[1]
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NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
DOI=10.1038/319407a0; PubMed=3753747 [NCBI, ExPASy, EBI, Israel, Japan]
Schumacher M.,
Camp S.,
Maulet Y.,
Newton M.,
McPhee-Quigley K.,
Taylor S.S.,
Friedmann T.,
Taylor P.;
"Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence.";
Nature 319:407-409(1986).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
PubMed=3198606 [NCBI, ExPASy, EBI, Israel, Japan]
Schumacher M.;
"Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase.";
J. Biol. Chem. 263:18979-18987(1988).
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[3]
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PROTEIN SEQUENCE OF 22-45 AND 214-237.
PubMed=3900071 [NCBI, ExPASy, EBI, Israel, Japan]
MacPhee-Quigley K.,
Taylor P.,
Taylor S.;
"Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences.";
J. Biol. Chem. 260:12185-12189(1985).
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[4]
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PROTEIN SEQUENCE OF 100-108.
PubMed=2068091 [NCBI, ExPASy, EBI, Israel, Japan]
Kreienkamp H.J.,
Weise C.,
Raba R.,
Aaviksaar A.,
Hucho F.;
"Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.";
Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991).
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[5]
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PROTEIN SEQUENCE OF 552-558.
PubMed=3335534 [NCBI, ExPASy, EBI, Israel, Japan]
Gibney G.,
Macphee-Quigley K.,
Thompson B.,
Vedvick T.,
Low M.G.,
Taylor S.S.,
Taylor P.;
"Divergence in primary structure between the molecular forms of acetylcholinesterase.";
J. Biol. Chem. 263:1140-1145(1988).
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[6]
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ALTERNATIVE SPLICING.
DOI=10.1016/0896-6273(90)90103-M; PubMed=2306366 [NCBI, ExPASy, EBI, Israel, Japan]
Maulet Y.,
Camp S.,
Gibney G.,
Rachinsky T.L.,
Ekstroem T.J.,
Taylor P.;
"Single gene encodes glycophospholipid-anchored and asymmetric acetylcholinesterase forms: alternative coding exons contain inverted repeat sequences.";
Neuron 4:289-301(1990).
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[7]
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DISULFIDE BONDS.
PubMed=3759980 [NCBI, ExPASy, EBI, Israel, Japan]
McPhee-Quigley K.,
Vedvick T.S.,
Taylor P.,
Taylor S.S.;
"Profile of the disulfide bonds in acetylcholinesterase.";
J. Biol. Chem. 261:13565-13570(1986).
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[8]
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STRUCTURE OF THE GPI-ANCHOR.
PubMed=8257440 [NCBI, ExPASy, EBI, Israel, Japan]
Mehlert A.,
Varon L.,
Silman I.,
Homans S.W.,
Ferguson M.A.;
"Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica.";
Biochem. J. 296:473-479(1993).
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[9]
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GPI-ANCHOR AT SER-564.
DOI=10.1016/0167-4838(95)00205-7; PubMed=8597567 [NCBI, ExPASy, EBI, Israel, Japan]
Bucht G.,
Hjalmarsson K.;
"Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored form.";
Biochim. Biophys. Acta 1292:223-232(1996).
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[10]
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MUTAGENESIS.
PubMed=2217185 [NCBI, ExPASy, EBI, Israel, Japan]
Gibney G.,
Camp S.,
Dionne M.,
McPhee-Quigley K.,
Taylor P.;
"Mutagenesis of essential functional residues in acetylcholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE, GLYCOSYLATION AT ASN-437, DISULFIDE BONDS, AND SUBUNIT.
PubMed=1678899 [NCBI, ExPASy, EBI, Israel, Japan]
Sussman J.L.,
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 253:872-879(1991).
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[12]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH SUBSTRATE ANALOGS.
PubMed=8415649 [NCBI, ExPASy, EBI, Israel, Japan]
Harel M.,
Schalk I.,
Ehret-Sabatier L.,
Bouet F.,
Goeldner M.,
Hirth C.,
Axelsen P.H.,
Silman I.,
Sussman J.L.;
"Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.";
Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993).
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[13]
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X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH FASCICULIN.
