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Tomosyn inhibits synaptic vesicle priming in Caenorhabditis elegansPurification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transportThree distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein familyPhosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assemblyGATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28Syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor attachment protein receptors required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophagesMolecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170A novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membraneInsulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissuesThe binary interacting network of the conserved oligomeric Golgi tethering complexA human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathwaysTRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion.How Tlg2p/syntaxin 16 'snares' Vps45Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiaeA SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and functionMembrane recruitment of the kinase cascade scaffold protein Ste5 by the Gbetagamma complex underlies activation of the yeast pheromone response pathwayTRAPP stably associates with the Golgi and is required for vesicle dockingGS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREsHigh-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle dockingPantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles.The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatusTwo new Ypt GTPases are required for exit from the yeast trans-Golgi compartmentmBet3p is required for homotypic COPII vesicle tethering in mammalian cells.Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31Wall mechanics and exocytosis define the shape of growth domains in fission yeastHigh resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complexMechanisms of inhibition of insulin release.Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers.Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.Ordering the final events in yeast exocytosis.BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs.Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosomeVps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late GolgiThree v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae
P2860
Q21563608-BD101803-D95F-4B64-8A98-DB5220F4F45EQ22004165-388C794F-6E9B-498D-B381-CF94104C9D73Q22008832-7F8BF2CB-33CD-4BBE-9811-33FE571B1CDDQ22010905-E7C94CC4-46FA-4725-B40B-3F0306A6DF28Q22253422-DEACA1B3-B952-4B95-82FD-BFCB3473AA64Q22254581-F100F676-F936-42B0-957A-0F96156FBE00Q24291271-7F4A9383-5814-472D-A957-07B6A6CCBF62Q24296761-51C7B880-2354-4C51-BB5D-D40143EBC11AQ24310308-3F02CC09-D4FD-45BF-A447-96D8E6D3CA99Q24316504-91099B0A-2A0F-41FC-9F7E-6215807C2B9AQ24321205-3FD7C1DE-5227-4C07-999E-A5DA98D7D767Q24321545-9D425CBB-24B1-441A-B446-F96EC3CE0CC5Q24323984-9461BC8D-B536-4160-9322-3EA1B35EA536Q24533229-E50EAB9A-7A13-4DF7-B22F-109F487BB9C5Q24534195-9A319172-6D38-4C76-A016-D9506FE15D90Q24554501-32838419-D10D-43A8-834A-92888ED22BD1Q24561799-337343CB-E115-4C7D-BF23-DDA3E5B5CC85Q24595623-0D154E2C-61EC-4765-917C-4FC8F42ACF64Q24597307-575E9DD6-3524-4546-8EA6-FD2BD332E02DQ24600972-9872E905-DFD1-4747-9B66-61C92BA0F152Q24644645-D3D68C8C-EFB6-4942-9534-36E679D14374Q24656954-CDDDB654-000E-4040-B170-433C6F80BC01Q24658241-D0028847-88E8-4D13-BE2F-E068E030D5A5Q24671770-2E49329E-996B-4B7F-87C1-BC24B7AD3E65Q24677983-8E2EE7DC-0B39-4F08-BA7D-3115E5114E3CQ24678537-E9CCD0E0-FD5B-431C-B5DA-A255FCD658F8Q24683056-063F4C0E-38E8-44E0-95F2-6752CF095DF1Q24683594-06C73F3E-5DDC-4880-9E59-FAFB509B9CC2Q27322497-7B275867-1D34-4D88-B708-13FA0DB34E0AQ27640208-58ED3990-3BBD-4CDB-B465-DA917AFEB227Q27867698-C96C961F-9B0F-43E7-AB81-7CAD9A457292Q27929817-5FE64E5A-3E4F-4509-81F8-5C26258EC920Q27929829-FF337425-7074-42A1-8F99-46E1A7CEE368Q27930282-12022935-78EF-42DB-95FA-664B51D8F20BQ27930329-EFFD681A-993D-4D1B-9B85-2736462B49D0Q27931498-D67CCE39-B009-4455-9EDA-2A3E47FD5F71Q27932559-86232AD8-7C7A-4A5A-BA4B-70076EDB446BQ27932636-9EAD0D0E-B0CB-471D-A1B8-1EF17C8198F9Q27932817-9E0522D7-693C-4839-A5A6-E8FD1527286BQ27933048-300F8E2E-03D2-4190-8EE0-60F45F6E1A7E
P2860
description
1994 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Nature
@fr
artículu científicu espublizáu en 1994
@ast
scientific article (publication date: 21 July 1994)
@en
wetenschappelijk artikel (gepubliceerd op 1994/07/21)
@nl
наукова стаття, опублікована в липні 1994
@uk
مقالة علمية (نشرت في 21-7-1994)
@ar
name
Vesicle fusion from yeast to man
@ast
Vesicle fusion from yeast to man
@en
type
label
Vesicle fusion from yeast to man
@ast
Vesicle fusion from yeast to man
@en
prefLabel
Vesicle fusion from yeast to man
@ast
Vesicle fusion from yeast to man
@en
P356
P1433
P1476
Vesicle fusion from yeast to man
@en
P2093
Ferro-Novick S
P2888
P304
P356
10.1038/370191A0
P407
P577
1994-07-01T00:00:00Z
P6179
1043932161