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Munc18-syntaxin complexes and exocytosis in human plateletsMunc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactionsPhotolysis of a caged peptide reveals rapid action of N-ethylmaleimide sensitive factor before neurotransmitter releaseARF6 controls post-endocytic recycling through its downstream exocyst complex effectorNeurotransmitter release: the last millisecond in the life of a synaptic vesicleMunc18-1 binding to the neuronal SNARE complex controls synaptic vesicle primingThe Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex RegulationEmerging Insights into the Roles of Membrane Tethers from Analysis of Whole Organisms: The Tip of an Iceberg?The Exocyst at a GlanceExorcising the exocyst complexStructural basis for the Golgi membrane recruitment of Sly1p by Sed5p.The Crystal Structure of Mouse Exo70 Reveals Unique Features of the Mammalian ExocystSec1p directly stimulates SNARE-mediated membrane fusion in vitro.Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum.The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation.Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes.The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE ComplexesMlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p.Mso1 is a novel component of the yeast exocytic SNARE complex.Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1.Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane.Sec6p anchors the assembled exocyst complex at sites of secretion.Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits.Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4pAn internal domain of Exo70p is required for actin-independent localization and mediates assembly of specific exocyst components.SNARE proteins are required for macroautophagySNAREs--engines for membrane fusionRole of Rab GTPases in membrane traffic and cell physiologyAAA+ proteins: have engine, will workYeast Sec1p functions before and after vesicle docking.Regulation of cellular communication by signaling microdomains in the blood vessel wall.Geranylgeranylated SNAREs are dominant inhibitors of membrane fusionThe exocytic gene secA is required for Dictyostelium cell motility and osmoregulationCharacterization of Mug33 reveals complementary roles for actin cable-dependent transport and exocyst regulators in fission yeast exocytosisSM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.Exocyst complex protein expression in the human placenta.SNARE-complex disassembly by NSF follows synaptic-vesicle fusionMembrane bridging and hemifusion by denaturated Munc18.RhoGTPase-binding proteins, the exocyst complex and polarized vesicle traffickingAt the junction of SNARE and SM protein function.
P2860
Q24298238-5D64B51A-701C-4CBF-94EB-15B4CEDB256FQ24557450-64ACD12B-0A3F-46F9-9B61-469D5DDBDDD8Q24657428-C528347F-5547-4102-8996-7F4195D17207Q24672390-518D4005-52A7-4E50-A16F-A9FECEE20BEFQ26269845-EE6CC122-2FC9-403F-B60A-963E17FBD7DEQ26269917-40CCCF3C-6D00-4A82-B5F7-7A73CE65B336Q26744489-A329AC9B-C14A-476E-B1AC-822838CB1FDCQ26765859-836E5F7B-81D5-4FDC-8BC3-8DF62F767681Q26799386-BFC9F356-9796-47C1-BABD-3CBBBFB9E03EQ26824772-3623961F-FF89-4145-8E6F-7807D0EEC881Q27639933-4DAF3D8B-5CB6-428F-A960-6338D44F5074Q27646228-AF311FB0-A358-44FC-B142-0E873A691196Q27931711-78A944D1-4934-4B68-BEA9-E0AC7F0D61FDQ27931819-F2FCF003-171F-41A3-929F-099634C64977Q27932292-B67016A5-4FCE-47B1-9E66-8EE1DB3B6298Q27932523-32F674CC-9030-4DAA-B780-F838991B2974Q27932655-5FDD85D5-EE65-4C7A-86E2-4AAF24DBE129Q27935161-C8118F08-AB66-4D90-9943-C6A5280D17CEQ27935333-E2C17BF1-C0F8-48F7-9AAF-32137ABB9516Q27937182-0C7BD2F8-A360-40E4-BADC-CFE2BDDECE30Q27937851-F381A7A7-A828-452E-852C-E2A9AF1FC934Q27937862-D988FE5C-95B9-4F74-9718-A5ADD8C08ED3Q27938871-610D054A-5D2D-49A2-94AF-3C9505DC8D6EQ27939279-B659D1C7-1F92-4604-BDC5-F4598FFA2875Q27939625-1DC9DB5B-8F25-4D79-BDAE-88FDE8D8D86EQ28742152-4EE9C95F-A18C-4D2C-B509-B185D97B9F20Q29547230-4EE7F196-BD89-4897-B171-B6DE6AFA4EFFQ29616548-F8DAF2E9-4025-4019-A68A-793DDBE604DBQ29617410-E7E11EE9-4C3B-4418-84E9-A24C89284C9DQ30381017-B7A0CC04-7C68-4E1D-8D41-CEDC3B4A5C91Q30406156-628BD357-2F3D-489A-9C0D-05286A8F3BF7Q30442013-B4B2E4A8-4141-4FFD-8B56-57A70CE26491Q30496602-A98EB45B-8403-4ABA-8CA5-1232560EE3B4Q30501053-B7BDB36A-2D4F-47CE-A168-AB09FD373662Q33764725-C6F7EB02-D5A6-40F9-BA95-C1AB8B4FE924Q33897043-5ED2EC6E-7852-4B59-BB51-6EC010DAD83EQ33947145-6DFE482F-26CA-4900-AB8C-0B07FB59DE88Q33963890-C50C3982-7F4B-403C-8269-172008751138Q33967748-27571DAF-A12C-41B1-AD79-95F2F3D8BA13Q34073357-05DD77CF-FA18-44FC-A268-91C67BE60AD9
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Ordering the final events in yeast exocytosis.
@ast
Ordering the final events in yeast exocytosis.
@en
Ordering the final events in yeast exocytosis.
@nl
type
label
Ordering the final events in yeast exocytosis.
@ast
Ordering the final events in yeast exocytosis.
@en
Ordering the final events in yeast exocytosis.
@nl
altLabel
Ordering the final events in yeast exocytosis
@en
prefLabel
Ordering the final events in yeast exocytosis.
@ast
Ordering the final events in yeast exocytosis.
@en
Ordering the final events in yeast exocytosis.
@nl
P2093
P2860
P3181
P356
P1476
Ordering the final events in yeast exocytosis.
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.151.2.439
P407
P577
2000-10-16T00:00:00Z