{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T01:29:06Z","timestamp":1776302946670,"version":"3.50.1"},"reference-count":24,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2004,6,1]],"date-time":"2004-06-01T00:00:00Z","timestamp":1086048000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2004,6,1]],"date-time":"2004-06-01T00:00:00Z","timestamp":1086048000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic &amp; Medicinal Chemistry"],"published-print":{"date-parts":[[2004,6]]},"DOI":"10.1016\/j.bmc.2004.03.006","type":"journal-article","created":{"date-parts":[[2004,4,26]],"date-time":"2004-04-26T05:21:14Z","timestamp":1082956874000},"page":"3055-3062","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"title":["Small tripeptide surrogates with low nanomolar affinity as potent inhibitors of the botulinum neurotoxin B metallo-proteolytic activity"],"prefix":"10.1016","volume":"12","author":[{"given":"Armand","family":"Blommaert","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Serge","family":"Turcaud","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christine","family":"Anne","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bernard P","family":"Roques","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bmc.2004.03.006_BIB1","series-title":"Botulinum Neurotoxin and Tetanus Toxin","first-page":"95","article-title":"Cell Surface Receptors for Protein Toxins","author":"Middlebrook","year":"1989"},{"key":"10.1016\/j.bmc.2004.03.006_BIB2","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1038\/359832a0","article-title":"Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin","volume":"359","author":"Schiavo","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.bmc.2004.03.006_BIB3","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0031-6997(25)06852-8","article-title":"The origin, structure, and pharmacological activity of botulinum toxin","volume":"33","author":"Simpson","year":"1981","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.bmc.2004.03.006_BIB4","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/0014-5793(94)00449-8","article-title":"Bacterial protein toxins penetrate cells via a four-step mechanism","volume":"346","author":"Montecucco","year":"1994","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bmc.2004.03.006_BIB5","doi-asserted-by":"crossref","first-page":"23479","DOI":"10.1016\/S0021-9258(18)35863-0","article-title":"Botulinum neurotoxins are zinc proteins","volume":"267","author":"Schiavo","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB6","doi-asserted-by":"crossref","first-page":"2338","DOI":"10.1111\/j.1471-4159.1993.tb07482.x","article-title":"Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease","volume":"61","author":"de Paiva","year":"1993","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB7","doi-asserted-by":"crossref","first-page":"6527","DOI":"10.1073\/pnas.112220599","article-title":"Progress in rapid screening of Bacillus antracis lethal factor activity","volume":"99","author":"Mock","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bmc.2004.03.006_BIB8","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0248-4900(00)01098-4","article-title":"Mechanism of action of clostridial neurotoxins and rational inhibitor design","volume":"92","author":"Roques","year":"2000","journal-title":"Biol. Cell"},{"key":"10.1016\/j.bmc.2004.03.006_BIB9","doi-asserted-by":"crossref","first-page":"4648","DOI":"10.1021\/jm0300680","article-title":"Developement of potent inhibitors of Botulinum neurotoxin type B","volume":"46","author":"Anne","year":"2003","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB10","first-page":"678","article-title":"Co crystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0\u2032 resolution","volume":"7","author":"Hanson","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bmc.2004.03.006_BIB11","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1038\/78005","article-title":"Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B","volume":"7","author":"Swaminathan","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bmc.2004.03.006_BIB12","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1006\/abio.2001.5028","article-title":"High-throughput assay determination of botulinum type B neurotoxin protease activity","volume":"291","author":"Anne","year":"2001","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB13","doi-asserted-by":"crossref","first-page":"4655","DOI":"10.1016\/S0968-0896(03)00450-4","article-title":"Thio-derived disulfides as potent inhibitors of botulinum neurotoxin type B: implications for zinc interaction","volume":"11","author":"Anne","year":"2003","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB14","doi-asserted-by":"crossref","first-page":"2950","DOI":"10.1021\/jm00044a016","article-title":"Differential inhibition of aminopeptidase A and aminopeptidase N by new-amino-thiols","volume":"37","author":"Chauvel","year":"1994","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB15","doi-asserted-by":"crossref","first-page":"4848","DOI":"10.1021\/jo9623853","article-title":"2,4-Dinitrophenyl 4-methoxybenzyldisulfide: a new efficient reagent for electrophilic sulfenylation of \u03b2-amino ester enolates","volume":"62","author":"Bischoff","year":"1997","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB16","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1351\/pac199062071241","article-title":"Camphor as a natural source of chirality in asymmetric synthesis","volume":"62","author":"Oppolzer","year":"1990","journal-title":"Pure Appl. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB17","doi-asserted-by":"crossref","first-page":"6547","DOI":"10.1016\/0040-4039(91)80217-T","article-title":"Asymmetric synthesis of l-pyrenylalanine and l-9-fluorenylglycine via room temperature alkylations of a sultam-derived glycine imine","volume":"32","author":"Josien","year":"1991","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.bmc.2004.03.006_BIB18","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0014-5793(93)80448-4","article-title":"Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds","volume":"335","author":"Schiavo","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bmc.2004.03.006_BIB19","doi-asserted-by":"crossref","first-page":"12764","DOI":"10.1016\/S0021-9258(18)99941-2","article-title":"Cleavage of members of the synaptobrevin\/VAMP family by types D and F botulinal neurotoxins and tetanus toxin","volume":"269","author":"Yamasaki","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB20","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1006\/bbrc.1994.1526","article-title":"Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2","volume":"200","author":"Yamasaki","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bmc.2004.03.006_BIB21","doi-asserted-by":"crossref","first-page":"2630","DOI":"10.1021\/bi9519009","article-title":"Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release","volume":"35","author":"Foran","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bmc.2004.03.006_BIB22","doi-asserted-by":"crossref","first-page":"15365","DOI":"10.1021\/bi00255a017","article-title":"Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane protein and various sized fragments","volume":"33","author":"Foran","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bmc.2004.03.006_BIB23","doi-asserted-by":"crossref","first-page":"3459","DOI":"10.1074\/jbc.272.6.3459","article-title":"Cooperative exosite-dependent cleavage of synaptobrevin by tetanos toxin light chain","volume":"272","author":"Cornille","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bmc.2004.03.006_BIB24","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","article-title":"Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition of an enzymatic reaction","volume":"22","author":"Cheng","year":"1973","journal-title":"Biochem. Pharmacol."}],"container-title":["Bioorganic &amp; Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089604001804?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0968089604001804?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T22:44:47Z","timestamp":1760827487000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968089604001804"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,6]]},"references-count":24,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2004,6]]}},"alternative-id":["S0968089604001804"],"URL":"https:\/\/doi.org\/10.1016\/j.bmc.2004.03.006","relation":{},"ISSN":["0968-0896"],"issn-type":[{"value":"0968-0896","type":"print"}],"subject":[],"published":{"date-parts":[[2004,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Small tripeptide surrogates with low nanomolar affinity as potent inhibitors of the botulinum neurotoxin B metallo-proteolytic activity","name":"articletitle","label":"Article Title"},{"value":"Bioorganic & Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bmc.2004.03.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2004 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}