Silman I, Shnyrov VL, Ashani Y, Roth E, Nicolas A, Sussman JL, Weiner L (2021)
Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif
Protein Science

Nachon F, Rosenberry TL, Silman I, Sussman JL (2020)
A Second Look at the Crystal Structures of Drosophila melanogaster Acetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and the Design of Specific Insecticides
Molecules 25: 1198

Sussman JL, Silman I (2020)
Computational studies on cholinesterases: Strengthening our understanding of the integration of structure, dynamics and function
Neuropharmacology

Toker L, Silman I, Zeev-Ben-Mordehai T, Sussman JL, Schopfer LM, Lockridge O (2020)
Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers
Chemico-Biological Interactions

Chandar NB, Efremenko I, Silman I, Martin JML, Sussman JL (2019)
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 310: 108715

Dighe SN, De la Mora E, Chan S, Kantham S, McColl G, Miles JA, Veliyath SK, Sreenivas BY, Nassar ZD, Silman I, Sussman JL, Weik M, McGeary RP, Parat MO, Brazzolotto X, Ross BP (2019)
Rivastigmine and metabolite analogues with putative Alzheimer's disease-modifying properties in a Caenorhabditis elegans model.
Communications chemistry 2: 35

Lalut J, Santoni G, Karila D, Lecoutey C, Davis A, Nachon F, Silman I, Sussman JL, Weik M, Maurice T, Dallemagne P, Rochais C (2019)
Novel multitarget-directed ligands targeting acetylcholinesterase and sigma1 receptors as lead compounds for treatment of Alzheimer's disease: Synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase
Eur Journal of Medicinal Chemistry 162: 234

Novichkova DA, Lushchekina SV, Dym O, Masson P, Silman I, Sussman JL (2019)
The four-helix bundle in cholinesterase dimers: Structural and energetic determinants of stability
Chemico-Biological Interactions 309: 108699

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, Colletier JP, Jean L, Routier S, Renard PY (2019)
Design, biological evaluation and X-ray crystallography of nanomolar multifunctional ligands targeting simultaneously acetylcholinesterase and glycogen synthase kinase-3
Eur Journal of Medicinal Chemistry 168: 58

Leung MR, van Bezouwen LS, Schopfer LM, Sussman JL, Silman I, Lockridge O, Zeev-Ben-Mordehai T (2018)
Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly
Proc Natl Acad Sci U S A 115: 13270

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 (2018)
Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents
Journal of Medicinal Chemistry 61: 7630

Zorbaz T, Braiki A, Marakovic N, Renou J, De la Mora E, Macek Hrvat N, Katalinic M, Silman I, Sussman JL, Mercey G, Gomez C, Mougeot R, Perez B, Baati R, Nachon F, Weik M, Jean L, Kovarik Z, Renard PY (2018)
Potent 3-Hydroxy-2-Pyridine Aldoxime Reactivators of Organophosphate-Inhibited Cholinesterases with Predicted Blood-Brain Barrier Penetration
Chemistry 24: 9675

Silman I, Sussman JL (2017)
Recent developments in structural studies on acetylcholinesterase
Journal of Neurochemistry 142 Suppl 2: 19

Xu Y, Cheng S, Sussman JL, Silman I, Jiang H (2017)
Computational Studies on Acetylcholinesterases
Molecules 22:

Ashani Y, Leader H, Aggarwal N, Silman I, Worek F, Sussman JL, Goldsmith M (2016)
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 259: 252

Dym O, Song W, Felder CE, Roth E, Shnyrov V, Ashani Y, Xu Y, Joosten RP, Weiner L, Sussman JL, Silman I (2016)
The Impact of Crystallization Conditions on Structure-Based Drug Design: A Case Study on the Methylene Blue/Acetylcholinesterase Complex
Protein Science 25: 1096

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, Fleishman SJ (2016)
Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability
Mol Cell 63: 337

Goldsmith M, Eckstein S, Ashani Y, Greisen P, Jr., Leader H, Sussman JL, Aggarwal N, Ovchinnikov S, Tawfik DS, Baker D, Thiermann H, Worek F (2016)
Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro
Archives of Toxicology 90: 2711

