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
Dvir H, Silman I, Harel M, Rosenberry TL, Sussman JL (2010)
Acetylcholinesterase: from 3D structure to function
Chemico-Biological Interactions 187: 10
Debord J, Harel M, Verneuil B, Bollinger JC, Dantoine T (2009)
Microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon
Analytical Biochemistry 389: 97
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
Talley TT, Harel M, Hibbs RE, Radic Z, Tomizawa M, Casida JE, Taylor P (2008)
Atomic interactions of neonicotinoid agonists with AChBP: molecular recognition of the distinctive electronegative pharmacophore
Proc Natl Acad Sci U S A 105: 7606
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
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
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
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
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
Hussein AS, Harel M, Selkirk ME (2002)
A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis
Molecular & Biochemical Parasitology 123: 125
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
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
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
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
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, 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
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
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
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
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
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
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
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
Sussman JL, Harel M, Silman I (1993)
Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs
Chemico-Biological Interactions 87: 187
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
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