Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F.
about
Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMPTransport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membraneCrystal structure of botulinum neurotoxin type A and implications for toxicityProteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavageTetanus and botulinum neurotoxins: mechanism of action and therapeutic uses.Evidence for synaptotagmin as an inhibitory clamp on synaptic vesicle release in Aplysia neuronsSpontaneous transmitter release is critical for the induction of long-term and intermediate-term facilitation in AplysiaVAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues.The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells.Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting.Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuro-exocytosis.Metal substitution of tetanus neurotoxin.PTP1B dephosphorylates N-ethylmaleimide-sensitive factor and elicits SNARE complex disassembly during human sperm exocytosis.Antagonism of botulinum toxin type A-induced cleavage of SNAP-25 in rat cerebral synaptosome by toosendanin.High Conservation of Tetanus and Botulinum Neurotoxins Cleavage Sites on Human SNARE Proteins Suggests That These Pathogens Exerted Little or No Evolutionary Pressure on Humans.Hsp90 is involved in the entry of clostridial neurotoxins into the cytosol of nerve terminals.Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the carboxyl-terminal region of syntaxins.
P2860
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P2860
Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F.
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@ast
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@en
type
label
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@ast
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@en
prefLabel
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@ast
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@en
P2093
P2860
P356
P1476
Synaptobrevin/vesicle-associat ...... inal neurotoxins type D and F.
@en
P2093
Kurazono H
Yamasaki S
P2860
P304
P356
10.1073/PNAS.91.11.4688
P407
P577
1994-05-01T00:00:00Z