(Q44499280)

3 December 2017

title

Functional characterization of palmitoylated and nonacylated SNAP-25 purified from insect cells infected with recombinant baculovirus (English)

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3 December 2017

Bettina Kammer

1

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3 December 2017

Michael F G Schmidt

series ordinal

2

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3 December 2017

Michael Veit

series ordinal

3

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3 December 2017

publication date

1 July 2003

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Molecular and Cellular Neuroscience

3 December 2017

published in

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3 December 2017

volume

23

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3 December 2017

issue

3

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3 December 2017

page(s)

333-340

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Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development.

3 December 2017

cites work

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7 January 2021

SNARE-mediated membrane fusion

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7 January 2021

Structural Changes Are Associated with SolubleN-Ethylmaleimide-sensitive Fusion Protein Attachment Protein Receptor Complex Formation

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7 January 2021

SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain.

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https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway

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7 January 2021

Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly

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7 January 2021

Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro.

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7 January 2021

The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS

1 reference

https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

Membrane fusion and exocytosis

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7 January 2021

Retarded processing of influenza virus hemagglutinin in insect cells

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https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment

1 reference

https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

Characterization of the palmitoylation domain of SNAP-25

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https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism

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7 January 2021

A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains

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7 January 2021

The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations

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7 January 2021

Protein sorting by transport vesicles

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7 January 2021

Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes

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7 January 2021

A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

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7 January 2021

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

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7 January 2021

Palmitoylation of the 25-kDa synaptosomal protein (SNAP-25) in vitro occurs in the absence of an enzyme, but is stimulated by binding to syntaxin

1 reference

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7 January 2021

Synaptobrevin 2 is palmitoylated in synaptic vesicles prepared from adult, but not from embryonic brain.

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7 January 2021

Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation.

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7 January 2021

Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25

1 reference

https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin

1 reference

https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting

1 reference

https://api.crossref.org/works/10.1016%2FS1044-7431%2803%2900064-2

7 January 2021

10.1016/S1044-7431(03)00064-2

Identifiers

DOI

1 reference

3 December 2017

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