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Mov10 is essential for normal neuronal development and brain function. Mov10 preferentially binds RNAs involved in actin binding, neuronal projection, and cytoskeleton. This is a completely new and critically important function for Mov10 in neuronal development.
Through interference with the ubiquitin-proteasome system, MOV10 enhances the level of apolipoprotein-B-mRNA-editing enzyme catalytic polypeptide-like 3G in HIV-1-infected cells and virions, and synergistically inhibits the replication and infectivity of HIV-1.
these results establish MOV10, an evolutionary conserved protein involved in RNA silencing, as an antiviral gene against RNA viruses that uses an retinoic acid-inducible gene I-like receptor-independent pathway to enhance IFN response
IRAV is an RNA binding protein and localizes to cytoplasmic processing bodies (P bodies) in uninfected cells, where it interacts with the MOV10 RISC complex RNA helicase, suggesting a role for IRAV in the processing of viral RNA.
MOV10 is a highly conserved cellular protein belonging to SF1 helicase family that plays critical roles in EV71 infection
MOV10 acts as an anti-influenza virus factor through specifically inhibiting the nuclear transportation of nucleoprotein and subsequently inhibiting the function of the viral ribonucleoprotein complex
The DEAG-box of huamn MOV10 was required for the enhancement of Rev/RRE-dependent nuclear export.
The endogenous Mov10 could promote hepatitis B virus replication in vitro.
A dual function for MOV10 in regulating translation: it facilitates microRNA-mediated translation of some RNAs, but it also increases expression of other RNAs by preventing AGO2 function.
Results show that MOV10 predominantly binds to 3' UTRs upstream of regions predicted to form local secondary structures and provide evidence that MOV10 helicase mutants are impaired in their ability to translocate 5' to 3' on their mRNA targets.
Association of the SNP rs2932538 in MOV10 and SNP rs4373814 in CACNB2 with an increased risk of hypertension in a Chinese Han population.
MOV10 contributes to the cellular control of long interspersed element 1 replication.
Authors conclude that HIV-1 virion incorporation and the antiviral activities of Mov10 and APOBEC3G do not require their localization to P bodies.
Depletion of endogenous MOV10 significantly enhances the retrotransposition of endogenous retroelements.
APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10
identified two critical MOV10 packaging determinants and eight other critical residues for anti-HIV-1 activity
Results suggest that Mov10 could be required during the lentiviral lifecycle and that its perturbation disrupts generation of infectious viral particles.
MOV10, co-purifies and interacts with components of Polycomb-repressive complex 1 from human cells. Knockdown of MOV10 in human fibroblasts leads to the upregulation of the INK4a.
The identification of capped small RNAs and the involvement of MOV10 in hepatitis delta virus replication further suggest a conserved mechanism related to RNA-directed transcription in lower eukaryotes.
These data suggest that MOV10 is involved in the progression of telomerase-catalyzing reaction via the interaction of telomerase protein and telomere DNA.
Mov10 coimmunoprecipitates with human Ago1 and Ago2 and also colocalizes with them in cytoplasmic P-bodies.
Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA- mediated cleavage of complementary mRNAs by RISC (By similarity).
Mov10, Moloney leukemia virus 10, homolog (mouse)
, moloney leukemia virus 10 protein
, putative helicase MOV-10
, Mov10, Moloney leukemia virus 10
, capping protein (actin filament) muscle Z-line, alpha 1
, functional spliceosome-associated protein 113