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Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Zusätzlich bieten wir Ihnen Vesicle-Associated Membrane Protein 1 (Synaptobrevin 1) Antikörper (84) und Vesicle-Associated Membrane Protein 1 (Synaptobrevin 1) Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
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These pathways are consistent with previously reported behavioral and biochemical phenotypes that typify mice lacking ENT1 (zeige SLC29A1 Proteine). Moreover, we validated decreased expression of the SNARE (zeige VTI1B Proteine) complex protein VAMP1 (synaptobrevin-1) in the dHip as well as decreased expression of pro-dynorphin (PDYN (zeige PDYN Proteine)), neuroendocrine convertase (PCSK1 (zeige PCSK1 Proteine)), and Leu-Enkephalin (dynorphin-A (zeige PDYN Proteine)) in the nucleus accumbens
residue 48 of VAMP1 varies frequently between M and I across seventeen closely related primate species, suggesting a potential selective pressure from members of BoNTs for resistance in vertebrates.
Genetically regulated VAMP1 expression in the brain may modify both Alzheimer's disease risk and may contribute to Alzheimer's pathophysiology
Vesicle release in syb2 (zeige VAMP2 Proteine) KO cultured neurons was massively reduced by a knockdown of syb1, demonstrating that syb1 is responsible for the remaining release activity.
A null mutation of Syb1 resulting from a spontaneous, nonsense mutation in mice significantly impairs the function, but not the structure, of the neuromuscular junction.
the trigger site in synaptobrevin is crucial for productive SNARE (zeige VTI1B Proteine) zippering
VAMP1 is selectively expressed in the retina and in discrete areas of the brain including the zona incerta and rostral periolivary region in murine lethal wasting disease.
CGRP was found to occur in the majority of neurons from rat trigeminal ganglia, together with the three exocytotic SNAREs [SNAP25, syntaxin 1 and the synaptobrevin (Sbr, also known as VAMP) isoforms] and synaptotagmin.
VAMP1 homozygous mutations causes of presynaptic congenital myasthenic syndrome.
This report identifies vesicle-associated membrane protein 1 (VAMP1), which encodes a critical protein for synaptic exocytosis, as the responsible gene fora dominantly inherited spastic ataxia
multiple domains outside the R-SNARE (zeige YKT6 Proteine) of tomosyn (zeige STXBP5 Proteine) are critical to the efficacy of inhibition by tomosyn (zeige STXBP5 Proteine) on exocytotic secretion
The expression of the SNARE protein SNAP-25 and its cellular homologue SNAP-23, as well as syntaxin1 and VAMP (vesicle-associated membrane protein) in samples of normal parathyroid tissue, chief cell adenoma, and parathyroid carcinoma, was examined.
The interaction and interdependence of Vangl2, VAMP1, aPKC and the stable microtubule cytoskeleton in the oocyte, shows that maternal Vangl2 and aPKC are required for specific oocyte asymmetries and vertebrate embryonic patterning.
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined.
vesicle-associated membrane protein 1 (synaptobrevin 1)
, synaptobrevin 1
, vesicle-associated membrane protein 1