Wille T, Neumaier K, Koller M, Ehinger C, Aggarwal N, Ashani Y, Goldsmith M, Sussman JL, Tawfik DS, Thiermann H, Worek F (2016)
Single treatment of VX poisoned guinea pigs with the phosphotriesterase mutant C23AL: Intraosseous versus intravenous injection
Toxicol Lett 258: 198

Ben-David M, Sussman JL, Maxwell CI, Szeler K, Kamerlin SC, Tawfik DS (2015)
Catalytic stimulation by restrained active-site floppiness--the case of high density lipoprotein-bound serum paraoxonase-1
Journal of Molecular Biology 427: 1359

Worek F, Seeger T, Goldsmith M, Ashani Y, Leader H, Sussman JL, Tawfik DS, Thiermann H, Wille T (2014)
Efficacy of the rePON1 mutant IIG1 to prevent cyclosarin toxicity in vivo and to detoxify structurally different nerve agents in vitro
Archives of Toxicology 88: 1257

Worek F, Seeger T, Reiter G, Goldsmith M, Ashani Y, Leader H, Sussman JL, Aggarwal N, Thiermann H, Tawfik DS (2014)
Post-exposure treatment of VX poisoned guinea pigs with the engineered phosphotriesterase mutant C23: A proof-of-concept study
Toxicol Lett 231: 45

Ben-David M, Wieczorek G, Elias M, Silman I, Sussman JL, Tawfik DS (2013)
Catalytic metal ion rearrangements underline promiscuity and evolvability of a metalloenzyme
Journal of Molecular Biology 425: 1028

Silman I, Roth E, Paz A, Triquigneaux MM, Ehrenshaft M, Xu Y, Shnyrov VL, Sussman JL, Deterding LJ, Ashani Y, Mason RP, Weiner L (2013)
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

Acheampong MG, Dueno DE, Glover BK, Henry AA, Mata R, Vanbrakle ML, Westblade LF, Sussman JL, Granberry AL (2012)
Acetylcholinesterase: substrate traffic and inhibition
Biochem Mol Biol Educ 40: 144

Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS (2012)
Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1
Journal of Molecular Biology 418: 181

Goldsmith M, Ashani Y, Simo Y, Ben-David M, Leader H, Silman I, Sussman JL, Tawfik DS (2012)
Evolved stereoselective hydrolases for broad-spectrum G-type nerve agent detoxification
Chemical Biology 19: 456

Greenblatt HM, Otto TC, Kirkpatrick MG, Kovaleva E, Brown S, Buchman G, Cerasoli DM, Sussman JL (2012)
Structure of Recombinant Human Carboxylesterase 1 Isolated from Whole Cabbage Looper Larvae
Acta Crystallographica Sect F Struct Biol Cryst Commun F68: 269

Khare SD, Kipnis Y, Greisen P, Jr., Takeuchi R, Ashani Y, Goldsmith M, Song Y, Gallaher JL, Silman I, Leader H, Sussman JL, Stoddard BL, Tawfik DS, Baker D (2012)
Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis
Nat Chemical Biology 8: 294

Paz A, Roth E, Ashani Y, Xu Y, Shnyrov VL, Sussman JL, Silman I, Weiner L (2012)
Structural and functional characterization of the interaction of the photosensitizing probe methylene blue with Torpedo californica acetylcholinesterase
Protein Science 21: 1138

Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA (2012)
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
Biomol NMR Assign 6: 15

Ashani Y, Goldsmith M, Leader H, Silman I, Sussman JL, Tawfik DS (2011)
In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases
Toxicol Lett 206: 24

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 (2011)
Directed evolution of hydrolases for prevention of G-type nerve agent intoxication
Nat Chemical Biology 7: 120

Prilusky J, Hodis E, Canner D, Decatur WA, Oberholser K, Martz E, Berchanski A, Harel M, Sussman JL (2011)
Proteopedia: a status report on the collaborative, 3D web-encyclopedia of proteins and other biomolecules
J Struct Biol 175: 244

Sanson B, Colletier JP, Xu Y, Lang PT, Jiang H, Silman I, Sussman JL, Weik M (2011)
Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations
Protein Science 20: 1114

Ashani Y, Gupta RD, Goldsmith M, Silman I, Sussman JL, Tawfik DS, Leader H (2010)
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

Dvir H, Silman I, Harel M, Rosenberry TL, Sussman JL (2010)
Acetylcholinesterase: from 3D structure to function
Chemico-Biological Interactions 187: 10

