Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion. - Wikidata - wikimedia - TriplyDB

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

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Structural Features of Apicomplexan Pore-Forming Proteins and Their Roles in Parasite Cell Traversal and Egress The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells.Cryo-EM structure of the exocyst complex.Two subunits of the exocyst, Sec3p and Exo70p, can function exclusively on the plasma membrane.Exocyst subunit EXO70H4 has a specific role in callose synthase secretion and silica accumulation.Polarized Exocytosis.Exposing the Elusive Exocyst Structure

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Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

http://www.wikidata.org/entity/Q37607936

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 23 January 2017

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@en

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

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type

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Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@en

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@nl

prefLabel

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@en

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@nl

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Nature Communications

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Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.

@en

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Johannes Lesigang

http://www.w3.org/2001/XMLSchema#string

Kunrong Mei

http://www.w3.org/2001/XMLSchema#string

Peng Yue

http://www.w3.org/2001/XMLSchema#string

Shaoxiao Wang

http://www.w3.org/2001/XMLSchema#string

Wei Guo

http://www.w3.org/2001/XMLSchema#string

Yubo Zhang

http://www.w3.org/2001/XMLSchema#string

Yueyao Zhu

http://www.w3.org/2001/XMLSchema#string

P2860

A conformational switch in syntaxin during exocytosis: role of munc18.

Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis

Membrane fusion: grappling with SNARE and SM proteins

Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115

Neurotransmitter release: the last millisecond in the life of a synaptic vesicle

Synaptic vesicle exocytosis

Conformational switch of syntaxin-1 controls synaptic vesicle fusion

The Exocyst at a Glance

Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly

A Structure-Based Mechanism for Vesicle Capture by the Multisubunit Tethering Complex Dsl1

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14236

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scholarly article

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10.1038/NCOMMS14236

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8

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2017-01-23T00:00:00Z

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28112172

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1603.02140

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5267525

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