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V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. Zusätzlich bieten wir Ihnen Vesicle Transport through Interaction with T-SNAREs Homolog 1B (Yeast) Antikörper (76) und und viele weitere Produktgruppen zu diesem Protein an.
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RABGEF1 mediates recycling endosome fusion with GAS-containing autophagosome-like vacuoles through the STX6-VAMP3-VTI1B complex; SNAREs are involved in autophagosome formation in response to bacterial infection
Vti1b-dependent tethering of Lytic granule and CD3 (zeige CD3 Proteine)-endo determines accumulation, docking, and efficient lytic granule secretion at the immunological synapse.
Results suggest that the combinational SNARE proteins VAMP8 and Vti1b mediate the fusion of antimicrobial and canonical autophagosomes with lysosomes, an essential event for autophagic degradation.
Ca(2 (zeige CA2 Proteine)+) dissociates the Hrs-containing complex but not the VAMP-2 (zeige VAMP2 Proteine)-containing SNARE (zeige NAPA Proteine) complex
epsin 4 epsin-related protein (zeige CLINT1 Proteine) is an adaptor for vti1b
Results report that syntaxin 7 (zeige STX7 Proteine), syntaxin 8 (zeige STX8 Proteine), vti1b and VAMP8 (zeige VAMP8 Proteine) physically and functionally interact with CFTR (zeige CFTR Proteine).
This studied demonstratedt that the dominant negative SNARE (dnSNARE) mouse model to dissect the role of astrocyte-derived signaling in corticolimbic circuits, with implications for cognitive processing. We found that the blockade of gliotransmitter release in astrocytes triggers a critical desynchronization of neural theta oscillations between dorsal hippocampus and prefrontal cortex.
Our data demonstrate that contrary to the accepted model, SEC22B (zeige SEC22B Proteine) is not necessary for cross-presentation, cautioning against extrapolating phenotypes from knockdown studies alone.
This study reveals that the SNARE-dependent exocytosis in glial cells contributes to neurotoxicity during ischemia in vivo and suggests glial exocytosis as a target for therapeutic approaches.
syntaxin 1 (zeige STX1A Proteine) and vesicle-associated membrane protein 1 (zeige VAMP1 Proteine) are more suitable targets to abolish functional soluble N-ethylmaleimide-sensitive factor attachment protein receptor complexes
These results suggest that SNARE proteins are necessary for the increased activity of KCC2 (zeige SLC12A5 Proteine) after Zn(2+) stimulation of mZnR/GPR39 (zeige GPR39 Proteine).
Results suggest that by regulating the availability of Vti1b, Stx11 (zeige STX11 Proteine) regulates trafficking steps between late endosomes, lysosomes and the cell surface in macrophages.
The identify IR as the first known tyrosine kinase (zeige TYRO3 Proteine) for Munc18c (zeige STXBP3 Proteine) as in GLUT4 (zeige SLC2A4 Proteine) vesicle exocytosis, exemplifying a new model for the coordination of SNARE assembly and vesicle mobilization events in response to a single extracellular stimulus.
Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development
Data show that deletion of CSPalpha produces an abnormal SNAP-25 (zeige SNAP25 Proteine) conformer that inhibits SNARE-complex formation, and is subject to ubiquitylation and proteasomal degradation.
Lysosomal fusion and SNARE function are impaired by cholesterol accumulation in lysosomal storage disorders.
V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence (By similarity).
vesicle transport through interaction with t-SNAREs homolog 1B
, vesicle transport v-SNARE protein Vti1-like 1
, vesicle-associated soluble NSF attachment protein receptor
, A novel SNARE
, Soluble N-ethylmaleimide-sensitive factor-attachment protein receptor
, vesicle transport through interaction with t-SNAREs 1B homolog
, vesicle transport through interaction with t-SNAREs 1B
, vesicle transport through interaction with t-SNAREs homolog 1B (yeast)