
|
| 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 |
0.582 |
|
| 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 |
0.555 |
|
| 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 |
0.579 |
|
| 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 |
0.749 |
|
| 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 |
0.552 |
|
| 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 |
0.528 |
|
| 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 |
0.53 |
|
| 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 |
0.406 |
|
| 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 |
0.576 |
|
| 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 |
0.569 |
|
| 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 |
0.563 |
|
| 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 |
0.589 |
|
| 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 |
0.532 |
|
| 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 |
0.545 |
|
| 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 |
0.571 |
|
| 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 |
0.544 |
|
| 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 |
0.422 |
|
| 2007 |
Sanson B, Nachon F, Colletier J, Silman I, Sussman JL, Masson P, Weik M. Crystal structures of conjugates of soman withTcAChE Acta Crystallographica Section a Foundations of Crystallography. 63: s122-s123. DOI: 10.1107/S0108767307097334 |
0.501 |
|
| 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 |
0.425 |
|
| 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 |
0.591 |
|
| 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 |
0.518 |
|
| 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 |
0.552 |
|
| 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 |
0.496 |
|
| 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 |
0.589 |
|
| 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 |
0.522 |
|
| 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 |
0.479 |
|
| 2006 |
Peleg Y, Albeck S, Burstein Y, Dym O, Jacobovitch Y, Levy N, Meged R, Michael Y, Prilusky J, Schreiber G, Silman I, Unger T, Sussman JL. Microbial Cell Factories. 5: P40. DOI: 10.1186/1475-2859-5-S1-P40 |
0.545 |
|
| 2006 |
Sussman J, Aharoni A, Harel M, Gaidukov L, Brumshtein B, Khersonsky O, Yagur S, Toker L, Silman I, Tawfik D. 3D structure of mammalian paraoxonase at 2.2Å resolution Toxicology Letters. 164: S9. DOI: 10.1016/J.Toxlet.2006.06.024 |
0.511 |
|
| 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 |
0.516 |
|
| 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 |
0.592 |
|
| 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 |
0.531 |
|
| 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 |
0.552 |
|
| 2005 |
Gabel F, Weik M, Masson P, Renault F, Fournier D, Brochier L, Doctor BP, Saxena A, Silman I, Zaccai G. Effects of soman inhibition and of structural differences on cholinesterase molecular dynamics: a neutron scattering study. Biophysical Journal. 89: 3303-11. PMID 16100272 DOI: 10.1529/Biophysj.105.061028 |
0.376 |
|
| 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 |
0.587 |
|
| 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 |
0.505 |
|
| 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 |
0.741 |
|
| 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 |
0.542 |
|
| 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 |
0.514 |
|
| 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 |
0.589 |
|
| 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 |
0.409 |
|
| 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 |
0.613 |
|
| 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 |
0.553 |
|
| 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 |
0.492 |
|
| 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 |
0.542 |
|
| 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 |
0.493 |
|
| 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 |
0.466 |
|
| 2004 |
Aharoni A, Gaidukov L, Yagur S, Toker L, Silman I, Tawfik DS. Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. Proceedings of the National Academy of Sciences of the United States of America. 101: 482-7. PMID 14695884 DOI: 10.1073/Pnas.2536901100 |
0.348 |
|
| 2004 |
