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anti-Human VAPB Antikörper:
anti-Rat (Rattus) VAPB Antikörper:
anti-Mouse (Murine) VAPB Antikörper:
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ACBD5 (zeige ACBD5 Antikörper)-VAPB interaction regulates peroxisome-endoplasmic reticulum associations. Loss of PO-ER association perturbs PO membrane expansion and increases PO movement.
VAP (zeige F10 Antikörper)-ACBD5 (zeige ACBD5 Antikörper)-mediated contact between the endoplasmic reticulum and peroxisomes mediate organelle maintenance and lipid homeostasis.
Effects of the combined absence of VAPA (zeige VAPA Antikörper) and VAPB in human cells were studied; cells lacking VAP (zeige F10 Antikörper) accumulate high levels of PI4P, actin comets, and trans-Golgi proteins on endosomes. Such defects are mimicked by downregulation of OSBP (zeige OSBP Antikörper), a VAP (zeige F10 Antikörper) interactor and PI4P transporter that participates in VAP (zeige F10 Antikörper)-dependent endoplasmic reticulum-endosomes tethers.
this is the first study to report Amyotrophic lateral sclerosis caused by a VAPB mutation in a Chinese population.
Our work revealed that VAP-A/B knockdown impaired the processing and secretion of PAUF, which is one of the cargo proteins of carriers of the trans-Golgi network to the cell surface.
Heterozygous P56S Vapb knock-in mice show mild age-dependent defects in motor behaviors as characteristic features of the disease. The homozygous P56S Vapb knock-in mice show more severe defects compared with heterozygous mice reflecting the dominant and dose-dependent effects of P56S mutation.
VAPB inhibited the degradation of DeltaF508-CFTR in the ER through interactions with the RMA1-Derlin-BAP31-VCP pathway.
Study characterizes the human VAPB-HCV NS5B interaction and reveals that NS5B C-linker is intrinsically disordered in solution but capable of binding the human VAPB-MSP (zeige MSMB Antikörper) domain which overlaps with those for binding HCV NS5A and human Eph (zeige EPHA1 Antikörper) receptors.
The VAPB and its interacting partners cooperatively regulate protein trafficking through the ERGIC by modulating PtdIns4P levels.
results suggest that the binding of vesicle-associated membrane protein-associated protein B(VAP-B) to Rab3 GTPase activating protein 1(RAB3GAP1 (zeige RAB3GAP1 Antikörper)) is implicated in the regulation of nuclear envelope formation through ER-Golgi intermediate compartment
To identify pathological defects in animals expressing the P56S mutant VAPB protein at physiological levels in the appropriate tissues, we have generated Vapb knock-in mice
The disruption of the IRE1 (zeige ERN1 Antikörper)-XBP1 (zeige XBP1 Antikörper) pathway is a cause for the reduced myotube formation in P56S-VAPB-mutation expressing cells.
Vapb knock-out mice exhibit abnormal muscular triacylglycerol levels and FoxO (zeige FOXO3 Antikörper) target gene transcriptional responses to fasting and refeeding
Mice knocked-out for Vapb showed mild motor deficits after 18 months of age.
VapB positively regulates RANKL (zeige TNFSF11 Antikörper)-mediated osteoclastogenesis via PLCgamma2 (zeige PLCG2 Antikörper)-Ca(2 (zeige CA2 Antikörper)+)-NFAT (zeige NFATC1 Antikörper) signaling
Co-expression of mutant protein-associated protein B (zeige LEPREL2 Antikörper) (VAPB) enhances the transactive response DNA-binding protein (zeige HSF4 Antikörper)-43 (TDP-43 (zeige TARDBP Antikörper))-induced motor neuronal cell death while that of wild type-VAPB attenuates it.
Adeno (zeige ADORA2A Antikörper)-associated viral-mediated over-expression of both wild-type and mutated form of human VAPB selectively induces death of primary motor neurons, albeit with different kinetics.
However, VAPBP56S but not VAPBwt transgenic mice develop cytoplasmic TDP-43 (zeige TARDBP Antikörper) accumulations within spinal cord motor neurons that were first detected at 18 months of age.
The total loss of VAPB function in unfolded protein response, induced by one P56S mutant allele, may contribute to the development of P56SVAPB- induced amyotrophic lateral sclerosis.
The protein encoded by this gene is a type IV membrane protein found in plasma and intracellular vesicle membranes. The encoded protein is found as a homodimer and as a heterodimer with VAPA. This protein also can interact with VAMP1 and VAMP2 and may be involved in vesicle trafficking.
vesicle-associated membrane protein-associated protein B/C
, VAMP (vesicle-associated membrane protein)-associated protein B and C
, VAMP-associated protein B/C
, VAMP-associated 33 kDa protein
, VAMP-associated protein B
, vesicle-associated membrane protein-associated protein B
, vesicle-associated membrane protein, associated protein B and C
, VAMP-associated protein 33b