DOI=10.1016/S0969-2126(01)00273-8; PubMed=8747462 [NCBI, ExPASy, EBI, Israel, Japan]
Harel M.,
Kleywegt G.J.,
Ravelli R.B.,
Silman I.,
Sussman J.L.;
"Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.";
Structure 3:1355-1366(1995).
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[14]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE INHIBITOR HUPERZINE A.
DOI=10.1038/nsb0197-57; PubMed=8989325 [NCBI, ExPASy, EBI, Israel, Japan]
Raves M.L.,
Harel M.,
Pang Y.P.,
Silman I.,
Kozikowski A.P.,
Sussman J.L.;
"Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.";
Nat. Struct. Biol. 4:57-63(1997).
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[15]
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X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558.
DOI=10.1021/bi982723p; PubMed=10231521 [NCBI, ExPASy, EBI, Israel, Japan]
Bartolucci C.,
Perola E.,
Cellai L.,
Brufani M.,
Lamba D.;
"'Back door' opening implied by the crystal structure of a carbamoylated acetylcholinesterase.";
Biochemistry 38:5714-5719(1999).
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[16]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558.
DOI=10.1021/bi982678l; PubMed=10353814 [NCBI, ExPASy, EBI, Israel, Japan]
Millard C.B.,
Kryger G.,
Ordentlich A.,
Greenblatt H.M.,
Harel M.,
Raves M.L.,
Segall Y.,
Barak D.,
Shafferman A.,
Silman I.,
Sussman J.L.;
"Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.";
Biochemistry 38:7032-7039(1999).
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[17]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH GALANTHAMINE.
DOI=10.1016/S0014-5793(99)01637-3; PubMed=10606746 [NCBI, ExPASy, EBI, Israel, Japan]
Greenblatt H.M.,
Kryger G.,
Lewis T.,
Silman I.,
Sussman J.L.;
"Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3-A resolution.";
FEBS Lett. 463:321-326(1999).
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[18]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR ARICEPT, AND GLYCOSYLATION AT ASN-80; ASN-437; ASN-478 AND ASN-554.
DOI=10.1016/S0969-2126(99)80040-9; PubMed=10368299 [NCBI, ExPASy, EBI, Israel, Japan]
Kryger G.,
Silman I.,
Sussman J.L.;
"Structure of acetylcholinesterase complexed with E2020 (Aricept(R)): implications for the design of new anti-Alzheimer drugs.";
Structure 7:297-307(1999).
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[19]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HUPRINE.
DOI=10.1021/bi011652i; PubMed=11863435 [NCBI, ExPASy, EBI, Israel, Japan]
Dvir H.,
Wong D.M.,
Harel M.,
Barril X.,
Orozco M.,
Luque F.J.,
Munoz-Torrero D.,
Camps P.,
Rosenberry T.L.,
Silman I.,
Sussman J.L.;
"3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates.";
Biochemistry 41:2970-2981(2002).
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[20]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE SYNTHETIC INHIBITOR RIVASTIGMINE.
DOI=10.1021/bi020016x; PubMed=11888271 [NCBI, ExPASy, EBI, Israel, Japan]
Bar-On P.,
Millard C.B.,
Harel M.,
Dvir H.,
Enz A.,
Sussman J.L.,
Silman I.;
"Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.";
Biochemistry 41:3555-3564(2002).
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[21]
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X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR CPT-11.
DOI=10.1124/mol.104.009944; PubMed=15772291 [NCBI, ExPASy, EBI, Israel, Japan]
Harel M.,
Hyatt J.L.,
Brumshtein B.,
Morton C.L.,
Yoon K.J.,
Wadkins R.M.,
Silman I.,
Sussman J.L.,
Potter P.M.;
"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.";
Mol. Pharmacol. 67:1874-1881(2005).
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[22]
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X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437, ACTIVE SITE, AND ENZYME REGULATION.
DOI=10.1038/sj.emboj.7601175; PubMed=16763558 [NCBI, ExPASy, EBI, Israel, Japan]
Colletier J.-P.,
Fournier D.,
Greenblatt H.M.,
Stojan J.,
Sussman J.L.,
Zaccai G.,
Silman I.,
Weik M.;
"Structural insights into substrate traffic and inhibition in acetylcholinesterase.";
EMBO J. 25:2746-2756(2006).
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