Colletier JP, Royant A, Specht A, Nachon F, Zaccai G, Goeldner M, Sussman JL, Silman I, Bourgeois D, Weik M. Kinetic crystallography on cholinesterases Acta Crystallographica Section a Foundations of Crystallography. 60: s122-s122. DOI: 10.1107/S0108767304097594 |
0.492 |
|
| 2004 |
Harel M, Aharoni A, Gaidukov L, Brumshtein B, Khersonsky O, Meged R, Dvir H, Ravelli RBG, McCarthy A, Toker L, Silman I, Sussman JL, Tawfik DS. Erratum: Corrigendum: Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes Nature Structural & Molecular Biology. 11: 1253-1253. DOI: 10.1038/Nsmb1204-1253A |
0.55 |
|
| 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 |
0.494 |
|
| 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 |
0.54 |
|
| 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 |
0.757 |
|
| 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 |
0.56 |
|
| 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 |
0.309 |
|
| 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 |
0.543 |
|
| 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 |
0.752 |
|
| 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 |
0.571 |
|
| 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 |
0.466 |
|
| 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 |
0.56 |
|
| 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+ |
0.584 |
|
| 2002 |
Shin I, Wachtel E, Roth E, Bon C, Silman I, Weiner L. Thermal denaturation of Bungarus fasciatus acetylcholinesterase: Is aggregation a driving force in protein unfolding? Protein Science : a Publication of the Protein Society. 11: 2022-32. PMID 12142456 DOI: 10.1110/Ps.0205102 |
0.306 |
|
| 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 |
0.578 |
|
| 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 |
0.508 |
|
| 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 |
0.58 |
|
| 2002 |
Weik M, Ravelli RBG, Silman I, Sussman JL, Gros P, Kroon J. Radiation damage to proteins studied by temperature-controlled cryo-crystallography Acta Crystallographica Section a Foundations of Crystallography. 58: c202-c202. DOI: 10.1107/S0108767302093078 |
0.467 |
|
| 2002 |
Dvir H, Wong DM, Harel M, Jiang HL, Rosenberry TL, Luque FJ, Camps P, Silman I, Sussman JL. 3D structures of Acetylcholinesterase complexes with potential drugs for the treatment of Alzheimer's disease Acta Crystallographica Section a Foundations of Crystallography. 58: c138-c138. DOI: 10.1107/S0108767302090542 |
0.509 |
|
| 2002 |
Jiang H, Shen J, Luo X, Liu H, Chen F, Tan X, Shen J, Chen K, Silman I, Sussman JL. Structure-based high throughput virtual screening for drug discovery Acta Crystallographica Section a Foundations of Crystallography. 58: c67-c67. DOI: 10.1107/S0108767302087706 |
0.486 |
|
| 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 |
0.529 |
|
| 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 |
0.537 |
|
| 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 |
0.554 |
|
| 2001 |
Nicolas A, Ferron F, Toker L, Sussman JL, Silman I. Histochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase. Acta Crystallographica. Section D, Biological Crystallography. 57: 1348-50. PMID 11526341 DOI: 10.1107/S0907444901010411 |
0.532 |
|
| 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 |
0.319 |
|
| 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 |
0.441 |
|
| 2001 |
Liu T, Gu J, Tan X, Zhu W, Luo X, Jiang H, Ji R, Chen K, Silman I, Sussman JL. Theoretical Insight into the Interactions of TMA-Benzene and TMA-Pyrrole with B3LYP Density-Functional Theory (DFT) and ab Initio Second Order Møller−Plesset Perturbation Theory (MP2) Calculations The Journal of Physical Chemistry A. 105: 5431-5437. DOI: 10.1021/JP003098C |
0.379 |
|
| 2001 |
Liu T, Gu J, Tan XJ, Zhu WL, Luo XM, Jiang HL, Ji RY, Chen KX, Silman I, Sussman JL. Theoretical insight into the interactions of TMA-benzene and TMA-pyrrole with B3LYP Density-Functional Theory (DFT) and ab initio second order Møller-Plesset perturbation theory (MP2) calculations Journal of Physical Chemistry A. 105: 5431-5437. DOI: 10.1021/Jp003098C |
0.507 |
|
| 2001 |
Felder C, Jiang H, Zhu W, Chen K, Silman I, Botti SA, Sussman JL. Quantum/Classical Mechanical Comparison of Cation−π Interactions between Tetramethylammonium and Benzene The Journal of Physical Chemistry A. 105: 1326-1333. DOI: 10.1021/JP002933N |
