Regulated vesicular fusion in neurons: snapping together the details.
about
Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretionCysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targetingDifferential localization of SNARE complex proteins SNAP-25, syntaxin, and VAMP during development of the mammalian retina.The role of the t-SNARE SNAP-25 in action potential-dependent calcium signaling and expression in GABAergic and glutamatergic neurons.An Arabidopsis syntaxin homologue isolated by functional complementation of a yeast pep12 mutant.Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development.The Tlg SNARE complex is required for TGN homotypic fusion.A single amino acid near the C terminus of the synaptosomeassociated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells.Secretagogin is expressed in sensory CGRP neurons and in spinal cord of mouse and complements other calcium-binding proteins, with a note on rat and human.SNAP-25 and synaptotagmin involvement in the final Ca(2+)-dependent triggering of neurotransmitter exocytosis.SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway.A review of the role of synaptosomal-associated protein 25 (SNAP-25) in neurological disorders.Taste cells with synapses in rat circumvallate papillae display SNAP-25-like immunoreactivity.SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain.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.AAEM case report 16. Botulism. American Association of Electrodiagnostic Medicine.Termination and initial branch formation of SNAP-25-deficient thalamocortical fibres in heterochronic organotypic co-cultures.Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: a t-SNARE is involved in axonal growth.Evidence of association between SNAP25 gene and attention deficit hyperactivity disorder in a Latin American sample.Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion.A shift in protein S-palmitoylation, with persistence of growth-associated substrates, marks a critical period for synaptic plasticity in developing brain.Developmental and plasticity-related differential expression of two SNAP-25 isoforms in the rat brain.Dual effects of botulinum neurotoxin A on the secretory stages of chromaffin cells
P2860
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P2860
Regulated vesicular fusion in neurons: snapping together the details.
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Regulated vesicular fusion in neurons: snapping together the details.
@ast
Regulated vesicular fusion in neurons: snapping together the details.
@en
type
label
Regulated vesicular fusion in neurons: snapping together the details.
@ast
Regulated vesicular fusion in neurons: snapping together the details.
@en
prefLabel
Regulated vesicular fusion in neurons: snapping together the details.
@ast
Regulated vesicular fusion in neurons: snapping together the details.
@en
P2860
P356
P1476
Regulated vesicular fusion in neurons: snapping together the details.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.11.4621
P407
P577
1994-05-01T00:00:00Z