Constitutive versus regulated SNARE assembly: a structural basis. - Wikidata - awgldk - TriplyDB

Constitutive versus regulated SNARE assembly: a structural basis.

Constitutive versus regulated SNARE assembly: a structural basis.

http://www.wikidata.org/entity/Q37259787

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A single-vesicle content mixing assay for SNARE-mediated membrane fusion.Hemifusion in SNARE-mediated membrane fusion.Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.Liposome reconstitution of a minimal protein-mediated membrane fusion machine.Molecular basis of the potent membrane-remodeling activity of the epsin 1 N-terminal homology domain.Accessory alpha-helix of complexin I can displace VAMP2 locally in the complexin-SNARE quaternary complex.SNARE-mediated lipid mixing depends on the physical state of the vesicles.Functional redundancy between trans-Golgi network SNARE family members in Arabidopsis thaliana.Determinants of synaptobrevin regulation in membranes.An intramolecular t-SNARE complex functions in vivo without the syntaxin NH2-terminal regulatory domain.Bacterially expressed human serotonin receptor 3A is functionally reconstituted in proteoliposomes The SNARE complex from yeast is partially unstructured on the membrane.A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion.A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion.SNARE assembly and membrane fusion, a kinetic analysis.A partially zipped SNARE complex stabilized by the membrane.A botulinum neurotoxin-like function of Potentilla chinensis extract that inhibits neuronal SNARE complex formation, membrane fusion, neuroexocytosis, and muscle contraction.

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Constitutive versus regulated SNARE assembly: a structural basis.

http://www.wikidata.org/entity/Q37259787

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 05 February 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Constitutive versus regulated SNARE assembly: a structural basis.

@en

Constitutive versus regulated SNARE assembly: a structural basis.

@nl

type

label

Constitutive versus regulated SNARE assembly: a structural basis.

@en

Constitutive versus regulated SNARE assembly: a structural basis.

@nl

prefLabel

Constitutive versus regulated SNARE assembly: a structural basis.

@en

Constitutive versus regulated SNARE assembly: a structural basis.

@nl

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SJ.EMBOJ.7600083

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The EMBO Journal

P1476

Constitutive versus regulated SNARE assembly: a structural basis.

@en

P2093

Fan Zhang

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

Yeon-Kyun Shin

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

Yibin Xu

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

Yong Chen

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

P2860

Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

Three-dimensional structure of the complexin/SNARE complex

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles.

Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.

A conserved domain is present in different families of vesicular fusion proteins: a new superfamily

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins.

Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae.

Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9.

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681-689

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scholarly article

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10.1038/SJ.EMBOJ.7600083

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4

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23

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2004-02-05T00:00:00Z

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8884600

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14765122

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380995

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