0.376 |
|
| 2001 |
Felder C, Jiang HL, Zhu WL, Chen KX, Silman I, Bottijt SA, Sussman JL. Quantum/classical mechanical comparison of cation-π interactions between tetramethylammonium and benzene Journal of Physical Chemistry A. 105: 1326-1333. DOI: 10.1021/Jp002933N |
0.492 |
|
| 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 |
0.49 |
|
| 2000 |
Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL. Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II Acta Crystallographica Section D: Biological Crystallography. 56: 1385-1394. PMID 11053835 DOI: 10.1107/S0907444900010659 |
0.584 |
|
| 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 |
0.613 |
|
| 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 |
0.539 |
|
| 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 |
0.489 |
|
| 2000 |
Arnon R, Silman I, Tarrab-Hazdai R. Acetylcholinesterase of Schistosoma mansoni--functional correlates. Contributed in honor of Professor Hans Neurath's 90th birthday. Protein Science : a Publication of the Protein Society. 8: 2553-61. PMID 10631970 DOI: 10.1110/Ps.8.12.2553 |
0.37 |
|
| 2000 |
Weik M, Gros P, Kroon J, Ursby T, Bourgeois D, Ravelli R, McSweeney S, Peng L, Specht A, Goeldner M, Kryger G, Silman I, Sussman J. Temperature-controlled crystallographic experiments on acetylcholinesterase Acta Crystallographica Section a Foundations of Crystallography. 56: s255-s255. DOI: 10.1107/S0108767300025472 |
0.442 |
|
| 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 |
0.505 |
|
| 2000 |
Greenblatt HM, Silman I, Sussman JL. Structural studies on vertebrate and invertebrate acetylcholinesterases and their complexes with functional ligands Drug Development Research. 50: 573-583. DOI: 10.1002/1098-2299(200007/08)50:3/4<573::AID-DDR41>3.0.CO;2-7 |
0.46 |
|
| 2000 |
Greenblatt HM, Silman I, Sussman JL. Structural studies on vertebrate and invertebrate acetylcholinesterases and their complexes with functional ligands Drug Development Research. 50: 573-583. DOI: 10.1002/1098-2299(200007/08)50:3/4<573::Aid-Ddr41>3.0.Co;2-7 |
0.581 |
|
| 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 |
0.57 |
|
| 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 |
0.534 |
|
| 1999 |
Weiner L, Roth E, Mazur Y, Silman I. Targeted cross-linking of a molten globule form of acetylcholinesterase by the virucidal agent hypericin. Biochemistry. 38: 11401-5. PMID 10471290 DOI: 10.1021/Bi991147+ |
0.326 |
|
| 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 |
0.614 |
|
| 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 |
0.543 |
|
| 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 |
0.587 |
|
| 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 |
0.508 |
|
| 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 |
0.505 |
|
| 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 |
0.577 |
|
| 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 |
0.582 |
|
| 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 |
0.552 |
|
| 1998 |
Shin I, Silman I, Bon C, Weiner L. Liposome-catalyzed unfolding of acetylcholinesterase from Bungarus fasciatus. Biochemistry. 37: 4310-6. PMID 9556345 DOI: 10.1021/Bi973005Q |
0.328 |
|
| 1998 |
Botti S, Felder C, Sussman J, Silman I. Electrostatic homology modelling of a set of ChE-like neural adhesion proteins identifies a shared ‘annular’ motif with ChEs. Structural implications for a cell-recognition role of ChEs Journal of Physiology-Paris. 92: 414-416. DOI: 10.1016/S0928-4257(99)80027-8 |
0.524 |
|
| 1998 |
Bar-On P, Harel M, Millard C, Enz A, Sussman J, Silman I. Kinetic and structural studies on the interaction of the anti-Alzheimer drug, ENA-713, with Torpedo californica acetylcholinesterase Journal of Physiology-Paris. 92: 406-407. DOI: 10.1016/S0928-4257(99)80019-9 |
0.52 |
|
| 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 |
0.563 |
|
| 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 |
0.61 |
|
| 1997 |
Giles K, Silman I, Sussman J. Human acetylcholinesterase II: In vivo expression and tissue distribution via est analyses Neuroscience Letters. 237: S19-S20. DOI: 10.1016/S0304-3940(97)90079-3 |
