Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
about
Discovery of a novel enzymatic cleavage site for botulinum neurotoxin F5Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosomeSNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretionSyntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomesSynaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assemblyMass Spectrometric Detection of Bacterial Protein Toxins and Their Enzymatic ActivityIterative Structure-Based Peptide-Like Inhibitor Design against the Botulinum Neurotoxin Serotype AIdentification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA,Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targetingSNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREsAccelerated neuronal cell recovery from Botulinum neurotoxin intoxication by targeted ubiquitinationThe destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion.Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.t-SNARE protein conformations patterned by the lipid microenvironment.Substrates and controls for the quantitative detection of active botulinum neurotoxin in protease-containing samplesCharacterization of neutralizing antibodies and identification of neutralizing epitope mimics on the Clostridium botulinum neurotoxin type A.A decrease in membrane tension precedes successful cell-membrane repairInvestigations into small molecule non-peptidic inhibitors of the botulinum neurotoxins.A V H H that neutralizes the zinc metalloproteinase activity of botulinum neurotoxin type ATetanus and botulinum neurotoxins: mechanism of action and therapeutic uses.Lipid and cationic polymer based transduction of botulinum holotoxin, or toxin protease alone, extends the target cell range and improves the efficiency of intoxicationSecond generation steroidal 4-aminoquinolines are potent, dual-target inhibitors of the botulinum neurotoxin serotype A metalloprotease and P. falciparum malariaBotulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors.Regional and developmental brain expression patterns of SNAP25 splice variants.Gβγ and the C terminus of SNAP-25 are necessary for long-term depression of transmitter release.Botulinum neurotoxins and botulism: a novel therapeutic approach.Time-dependent botulinum neurotoxin serotype A metalloprotease inhibitors.Targeting botulinum neurotoxin persistence by the ubiquitin-proteasome system.Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion.Analysis of Botulinum Neurotoxin Serotype A Metalloprotease Inhibitors: Analogs of a Chemotype for Therapeutic Development in the Context of a Three-Zone PharmacophoreA highly Ca2+-sensitive pool of vesicles is regulated by protein kinase C in adrenal chromaffin cells.Small-molecule quinolinol inhibitor identified provides protection against BoNT/A in mice.Botulinum toxin: bioweapon & magic drugSensitive and quantitative detection of botulinum neurotoxin in neurons derived from mouse embryonic stem cells.Botulinum neurotoxin subtype A2 enters neuronal cells faster than subtype A1Astrocytes protect neurons against methylmercury via ATP/P2Y(1) receptor-mediated pathways in astrocytes.A chemotype that inhibits three unrelated pathogenic targets: the botulinum neurotoxin serotype A light chain, P. falciparum malaria, and the Ebola filovirus.Different substrate recognition requirements for cleavage of synaptobrevin-2 by Clostridium baratii and Clostridium botulinum type F neurotoxins.Isolation and functional characterization of the novel Clostridium botulinum neurotoxin A8 subtype.The zinc-dependent protease activity of the botulinum neurotoxins
P2860
Q24299963-FE064DCB-0BF4-4FD1-A3B9-5EEEF8899B99Q24321758-F07F16B7-D4CE-4D9C-934F-B958944F37A8Q24531420-2BD5ACCA-1787-4E12-AF41-C4A6BC6C4501Q24682732-447FDDDD-17B0-4577-99EF-798FA5BCFB95Q26269962-B7FE268A-18EC-4F6C-A4CF-B29956FF393FQ26781284-35DA19D9-D193-4196-BB22-0C8DD5A3A87DQ27663273-BFAA7231-5FEB-4805-9DAC-DC0F1FCAE2FEQ27664131-1EF14258-8D2B-40EA-8E9E-B26502C9B983Q28344389-1CC44303-FF4B-4B98-BA39-40FC19E5DD7AQ28571757-732FED45-B5B1-4A89-8F17-DD7BCCFB57DAQ28744316-36A892E6-89ED-4DDA-9F64-E44178FE3977Q30279046-B6C18EA2-62B3-4159-8759-69840D62CFD5Q30442248-A9074DFD-7146-4DD2-B611-1AE9789AAF0EQ30494220-43E71DB0-7FF2-4BBF-9882-BA7A7DC58345Q30543272-B63781D4-428F-4374-B52C-F560EF3D89FCQ30682983-F5768FF7-FBF3-4783-ABC4-563AC0CEA2B1Q30974641-39EFB140-3A24-465A-A4A0-F98E616ECE30Q33423292-0D5A2E96-C249-4182-99E3-991C0D8DF7DBQ33525766-719B4E99-C1AB-43F2-915C-04EB8CD405E6Q33598965-BE57E348-C198-42B2-BF51-B75A54625710Q33620738-BE794891-5FD6-463E-AA83-B1FE51758F1FQ33654562-3F653EA5-CC6E-44BF-9711-0B84E32B8D15Q33869062-A026F78C-E7FE-4091-809E-6CA5403D812BQ33884039-3D93C33A-2BEE-4BEC-88BA-E1EF6099A1D4Q33919805-62254B0E-C0FB-4F93-90DB-C9ADBFFD28CCQ34070659-78C72D4F-FC38-42B0-BD38-8951F0CEF7FEQ34074218-29596920-FFA4-4BE3-BC53-F5BC136E6849Q34151851-67481350-2CFF-41A5-B02F-4A69B933680AQ34297685-65F04E9F-BB86-454C-9AB1-345AAA6DE133Q34317228-5259EE5A-AD52-48F0-A6AD-487E645EB808Q34430854-F3F339CF-881D-4A2D-846E-7ABA60C343AFQ34447906-84251F75-B2C7-468D-BD43-32EA0F112BB6Q34530009-3D1BD45C-AA99-4C30-9C9C-CE04785AB364Q34552134-9A08D107-FA3E-46D8-A197-9476682EA493Q34583087-F276A7EB-06D4-4D09-9084-4B62A0ECCF28Q34612600-C758E194-EF11-42FF-BC8D-A10C8A846700Q34665879-16009D43-D3EA-41BC-A9CF-FD0011E373F9Q34738054-54721BBA-BF5D-42DA-A560-DB028A302F64Q35058841-C3675374-E93E-4FA5-A6CF-C640CFA69007Q35155792-1E0F738B-4659-43B5-BA0B-D0D608CC658D
P2860
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
description
1994 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1994
@ast
im Januar 1994 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1994/01/21)
@sk
vědecký článek publikovaný v roce 1994
@cs
wetenschappelijk artikel (gepubliceerd op 1994/01/21)
@nl
наукова стаття, опублікована в січні 1994
@uk
name
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@ast
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@en
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@nl
type
label
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@ast
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@en
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@nl
prefLabel
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@ast
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@en
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@nl
P2093
P1476
Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
@en
P2093
P304
P407
P577
1994-01-01T00:00:00Z