Clostridial neurotoxins: new tools for dissecting exocytosis.
about
Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosisTetanus neurotoxin-mediated cleavage of cellubrevin impairs epithelial cell migration and integrin-dependent cell adhesion.A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signalA novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cellsNuclear translocation of an ICA512 cytosolic fragment couples granule exocytosis and insulin expression in {beta}-cellsStimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosisRab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by rasSynaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assemblyTargeting of SNAP-23 and SNAP-25 in polarized epithelial cellsProtease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structureHC fragment (C-terminal portion of the heavy chain) of tetanus toxin activates protein kinase C isoforms and phosphoproteins involved in signal transductionModulation of Kv2.1 channel gating and TEA sensitivity by distinct domains of SNAP-25Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoformsSNAP-23 participates in SNARE complex assembly in rat adipose cellsD53 is a novel endosomal SNARE-binding protein that enhances interaction of syntaxin 1 with the synaptobrevin 2 complex in vitroProteolysis 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 cleavageAssembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesiclesDynamin, endocytosis and intracellular signalling (review).A high-throughput screen for chemical inhibitors of exocytic transport in yeastThe genome sequence of Clostridium botulinum type C neurotoxin-converting phage and the molecular mechanisms of unstable lysogeny.Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion.Structural studies on the zinc-endopeptidase light chain of tetanus neurotoxin.The thioredoxin reductase-thioredoxin system is involved in the entry of tetanus and botulinum neurotoxins in the cytosol of nerve terminals.Botulinum neurotoxin type A is internalized and translocated from small synaptic vesicles at the neuromuscular junction.VAMP2, but not VAMP3/cellubrevin, mediates insulin-dependent incorporation of GLUT4 into the plasma membrane of L6 myoblasts.Mushroom bodies suppress locomotor activity in Drosophila melanogasterCa2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin.Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coliInhibition of uptake unmasks rapid extracellular turnover of glutamate of nonvesicular origin.Functional interaction of syntaxin and SNAP-25 with voltage-sensitive L- and N-type Ca2+ channels.Mutational analysis of VAMP domains implicated in Ca2+-induced insulin exocytosis.Coarse-grain simulations reveal movement of the synaptobrevin C-terminus in response to piconewton forces.SNAP-25 is expressed in islets of Langerhans and is involved in insulin release.Restriction of secretory granule motion near the plasma membrane of chromaffin cellsBlock of transmitter release by botulinum C1 action on syntaxin at the squid giant synapse.SNARE proteins synaptobrevin, SNAP-25, and syntaxin are involved in rapid and slow endocytosis at synapses.Acute decrease in net glutamate uptake during energy deprivation.The SNARE complex from yeast is partially unstructured on the membrane.Nitric oxide-related species inhibit evoked neurotransmission but enhance spontaneous miniature synaptic currents in central neuronal cultures.Rapid structural change in synaptosomal-associated protein 25 (SNAP25) precedes the fusion of single vesicles with the plasma membrane in live chromaffin cells.
P2860
Q24313333-1BA1B1FC-26E5-4498-B838-3232EEC59CD7Q24524084-87940A4E-F444-4260-930C-6048EF0425D2Q24648894-C7D54748-3558-46DE-B8DF-D107B15BB65FQ24650961-1B5994F5-710A-44E1-B1EC-9F2F088A42E7Q24676036-993C6DF5-FF5C-49DD-8046-2C98C3B01658Q24678373-D4A41BBA-127F-4180-AE0E-0E0FF8E59A93Q26269958-E950A5EA-5E04-4BDE-B140-CE8BA14907EAQ26269962-5D9D3F20-0732-40A6-97E5-81F21214902FQ28260778-B5B631FA-C4A8-4DFA-A22E-7920C0FB8444Q28268641-E198A74D-397B-463E-820D-BA2EA83D00F0Q28364243-DDAD4A7E-5E40-4954-A6A6-07FFAE97A793Q28575851-3003AC3E-9A4B-401D-96A0-612D14AA3401Q28576116-4129F320-3C66-4E6C-829D-854DD65AD975Q28581582-D8B22DFC-2315-40D6-8125-69031D8EA9A0Q28590292-53456749-FDE7-4A39-8D0E-4094FD70410EQ28609220-72A2D403-F995-485D-B950-A66AFF1DA050Q28609831-280C50E6-EA5C-408B-9692-42D60F8001CFQ30176794-7B47B858-C647-4892-8E0B-187822DE06C4Q33576087-E9FBBA3E-8690-4659-B1A2-1830DCDEF06EQ34132692-309FAC63-2DD0-435C-BC43-C1C11B59345CQ34297685-0CB034C3-4C5A-4A15-8504-7EEE68FDA9EEQ34310242-21A54013-2C2A-4D8C-B2B7-4D50E0FF2E1AQ34313523-43F09CBE-05CD-4349-B5BE-6C199E21FDDDQ34614163-F98AC94C-9D2A-4D1A-932B-C67240C6D18DQ34734230-D60AD71F-2B27-45C6-A422-4F898CA0C333Q35038876-229F09C1-5B4A-47AB-8F7C-028FF25BDBA2Q35212588-FFB5684A-76AB-4982-80F6-570681868A80Q35424656-D92A6722-C7F0-44B8-9C16-FFBB2BD9C99FQ35563396-B1266DDE-09CD-4A27-BD4A-DA8BFD79DF56Q35906137-A375D829-8C54-4F16-AF53-EE972A4B54C5Q35917172-E6220406-C90A-455C-BBB9-79FD0FA804A4Q36207983-DD8071E7-C3B2-4C64-9B28-CAA0D4CA0A8FQ36235424-0966DAEC-47F8-4864-B16A-2CE2C6B278A7Q36342421-3F786FF2-52F4-4B1B-94A4-16F5EE5D2FA6Q36833202-8F269E54-3A0C-4400-A793-91F7BB98A859Q36902034-DA94E1D4-8524-4ADD-913C-70B94A1FE6B0Q36985138-7A67819B-2B86-4CB0-A17F-67BBEDD20134Q37069857-12B7C9AC-D30D-45EC-BF65-2C31436D6CC4Q37095829-D7F251D8-4599-4118-B3EF-05D19AE73E45Q37143588-2A0FCBB9-E925-486C-A125-BE5E925BA77B
P2860
Clostridial neurotoxins: new tools for dissecting exocytosis.
description
1994 nî lūn-bûn
@nan
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
1994年论文
@zh
1994年论文
@zh-cn
name
Clostridial neurotoxins: new tools for dissecting exocytosis.
@en
type
label
Clostridial neurotoxins: new tools for dissecting exocytosis.
@en
prefLabel
Clostridial neurotoxins: new tools for dissecting exocytosis.
@en
P1476
Clostridial neurotoxins: new tools for dissecting exocytosis.
@en
P2093
P304
P356
10.1016/0962-8924(94)90203-8
P577
1994-05-01T00:00:00Z