The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
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Comparisons of the M1 genome segments and encoded mu2 proteins of different reovirus isolatesSynergistic effects of oncolytic reovirus and docetaxel chemotherapy in prostate cancer.Reovirus induction of and sensitivity to beta interferon in cardiac myocyte cultures correlate with induction of myocarditis and are determined by viral core proteins.Reovirus core protein mu2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules.A post-entry step in the mammalian orthoreovirus replication cycle is a determinant of cell tropism.Sequence analysis of the genome of piscine orthoreovirus (PRV) associated with heart and skeletal muscle inflammation (HSMI) in Atlantic salmon (Salmo salar).Functional investigation of grass carp reovirus nonstructural protein NS80.A single-amino-acid polymorphism in reovirus protein μ2 determines repression of interferon signaling and modulates myocarditisGuanidine hydrochloride inhibits mammalian orthoreovirus growth by reversibly blocking the synthesis of double-stranded RNA.Characterization of grass carp reovirus minor core protein VP4.Identification of functional domains in reovirus replication proteins muNS and mu2.Reovirus replication protein μ2 influences cell tropism by promoting particle assembly within viral inclusions.Mammalian reovirus nonstructural protein microNS forms large inclusions and colocalizes with reovirus microtubule-associated protein micro2 in transfected cellsIncreased ubiquitination and other covariant phenotypes attributed to a strain- and temperature-dependent defect of reovirus core protein mu2.Dissection of mammalian orthoreovirus µ2 reveals a self-associative domain required for binding to microtubules but not to factory matrix protein µNS.Silencing and complementation of reovirus core protein mu2: functional correlations with mu2-microtubule association and differences between virus- and plasmid-derived mu2.A Cytoplasmic RNA Virus Alters the Function of the Cell Splicing Protein SRSF2.Inhibition of reovirus by mycophenolic acid is associated with the M1 genome segment.Reovirus mu2 protein inhibits interferon signaling through a novel mechanism involving nuclear accumulation of interferon regulatory factor 9.Conserved sequence motifs for nucleoside triphosphate binding unique to turreted reoviridae members and coltiviruses.Reovirus Nonstructural Protein σNS Acts as an RNA-Stability Factor Promoting Viral Genome Replication.
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P2860
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@ast
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@en
type
label
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@ast
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@en
prefLabel
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@ast
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@en
P2093
P2860
P1433
P1476
The reovirus protein mu2, encoded by the M1 gene, is an RNA-binding protein.
@en
P2093
P2860
P304
P577
1998-10-01T00:00:00Z