Xu Y, Colletier JP, Weik M, Qin G, Jiang H, Silman I, Sussman JL (2010)
Long route or shortcut? A molecular dynamics study of traffic of thiocholine within the active-site gorge of acetylcholinesterase
Biophysical Journal 99: 4003

Khersonsky O, Rosenblat M, Toker L, Yacobson S, Hugenmatter A, Silman I, Sussman JL, Aviram M, Tawfik DS (2009)
Directed evolution of serum paraoxonase PON3 by family shuffling and ancestor/consensus mutagenesis, and its biochemical characterization
Biochemistry 48: 6644

Paz A, Xie Q, Greenblatt HM, Fu W, Tang Y, Silman I, Qiu Z, Sussman JL (2009)
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

Sanson B, Nachon F, Colletier JP, Froment MT, Toker L, Greenblatt HM, Sussman JL, Ashani Y, Masson P, Silman I, Weik M (2009)
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

Zeev-Ben-Mordehai T, Paz A, Peleg Y, Toker L, Wolf SG, Rydberg EH, Sussman JL, Silman I (2009)
Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: over-expression, purification and biophysical characterization
Protein Expr Purif 63: 147

Zeev-Ben-Mordehai T, Mylonas E, Paz A, Peleg Y, Toker L, Silman I, Svergun DI, Sussman JL (2009)
The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties
Biophysical Journal 97: 2316

Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M (2008)
Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography
Proc Natl Acad Sci U S A 105: 11742

Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL (2008)
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

Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I (2008)
Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3
Biophysical Journal 95: 1928

Silman I, Sussman JL (2008)
Acetylcholinesterase: how is structure related to function?
Chemico-Biological Interactions 175: 3

Xu Y, Colletier JP, Jiang H, Silman I, Sussman JL, Weik M (2008)
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

Xu Y, Colletier JP, Weik M, Jiang H, Moult J, Silman I, Sussman JL (2008)
Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics
Biophysical Journal 95: 2500

Colletier JP, Royant A, Specht A, Sanson B, Nachon F, Masson P, Zaccai G, Sussman JL, Goeldner M, Silman I, Bourgeois D, Weik M (2007)
Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography
Acta Crystallographica D Biol Crystallogr 63: 1115

Haviv H, Wong DM, Silman I, Sussman JL (2007)
Bivalent ligands derived from Huperzine A as acetylcholinesterase inhibitors
Curr Top Med Chem 7: 375

Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M (2006)
Structural insights into substrate traffic and inhibition in acetylcholinesterase
EMBO Journal 25: 2746

Rydberg EH, Brumshtein B, Greenblatt HM, Wong DM, Shaya D, Williams LD, Carlier PR, Pang YP, Silman I, Sussman JL (2006)
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

Harel M, Hyatt JL, Brumshtein B, Morton CL, Yoon KJ, Wadkins RM, Silman I, Sussman JL, Potter PM (2005)
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

Harel M, Hyatt JL, Brumshtein B, Morton CL, Wadkins RM, Silman I, Sussman JL, Potter PM (2005)
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 157-158: 153

Hasin Y, Avidan N, Bercovich D, Korczyn AD, Silman I, Beckmann JS, Sussman JL (2005)
Analysis of genetic polymorphisms in acetylcholinesterase as reflected in different populations
Curr Alzheimer Res 2: 207

Haviv H, Wong DM, Greenblatt HM, Carlier PR, Pang YP, Silman I, Sussman JL (2005)
Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase
Journal of the American Chemical Society 127: 11029

Hyatt JL, Tsurkan L, Morton CL, Yoon KJ, Harel M, Brumshtein B, Silman I, Sussman JL, Wadkins RM, Potter PM (2005)
Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11
Chemico-Biological Interactions 157-158: 247

Niu C, Xu Y, Luo X, Duan W, Silman I, Sussman JL, Zhu W, Chen K, Shen J, Jiang H (2005)
Dynamic mechanism of E2020 binding to acetylcholinesterase: a steered molecular dynamics simulation
J Phys Chem B 109: 23730

Silman I, Sussman JL (2005)
Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology
Curr Opin Pharmacol 5: 293