0.447 |
|
| 1997 |
Giles K, Sussman J, Silman I. Human acetylcholinesterase I: In vitro assembly of subunits Neuroscience Letters. 237: S19. DOI: 10.1016/S0304-3940(97)90078-1 |
0.467 |
|
| 1997 |
Botti S, Felder C, Lifson S, Silman I, Sussman J. An integrated model for the molecular traffic through the active site of cholinesterases Neuroscience Letters. 237: S11. DOI: 10.1016/S0304-3940(97)90044-6 |
0.531 |
|
| 1997 |
Botti S, Felder C, Sussman J, Silman I. The conjuction of a conserved electrostatic motif and a common cholinesterase fold defines a class of adhesion proteins Neuroscience Letters. 237: S11. DOI: 10.1016/S0304-3940(97)90043-4 |
0.564 |
|
| 1997 |
Bar-On P, Millard C, Enz A, Sussman J, Silman I. Evidence that the anti-Alzheimer drug, ENA-713, inhibits acetylcholinesterase by more than one mechanism Neuroscience Letters. 237: S6. DOI: 10.1016/S0304-3940(97)90026-4 |
0.468 |
|
| 1996 |
Porschke D, Créminon C, Cousin X, Bon C, Sussman J, Silman I. Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase. Biophysical Journal. 70: 1603-8. PMID 8785319 DOI: 10.1016/S0006-3495(96)79759-X |
0.529 |
|
| 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 |
0.375 |
|
| 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 |
0.561 |
|
| 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 |
0.57 |
|
| 1996 |
Raves ML, Ravelli RBG, Kroon J, Roth M, Bourgeois D, Peng L, Goeldner M, Silman I, Sussman JL. Laue studies on acetylcholinesterase Acta Crystallographica Section a Foundations of Crystallography. 52: C50-C50. DOI: 10.1107/S0108767396097048 |
0.487 |
|
| 1996 |
Harel M, Kleywegt GJ, Ravelli RBG, Silman I, Sussman JL. Structure and interactions of a complex of snake venom toxin and acetylcholinesterase Acta Crystallographica Section a Foundations of Crystallography. 52: C121-C121. DOI: 10.1107/S0108767396094329 |
0.541 |
|
| 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 |
0.567 |
|
| 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 |
0.563 |
|
| 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 |
0.306 |
|
| 1995 |
Eichler J, Silman I. The activity of an endoplasmic reticulum-localized pool of acetylcholinesterase is modulated by heat shock. The Journal of Biological Chemistry. 270: 4466-72. PMID 7876213 DOI: 10.1074/Jbc.270.9.4466 |
0.321 |
|
| 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 |
0.499 |
|
| 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 |
0.339 |
|
| 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 |
0.584 |
|
| 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 |
0.53 |
|
| 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 |
0.523 |
|
| 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 |
0.566 |
|
| 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 |
0.578 |
|
| 1993 |
Mehlert A, Silman I, Homans SW, Ferguson MA. The structure of the glycosylphosphatidylinositol anchor from Torpedo californica acetylcholinesterase. Biochemical Society Transactions. 21: 43S. PMID 8449327 DOI: 10.1042/Bst021043S |
0.357 |
|
| 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 |
0.556 |
|
| 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 |
0.614 |
|
| 1993 |
Massoulié J, Sussman J, Bon S, Silman I. Structure and functions of acetylcholinesterase and butyrylcholinesterase. Progress in Brain Research. 98: 139-46. PMID 8248501 DOI: 10.1016/S0079-6123(08)62391-2 |
0.577 |
|
| 1993 |
Dolginova EA, Roth E, Silman I, Weiner LM. Chemical modification of Torpedo acetylcholinesterase by disulfides: appearance of a "molten globule" state. Biochemistry. 31: 12248-54. PMID 1333796 DOI: 10.1021/Bi00163A039 |
0.386 |
|
| 1993 |
Harel M, Silman I, Sussman JL. Conversion of the three-dimensional structure of acetylcholinesterase to butyrylcholine-sterase: modeling and mutagenesis Acta Crystallographica Section a Foundations of Crystallography. 49: c99-c100. DOI: 10.1107/S0108767378097160 |
0.525 |
|
| 1993 |
Harel M, Silman I, Sussman JL. Quaternary ligand binding sites of acetylcholinesterase as revealed by X-ray crystallography Acta Crystallographica Section a Foundations of Crystallography. 49: c157-c157. DOI: 10.1107/S0108767378095501 |
0.508 |
|
| 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 |
