about
SV2 mediates entry of tetanus neurotoxin into central neuronsAn overview of Cdk1-controlled targets and processesSyntaxin7 is required for lytic granule release from cytotoxic T lymphocytesAutophagosome targeting and membrane curvature sensing by Barkor/Atg14(L).Synaptic vesicle trafficking and Parkinson's diseaseStructural basis of Vps33A recruitment to the human HOPS complex by Vps16Munc18-2 deficiency causes familial hemophagocytic lymphohistiocytosis type 5 and impairs cytotoxic granule exocytosis in patient NK cellsVps33b pathogenic mutations preferentially affect VIPAS39/SPE-39-positive endosomesThe Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).A dual role of SNAP-25 as carrier and guardian of synaptic transmissionThe diversity of calcium sensor proteins in the regulation of neuronal functionThe molecular physiology of activity-dependent bulk endocytosis of synaptic vesiclesIzumo is part of a multiprotein family whose members form large complexes on mammalian spermAlpha-synuclein promotes SNARE-complex assembly in vivo and in vitroRegulation of intracellular membrane trafficking and cell dynamics by syntaxin-6Retinoic Acid and LTP Recruit Postsynaptic AMPA Receptors Using Distinct SNARE-Dependent MechanismsUbiquitin-Synaptobrevin Fusion Protein Causes Degeneration of Presynaptic Motor Terminals in MiceSynaptotagmin-7 phosphorylation mediates GLP-1-dependent potentiation of insulin secretion from β-cellsSynaptotagmin-1 and synaptotagmin-7 trigger synchronous and asynchronous phases of neurotransmitter releaseNeurotransmitter release: the last millisecond in the life of a synaptic vesicleLipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter releaseDeconstructing complexin function in activating and clamping Ca2+-triggered exocytosis by comparing knockout and knockdown phenotypesLTP requires a unique postsynaptic SNARE fusion machinerySyntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusionThe presynaptic active zoneC-terminal complexin sequence is selectively required for clamping and priming but not for Ca2+ triggering of synaptic exocytosisComplexin activates exocytosis of distinct secretory vesicles controlled by different synaptotagminsSynaptic vesicle exocytosisPostsynaptic complexin controls AMPA receptor exocytosis during LTPComplexin clamps asynchronous release by blocking a secondary Ca(2+) sensor via its accessory α helixCell biology of Ca2+-triggered exocytosisStructural and mutational analysis of functional differentiation between synaptotagmins-1 and -7Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor synaptotagmin-10Testing the SNARE/SM protein model of membrane fusionAlpha-latrotoxin stimulates a novel pathway of Ca2+-dependent synaptic exocytosis independent of the classical synaptic fusion machineryHemophagocytic Lymphohistiocytosis in Children: Pathogenesis and TreatmentSNARE zipperingExosomes as potent regulators of HCC malignancy and potential bio-tools in clinical applicationComplexins: small but capableReconciling the regulatory role of Munc18 proteins in SNARE-complex assembly
P2860
Q21090499-0914CEFE-3317-4B19-8EF8-2475647C52E8Q21203553-08FE993C-990E-4E26-A16F-B089D3AC14C2Q24298095-DCF5D3A3-1DF9-40CF-A1F1-39EFD4056F79Q24300421-519119D4-6848-4232-B973-A84650D507A1Q24302024-67DEAA66-3398-4B73-AC57-6016D2DBFF77Q24313126-20B78310-52CC-4614-86EA-A9A083DEC422Q24313947-622F76F6-B519-4AE0-9B66-AB24CEF17777Q24315069-ED79916E-6D4C-4E80-AE06-B02128037F0AQ24338818-CDDB5545-D4EC-46DD-A9FE-C2250C3E2C44Q24603892-51D0FCA0-CE40-4B5F-BC33-73AEC4D0A4D5Q24604134-4B6284FC-6DF4-4F70-82F4-4D56646A539EQ24616029-AD5665C1-9622-4C85-9E78-962AFEE41979Q24619352-4918F52F-D61E-4118-92BA-F94624EA3CF5Q24629968-0621A67F-E563-428B-8DA5-B69F4784775AQ24633280-B1E442DA-7FEB-4EED-B8B8-29FC113B5BCCQ26269820-3DAD5DE7-8DC8-4676-A442-2CC8A57BCA86Q26269823-AA93F94E-C306-4F6E-9A99-E3F8C083E1D3Q26269824-A7F3A5F2-BD22-4182-965F-936D7FB7BE09Q26269844-421D7457-340E-4D7E-BE03-A103B71E8F8FQ26269845-26C03503-9BAE-4A1D-AAD7-A0546E35DC45Q26269847-0F26ED07-B9E2-4D0C-A2AA-511976D3A631Q26269851-4F4F1E04-9BE1-47B2-81AB-6BB5826C2373Q26269854-716B17EB-9D18-4070-BF0A-DC28C6C1596CQ26269861-08EF0727-1D22-4532-A465-55138012D1DBQ26269863-54FE6A08-55FA-4FF0-8820-9FE873988646Q26269864-AFD0911E-7485-4C26-9D1E-3CA34810786BQ26269866-89710F86-A856-45AC-9424-AB486068F1B3Q26269869-9A766BA9-8D84-466C-BA4C-1AF3EEDC87E6Q26269872-D8E879E7-009B-47C4-8AD3-815150671B77Q26269900-28D2CDFB-09C5-4095-97B7-BB7F8B00A1B8Q26269905-8A56D2B4-E5D7-4E2D-9496-59D2EC73A35FQ26269910-65A34992-4BAC-4826-816F-5C510166E119Q26269914-7E99B024-EEE6-45FB-B7E5-80CC148E2BE1Q26269922-DD532C69-81D6-4805-9377-B1BAE54447DCQ26269933-24BD27F4-DB49-4C88-8C6D-FE66CE368AA4Q26744508-8AE10F50-9F76-4B0C-AE15-82678E292DCDQ26751424-2337B68E-9EF2-4781-8B3A-9E91AE6B0377Q26771839-3B0BEEDC-B3EE-4463-8B3B-B5B74D36EAAFQ26798363-F9064C68-11A9-4C4D-8748-FE6AA6AF5E09Q26821963-A15CA43F-3075-414A-896C-3CE4D9F0E8AE
P2860
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Membrane fusion: grappling with SNARE and SM proteins
@ast
Membrane fusion: grappling with SNARE and SM proteins
@en
Membrane fusion: grappling with SNARE and SM proteins
@nl
type
label
Membrane fusion: grappling with SNARE and SM proteins
@ast
Membrane fusion: grappling with SNARE and SM proteins
@en
Membrane fusion: grappling with SNARE and SM proteins
@nl
prefLabel
Membrane fusion: grappling with SNARE and SM proteins
@ast
Membrane fusion: grappling with SNARE and SM proteins
@en
Membrane fusion: grappling with SNARE and SM proteins
@nl
P2860
P3181
P356
P1433
P1476
Membrane fusion: grappling with SNARE and SM proteins
@en
P2093
James E Rothman
P2860
P3181
P356
10.1126/SCIENCE.1161748
P407
P5008
P577
2009-01-23T00:00:00Z