Colletier JP, Fournier D, Greenblatt HM, Sussman JL, Zaccai G, Silman I, Weik M (2004)
Poster (74) Structural studies on torpedo californica acetylcholinesterase in complex with a substrate analogue
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 359

Dvir H, Jiang H, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL (2004)
Poster (79) X-ray structures of TcAChE complexed with (+)-huperzine a and (-)-huperzine b: structural evidence for an active-site rearrangement
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 362

Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I (2004)
The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix
EMBO Journal 23: 4394

Fuchs S, Kasher R, Balass M, Scherf T, Harel M, Fridkin M, Sussman JL, Katchalski-Katzir E (2004)
The binding site for alpha-bungarotoxin in the acetylcholine receptor.
Cholinergic Mechanisms, CRC Press

Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti SA, Badet B, Thal C, Silman I, Sussman JL (2004)
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

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 (2004)
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes
Nat Struct Mol Biol 11: 412

Harel M, Dvir H, Bon S, Liu WQ, Garbay C, Sussman JL, Massoulie J, Silman I (2004)
Crystal structure of the tetramerization domain of acetylcholinesterase at 2.
Cholinergic Mechanisms, CRC Press

Harel M, Dvir H, Bon S, Liu WQ, Garbay C, Sussman JL, Massoulie J, Silman I (2004)
Poster (48) Crystal structure of the tetramerization domain of acetylcholinesterase reveals a model of the AChE tetramer
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 347

Hasin Y, Avidan N, Bercovich D, Korczyn A, Silman I, Beckmann JS, Sussman JL (2004)
A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene
Hum Mutat 24: 408

Rydberg EH, Macion R, Zeev-Ben-Mordehai T, Solomon A, Rees DM, Toker L, Botti SA, Auld VJ, Silman I, Sussman JL (2004)
Overexpression of the extracellular and cytoplasmic domains of the Drosophila adhesion protein, gliotactin.
Cholinergic Mechanisms, CRC Press

Silman I, Greenblatt HM, Zeev-Ben-Mordehai T, Sussman JL (2004)
Poster (47) Conformational plasticity of acetylcholinesterase
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 346

Sussman JL, Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Botti SA, Auld VJ, Silman I (2004)
Poster (31) Natively unstructured proteins: a case study of cholinesterase-like adhesion molecules (clams)
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 337

Toutant JP, Massoulie J, Fournier D, Marty JL, Schmid RD, Pfeiffer D, Selkirk ME, Sussman JL, Silman I, Talesa V, Wodak SJ, Stojan J, Magearu V (2004)
New biosensors for improved detection of environmental and food contamination by anticholinesterase pesticides
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 233

Toutant JP, Massoulie J, Fournier D, Schmid RD, Pfeiffer D, Selkirk ME, Sussman JL, Silman I, Talesa V, Wodak SJ (2004)
Poster (24) New biosensors for improved detection of environmental contamination by anticholinesterase pesticides
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 333

Zeev-Ben-Mordehai T, Silman I, Sussman JL (2004)
Use of the morphing graphics technique to visualize conformational differences between acetylcholinesterases from different species and inhibitor-induced conformational changes.
Cholinergic Mechanisms, CRC Press

Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Silman I, Sussman JL (2004)
Poster (104) Biophysical and bioinformatic analysis of the cytoplasmic portion of gliotactin
In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina: 375

Greenblatt HM, Dvir H, Silman I, Sussman JL (2003)
Acetylcholinesterase: a multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease
Journal of Molecular Neuroscience 20: 369

Wong DM, Greenblatt HM, Dvir H, Carlier PR, Han YF, Pang YP, Silman I, Sussman JL (2003)
Acetylcholinesterase Complexed with Bivalent Ligands Related to Huperzine A: Experimental Evidence for Species-Dependent Protein-Ligand Complementarity
J Am Chem Soc 125: 363

Xu Y, Shen J, Luo X, Silman I, Sussman JL, Chen K, Jiang H (2003)
How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations
Journal of the American Chemical Society 125: 11340

Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti SA, Sussman JL (2003)
The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded
Proteins 53: 758

Zeev-Ben-Mordehai T, Silman I, Sussman JL (2003)
Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure
Biopolymers 68: 395

Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I (2002)
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine
Biochemistry 41: 3555

