(Q28268641)

1

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J C Hao

2

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P N Malkus

3

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C Chan

4

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M F Moore

5

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D S King

6

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M K Bennett

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

1 May 1998

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published in

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volume

273

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issue

18

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page(s)

11370-7

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cites work

A molecular description of synaptic vesicle membrane trafficking

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The synaptic vesicle cycle: a cascade of protein-protein interactions

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Clostridial neurotoxins as tools to investigate the molecular events of neurotransmitter release

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Clostridial neurotoxins: new tools for dissecting exocytosis

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Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila

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

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Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking

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Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation

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Specificity and regulation of a synaptic vesicle docking complex

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An alpha-helical minimal binding domain within the H3 domain of syntaxin is required for SNAP-25 binding

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Predicting coiled coils from protein sequences

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Coiled coils: new structures and new functions

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Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase

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Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Inhibition of neurotransmitter release by synthetic proline-rich peptides shows that the N-terminal domain of vesicle-associated membrane protein/synaptobrevin is critical for neuro-exocytosis

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

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A Structural Change Occurs upon Binding of Syntaxin to SNAP-25

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The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin

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Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy

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Structural organization of the synaptic exocytosis core complex

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Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers

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