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V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. Additionally we are shipping Vesicle Transport through Interaction with T-SNAREs Homolog 1B (Yeast) Antibodies (76) and and many more products for this protein.
Showing 7 out of 9 products:
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 (show CD3 Proteins)-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 (show CA2 Proteins)+) dissociates the Hrs-containing complex but not the VAMP-2 (show VAMP2 Proteins)-containing SNARE (show NAPA Proteins) complex
epsin 4 epsin-related protein (show CLINT1 Proteins) is an adaptor for vti1b
Results report that syntaxin 7 (show STX7 Proteins), syntaxin 8 (show STX8 Proteins), vti1b and VAMP8 (show VAMP8 Proteins) physically and functionally interact with CFTR (show CFTR Proteins).
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 (show SEC22B Proteins) 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 (show STX1A Proteins) and vesicle-associated membrane protein 1 (show VAMP1 Proteins) 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 (show SLC12A5 Proteins) after Zn(2+) stimulation of mZnR/GPR39 (show GPR39 Proteins).
Results suggest that by regulating the availability of Vti1b, Stx11 (show STX11 Proteins) regulates trafficking steps between late endosomes, lysosomes and the cell surface in macrophages.
The identify IR as the first known tyrosine kinase (show TYRO3 Proteins) for Munc18c as in GLUT4 (show SLC2A4 Proteins) 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 (show SNAP25 Proteins) 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)