Dvir H, Wong DM, Harel M, Barril X, Orozco M, Luque FJ, Munoz-Torrero D, Camps P, Rosenberry TL, Silman I, Sussman JL (2002)
3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates
Biochemistry 41: 2970

Dvir H, Jiang H, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL (2002)
X-ray Structures of Torpedo californica Acetylcholinesterase Complexed with (+)-Huperzine A and (-)-Huperzine B: Structural Evidence for an Active Site Rearrangement
Biochemistry 41: 10810

Felder CE, Harel M, Silman I, Sussman JL (2002)
Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase
Acta Crystallographica D Biol Crystallogr 58: 1765

Koellner G, Steiner T, Millard CB, Silman I, Sussman JL (2002)
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

Weik M, Berges J, Raves ML, Gros P, McSweeney S, Silman I, Sussman JL, Houee-Levin C, Ravelli RB (2002)
Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation
J Synchrotron Radiat 9: 342

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 (2001)
A structure-based design approach to the development of novel, reversible AChE inhibitors
Journal of Medicinal Chemistry 44: 3203

Nicolas A, Ferron F, Toker L, Sussman JL, Silman I (2001)
Histochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase
Acta Crystallographica D Biol Crystallogr 57: 1348

Weik M, Ravelli RB, Silman I, Sussman JL, Gros P, Kroon J (2001)
Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes
Protein Science 10: 1953

Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL (2000)
Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors
Protein Science 9: 1063

Koellner G, Kryger G, Millard CB, Silman I, Sussman JL, Steiner T (2000)
Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica
Journal of Molecular Biology 296: 713

Kraut D, Goff H, Pai RK, Hosea NA, Silman I, Sussman JL, Taylor P, Voet JG (2000)
Inactivation studies of acetylcholinesterase with phenylmethylsulfonyl fluoride
Molecular Pharmacology 57: 1243

Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL (2000)
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
Acta Crystallographica D Biol Crystallogr 56: 1385

Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL (2000)
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

Botti SA, Felder CE, Lifson S, Sussman JL, Silman I (1999)
A modular treatment of molecular traffic through the active site of cholinesterase
Biophysical Journal 77: 2430

Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL (1999)
Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution
FEBS Letters 463: 321

Kryger G, Silman I, Sussman JL (1999)
Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs
Structure 7: 297

Millard CB, Kryger G, Ordentlich A, Greenblatt HM, Harel M, Raves ML, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL (1999)
Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level
Biochemistry 38: 7032

Millard CB, Koellner G, Ordentlich A, Shafferman A, Silman I, Sussman JL (1999)
Reaction Products of Acetylcholinesterase and Vx Reveal a Mobile Histidine in the Catalytic Triad
Journal of the American Chemical Society 121: 9883

Morel N, Bon S, Greenblatt HM, Van Belle D, Wodak SJ, Sussman JL, Massoulie J, Silman I (1999)
Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase
Molecular Pharmacology 55: 982

Silman I, Millard CB, Ordentlich A, Greenblatt HM, Harel M, Barak D, Shafferman A, Sussman JL (1999)
A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase
Chemico-Biological Interactions 119-120: 43

Bar-On P, Harel M, Millard CB, Enz A, Sussman JL, Silman I (1998)
Kinetic and structural studies on the interaction of the anti-Alzheimer drug, ENA-713, with Torpedo californica acetylcholinesterase
Journal de Physiologie (Paris) 92: 406

Bar-On P, Harel M, Millard CB, Enz A, Sussman JL, Silman I (1998)
Kinetic and X-Ray Crystallographic Studies of the Binding of ENA-713 to Torpedo Californica Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 373

Botti SA, Felder CE, Sussman JL, Silman I (1998)
Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs
Protein Engineering 11: 415

Botti SA, Felder CE, Sussman JL, Silman I (1998)
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 de Physiologie (Paris) 92: 414

Botti SA, Felder CE, Lifson S, Sussman JL, Silman I (1998)
An Integrated Model for the Molecular Traffic through the Active Site of Cholinesterases
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 227

Botti SA, Felder CE, Sussman JL, Silman I (1998)
The Conjunction of a Conserved Electrostatic Motif and a Common Cholinesterase Fold Defines a Class of Adhesion Proteins
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 448

Giles K, Ben-Yohanan R, Velan B, Shafferman A, Sussman JL, Silman I (1998)
Assembly of Acetylcholinesterase Subunits in vitro
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 442