0.577 |
|
| 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 |
0.338 |
|
| 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 |
0.565 |
|
| 1992 |
Sussman JL, Silman I. Acetylcholinesterase: Structure and use as a model for specific cation-protein interactions Current Biology. 2: 612. DOI: 10.1016/0960-9822(92)90176-B |
0.492 |
|
| 1992 |
Sussman JL, Silman I. Acetylcholinesterase: structure and use as a model for specific cation—protein interactions Current Opinion in Structural Biology. 2: 721-729. DOI: 10.1016/0960-9822(92)90176-B |
0.464 |
|
| 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 |
0.574 |
|
| 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 |
0.503 |
|
| 1991 |
Espinoza B, Silman I, Arnon R, Tarrab-Hazdai R. Phosphatidylinositol-specific phospholipase C induces biosynthesis of acetylcholinesterase via diacylglycerol in Schistosoma mansoni. European Journal of Biochemistry. 195: 863-70. PMID 1847873 DOI: 10.1111/J.1432-1033.1991.Tb15776.X |
0.32 |
|
| 1991 |
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science (New York, N.Y.). 253: 872-9. PMID 1678899 DOI: 10.1126/Science.1678899 |
0.599 |
|
| 1988 |
SILMAN I, FUTERMAN AH. Modes of attachment of acetylcholinesterase to the surface membrane European Journal of Biochemistry. 170: 11-22. PMID 3319614 DOI: 10.1111/J.1432-1033.1987.Tb13662.X |
0.332 |
|
| 1988 |
Espinoza B, Tarrab-Hazdai R, Silman I, Arnon R. Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol. Molecular and Biochemical Parasitology. 29: 171-9. PMID 3137466 DOI: 10.1016/0166-6851(88)90072-2 |
0.304 |
|
| 1988 |
Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I. Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C. Journal of Molecular Biology. 203: 821-3. PMID 2850366 DOI: 10.1016/0022-2836(88)90213-6 |
0.514 |
|
| 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 DOI: 10.1042/Bj2410615 |
0.327 |
|
| 1987 |
Silman I, Futerman AH. Posttranslational modification as a means of anchoring acetylcholinesterase to the cell surface Biopolymers - Peptide Science Section. 26. PMID 3555636 DOI: 10.1002/Bip.360260021 |
0.363 |
|
| 1986 |
Goldlust A, Arnon R, Silman I, Tarrab-Hazdai R. Acetylcholinesterase of Schistosoma mansoni: purification and characterization. Journal of Neuroscience Research. 15: 569-81. PMID 3723610 DOI: 10.1002/Jnr.490150413 |
0.369 |
|
| 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 |
0.311 |
|
| 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 DOI: 10.1042/Bj2260369 |
0.347 |
|
| 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 |
0.31 |
|
| 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 |
0.336 |
|
| 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 |
0.352 |
|
| 1977 |
Aharonov A, Tarrab-Hazdai R, Silman I, Fuchs S. Immunochemical studies on acetylcholine receptor from Torpedo californica. Immunochemistry. 14: 129-37. PMID 67081 DOI: 10.1016/0019-2791(77)90291-9 |
0.312 |
|
| 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 |
0.343 |
|
| 1976 |
Silman I. Molecular structure of acetylcholinesterase Trends in Biochemical Sciences. 1: 225-227. DOI: 10.1016/S0968-0004(76)80096-5 |
0.381 |
|
| 1975 |
Fuchs S, Gurari D, Silman I. Chemical modification of electric eel acetylcholinesterase by tetranitromethane. Archives of Biochemistry and Biophysics. 165: 90-7. PMID 4441088 DOI: 10.1016/0003-9861(74)90145-3 |
0.315 |
|
| 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 |
0.322 |
|
| 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 |
0.321 |
|
| 1974 |
Gurari D, Silman I, Fuchs S. Immunochemical and enzymic properties of the electric eel acetylcholinesterase-antiacetylcholinesterase system. European Journal of Biochemistry. 43: 179-87. PMID 4134781 DOI: 10.1111/J.1432-1033.1974.Tb03398.X |
0.314 |
|
| 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 |
0.315 |
|
| 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 |
0.344 |
|
| 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 |
0.311 |
|
| 1969 |
Silman I. Microenvironmental Effects on Enzyme Activity The Journal of General Physiology. 54: 50-57. DOI: 10.1085/Jgp.54.1.50 |
0.312 |
|
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