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report on a novel mutation of p.Pro56His in VABP found in a Chinese familial amyotrophic lateral sclerosis pedigree and description of the clinical characteristics of the family.
the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3.
Lifelong elevation of neuronal VAPB slowed the decline of neurological impairment, delayed denervation of hindlimb muscles, and prolonged survival of spinal motor neurons.
Study showed that alpha-synuclein perturbs endoplasmic reticulum-mitochondria associations and that this involves disruption to the VAPB-PTPIP51 tethering proteins. Using a range of assays including immunoprecipitation, cellular glutathione S-transferase pull-down, proximity ligation and in vitro binding of recombinant proteins, study showed that alpha-synuclein is a direct binding partner for VAPB.
ACBD5-VAPB interaction regulates peroxisome-endoplasmic reticulum associations. Loss of PO-ER association perturbs PO membrane expansion and increases PO movement.
VAP-ACBD5-mediated contact between the endoplasmic reticulum and peroxisomes mediate organelle maintenance and lipid homeostasis.
Effects of the combined absence of VAPA and VAPB in human cells were studied; cells lacking VAP accumulate high levels of PI4P, actin comets, and trans-Golgi proteins on endosomes. Such defects are mimicked by downregulation of OSBP, a VAP interactor and PI4P transporter that participates in VAP-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 domain which overlaps with those for binding HCV NS5A and human Eph receptors.
The VAPB and its interacting partners cooperatively regulate protein trafficking through the ERGIC by modulating PtdIns4P levels.
Collectively, these results not only lead to a better understanding of hVAPB function but also point to potentially relevant targets for therapeutic intervention.
results suggest that the binding of vesicle-associated membrane protein-associated protein B(VAP-B) to Rab3 GTPase activating protein 1(RAB3GAP1) is implicated in the regulation of nuclear envelope formation through ER-Golgi intermediate compartment
P56S-VAPB was found to suppress adipocyte differentiation by promoting the activation of the ATF4-CHOP pathway
The repertoire of VAPB interactors is more diverse than previously anticipated and link VAPB to the function of ATPase complexes such as p97/FAF1 and ASNA1/transmembrane-domain recognition complex.
In patients with familial or sporadic amyotrophic lateral sclerosis (ALS) from Portugal, Iceland and Sweden no association is found with disease and VAMP-associated protein type B (VAPB) mutations.
Findings provide new pathophysiological mechanisms of P56S VAPB that differentially affect the function and survival of corticospinal and spinal motor neurons in familial amyotrophic lateral sclerosis 8.
genetic screening for this mutation should be performed in all adult patients with lower motor neuron disease, regardless of family history because of the rarity of this disease, physicians often do not suspect it, and many cases may be missed in Brazil.
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.
VAMP-associated 33 kDa protein
, 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 protein B
, vesicle-associated membrane protein, associated protein B and C
, vesicle-associated membrane protein-associated protein B
, VAMP-associated protein 33b
, VAMP (vesicle-associated membrane protein)-associated protein B and C L homeolog