Giles K, Silman I, Sussman JL (1998)
Expression and Tissue Distribution of Cholinesterases Via EST Analysis
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 450

Greenblatt HM, Kryger G, Harel M, Lewis T, Taylor J, Silman I, Sussman JL (1998)
Crystal Structures of Complexes of E2020-Related Compounds with Torpedo Californica Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 371-371

Kryger G, Silman I, Sussman JL (1998)
Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica
Journal de Physiologie Paris 92: 191

Kryger G, Giles K, Harel M, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL (1998)
3D Structure at 2.7 Resolution of Native and E202Q Mutant Human Acetylcholinesterase Complexed with Fasciculin-II
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 323

Kryger G, Giles K, Harel M, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL (1998)
3D Structure of a Complex of Human Acetylcholinesterase with Fasciculin-II at 2.7 Resolution
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 370

Kryger G, Silman I, Sussman JL (1998)
3D Structure of a Complex of the Anti-Alzheimer Drug, E2020, with Acetylcholinesterase at 2.5 Resolution
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 469

Millard CB, Kryger G, Ordentlich A, Harel M, Raves ML, Greenblatt HM, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL (1998)
Crystal structure of Aged phosphorylated and phosphonylated Torpedo Californica Acetylcholinesterase
In Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 425

Millard CB, Kryger G, Ordentlich A, Harel M, Raves ML, Greenblatt HM, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL (1998)
Crystal Structures of Aged Phosphorylated and Phosphonylated Torpedo Californica Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 425

Millard CB, Kryger G, Ordentlich A, Harel M, Raves ML, Greenblatt HM, Segall Y, Barak D, Shafferman A, Silman I, Sussman JL (1998)
Crystal Structures of Aged Phosphorylated and Phosphonylated Torpedo Californica Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 454

Morel N, Bon S, Sussman JL, Massoulie J, Silman I (1998)
Surface Residues Near the Peripheral Site Affect the Stability of Torpedo Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 435

Nicolas A, Millard CB, Raves ML, Ravelli RB, Kroon J, Silman I, Sussman JL (1998)
Activity of Torpedo Californica Acetylcholinesterase in the Crystalline State
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 230

Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL (1998)
Static laue diffraction studies on acetylcholinesterase
Acta Crystallographica D Biol Crystallogr 54: 1359

Raves ML, Giles K, Schrag JD, Schmid MF, Phillips JN, Jr., Chiu W, Howard AJ, Silman I, Sussman JL (1998)
Quaternary Structure of Tetrameric Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 351

Raves ML, Greenblatt HM, Kryger G, Nicolas A, Ravelli RB, Harel M, Kroon J, Silman I, Sussman JL (1998)
Alternative Crystal Forms of Torpedo Californica Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 372

Silman I, Sussman JL (1998)
Irwin B. Wilson Plenary Lecture Structural and Functional Studies on Acetylcholinesterase
In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp.: 25

Felder CE, Botti SA, Lifson S, Silman I, Sussman JL (1997)
External and internal electrostatic potentials of cholinesterase models
J Mol Graph Model 15: 318

Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL (1997)
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A
Nat Struct Biol 4: 57

Faerman C, Ripoll D, Bon S, Le Feuvre Y, Morel N, Massoulie J, Sussman JL, Silman I (1996)
Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function
FEBS Letters 386: 65

Harel M, Quinn DM, Nair HK, Silman I, Sussman JL (1996)
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

Marchot P, Ravelli RB, Raves ML, Bourne Y, Vellom DC, Kanter J, Camp S, Sussman JL, Taylor P (1996)
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin
Protein Science 5: 672

Peng L, Silman I, Sussman JL, Goeldner M (1996)
Biochemical evaluation of photolabile precursors of choline and of carbamylcholine for potential time-resolved crystallographic studies on cholinesterases
Biochemistry 35: 10854

Porschke D, Creminon C, Cousin X, Bon C, Sussman JL, Silman I (1996)
Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase
Biophysical Journal 70: 1603

Wlodek ST, Antosiewicz J, McCammon JA, Straatsma TP, Gilson MK, Briggs JM, Humblet C, Sussman JL (1996)
Binding of tacrine and 6-chlorotacrine by acetylcholinesterase
Biopolymers 38: 109

Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL (1995)
Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target
Structure 3: 1355

