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vesicle docking

Known as: vesicle to membrane docking 
The initial attachment of a transport vesicle membrane to the target membrane, mediated by proteins protruding from the membrane of the vesicle and… Expand
National Institutes of Health

Papers overview

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Highly Cited
2011
Highly Cited
2011
At presynaptic active zones, neurotransmitter release is initiated by the opening of voltage-gated Ca²+ channels close to docked… Expand
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Highly Cited
2009
Highly Cited
2009
Soluble N‐ethylmaleimide‐sensitive factor attachment protein receptor (SNARE) complexes execute synaptic vesicle (SV) fusion… Expand
Highly Cited
2001
Highly Cited
2001
Secretory vesicles dock at the plasma membrane before Ca(2+) triggers their exocytosis. Exocytosis requires the assembly of SNARE… Expand
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Highly Cited
2000
Highly Cited
2000
In yeast, the Class C Vps protein complex (C-Vps complex), composed of Vps11, Vps16, Vps18, and Vps33, functions in Golgi-to… Expand
Highly Cited
1998
Highly Cited
1998
ER‐to‐Golgi transport in yeast may be reproduced in vitro with washed membranes, purified proteins (COPII, Uso1p and LMA1) and… Expand
Highly Cited
1998
Highly Cited
1998
We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extracts of… Expand
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Review
1996
Review
1996
  • S. Pfeffer
  • Annual review of cell and developmental biology
  • 1996
  • Corpus ID: 32959624
Proteins that function in transport vesicle docking are being identified at a rapid rate. So-called v- and t-SNAREs form the core… Expand
Highly Cited
1995
Highly Cited
1995
In synaptic transmission, vesicles are proposed to dock at presynaptic active zones by the association of synaptobrevin (v-SNARE… Expand
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Highly Cited
1995
Highly Cited
1995
Syntaxin 1 and synaptosome-associated protein of 25 kD (SNAP-25) are neuronal plasmalemma proteins that appear to be essential… Expand
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Highly Cited
1993
Highly Cited
1993
The N-ethylmaleimide-sensitive fusion protein (NSF) and the soluble NSF attachment proteins (SNAPs) appear to be essential… Expand