SNAREpins: minimal machinery for membrane fusion (Q28131697)

4

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author name string

B V Zemelman

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J A McNew

3

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M Gmachl

5

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F Parlati

6

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T H Söllner

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J E Rothman

A family of proteins involved in intracellular transport

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language of work or name

English

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publication date

20 March 1998

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published in

Cell

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volume

92

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page(s)

759-72

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issue

6

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cites work

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Botulinum neurotoxin light chains inhibit both Ca(2+)-induced and GTP analogue-induced catecholamine release from permeabilised adrenal chromaffin cells

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Transbilayer lipid redistribution accompanies poly(ethylene glycol) treatment of model membranes but is not induced by fusion

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A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum

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SNAREs involved in traffic through the Golgi complex

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Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro

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A rapid, sensitive, and specific method for the determination of protein in dilute solution

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Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses

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A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles

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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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SNAP receptors implicated in vesicle targeting and fusion

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VAMP-1: a synaptic vesicle-associated integral membrane protein

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A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion

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The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling

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Atomic structure of the ectodomain from HIV-1 gp41

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