Ripoll DR, Faerman CH, Gillilan R, Silman I, Sussman JL (1995)
Electrostatic Properties of Human Acetylcholinesterase
In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp.: 67

Silman I, Kreimer DI, Shin I, Dolginova EA, Roth E, Goldfarb D, Szosenfogel R, Raves ML, Sussman JL, Borochov N, Weiner L (1995)
Studies on Partially Unfolded States of Torpedo californica Acetylcholinesterase
In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp.: 77

Sussman JL, Harel M, Raves ML, Quinn DM, Nair HK, Silman I (1995)
Structures of Complexes of Acetylcholinesterase with Covalently and Non-Covalently Bound Inhibitors
In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp.: 59

Axelsen PH, Harel M, Silman I, Sussman JL (1994)
Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography
Protein Science 3: 188

Eichler J, Anselmet A, Sussman JL, Massoulie J, Silman I (1994)
Differential effects of peripheral site ligands on Torpedo and chicken acetylcholinesterase
Molecular Pharmacology 45: 335

Gilson MK, Straatsma TP, McCammon JA, Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL (1994)
Open back door in a molecular dynamics simulation of acetylcholinesterase
Science 263: 1276

Kreimer DI, Dolginova EA, Raves ML, Sussman JL, Silman I, Weiner L (1994)
A metastable state of Torpedo californica acetylcholinesterase generated by modification with organomercurials
Biochemistry 33: 14407

Silman I, Harel M, Axelsen PH, Raves ML, Sussman JL (1994)
Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents
Biochemical Society Transactions 22: 745

Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP (1993)
Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
Protein Science 2: 366

Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL (1993)
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

Massoulie J, Sussman JL, Bon S, Silman I (1993)
Structure and functions of acetylcholinesterase and butyrylcholinesterase
Prog Brain Res 98: 139

Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL (1993)
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

Sussman JL, Harel M, Silman I (1993)
Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs
Chemico-Biological Interactions 87: 187

Tan RC, Truong TN, McCammon JA, Sussman JL (1993)
Acetylcholinesterase: electrostatic steering increases the rate of ligand binding
Biochemistry 32: 401

Duval N, Bon S, Silman I, Sussman JL, Massoulie J (1992)
Site-directed mutagenesis of active-site-related residues in Torpedo acetylcholinesterase. Presence of a glutamic acid in the catalytic triad
FEBS Letters 309: 421

Harel M, Sussman JL, Krejci E, Bon S, Chanal P, Massoulie J, Silman I (1992)
Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis
Proceedings of the National Academy of Sciences of the United States of America 89: 10827

Harel M, Silman I, Sussman JL (1992)
A Model of Butyrylcholinesterase Based on the X-Ray Structure of Acetylcholinesterase Indicates Differences in Specificity
In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases (Shafferman, A. and Velan, B., Eds) Plenum Press, New York: 189

Massoulie J, Sussman JL (1992)
Recommendations for Nomenclature in Cholinesterases
In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases (Shafferman, A. and Velan, B., Eds) Plenum Press, New York: 285

Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag JD, Sussman JL, Verschueren KHG, Goldman A (1992)
The alpha/beta hydrolase fold
Protein Engineering 5: 197

Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, Harel M, Silman I, Sussman JL, Velan B (1992)
Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding
Journal of Biological Chemistry 267: 17640

Sussman JL, Harel M, Silman I (1992)
Three Dimensional Structure of Acetylcholinesterase
In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases (Shafferman, A. and Velan, B., Eds) Plenum Press, New York: 95

Harel M, Su CT, Frolow F, Ashani Y, Silman I, Sussman JL (1991)
Refined crystal structures of aged and non-aged organophosphoryl conjugates of gamma-chymotrypsin
Journal of Molecular Biology 221: 909

Su CT, Steinberg N, Silman I, Harel M, Sussman JL, Grunwald J, Ashani Y (1991)
Poster: Physicochemical and crystallographic studies on the stability and structure of aged and nonaged organophosphoryl conjugates of chymotrypsin
In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC: 274

Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I (1991)
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
Science 253: 872

Sussman JL, Harel M, Frolow F, Oefner C, Toker L, Silman I (1991)
Structural Studies on Acetylcholinesterase from Torpedo californica
In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC: 7

Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, Silman I (1988)
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