The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.
about
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityUpregulation of protein phosphatase 2Ac by hepatitis C virus modulates NS3 helicase activity through inhibition of protein arginine methyltransferase 1.Effect of bottlenecking on evolution of the nonstructural protein 3 gene of hepatitis C virus during sexually transmitted acute resolving infectionStructurally conserved amino Acid w501 is required for RNA helicase activity but is not essential for DNA helicase activity of hepatitis C virus NS3 protein.Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylationNoise induced changes in the expression of p38/MAPK signaling proteins in the sensory epithelium of the inner ear.Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase.Alternative ways of modulating JAK-STAT pathway: Looking beyond phosphorylation.The hepatitis C virus NS3 protein: a model RNA helicase and potential drug targetRegulation of the EBNA1 Epstein-Barr virus protein by serine phosphorylation and arginine methylationProtein arginine methyltransferase 1-directed methylation of Kaposi sarcoma-associated herpesvirus latency-associated nuclear antigen.Protein interfaces in signaling regulated by arginine methylation.A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3Post-translational modifications of hepatitis C viral proteins and their biological significance.Unconventional post-translational modifications in immunological signaling.Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.An updated evolutionary study of Flaviviridae NS3 helicase and NS5 RNA-dependent RNA polymerase reveals novel invariable motifs as potential pharmacological targets.E2-EPF UCP targets pVHL for degradation and associates with tumor growth and metastasis.Are STATS arginine-methylated?
P2860
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P2860
The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The arginine-1493 residue in Q ...... n arginine methyltransferase 1
@nl
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@ast
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en-gb
type
label
The arginine-1493 residue in Q ...... n arginine methyltransferase 1
@nl
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@ast
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en-gb
altLabel
The Arginine-1493 Residue in Q ...... n Arginine Methyltransferase 1
@en
prefLabel
The arginine-1493 residue in Q ...... n arginine methyltransferase 1
@nl
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@ast
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en-gb
P2093
P2860
P1433
P1476
The arginine-1493 residue in Q ...... arginine methyltransferase 1.
@en
P2093
P2860
P304
P356
10.1128/JVI.75.17.8031-8044.2001
P407
P577
2001-09-01T00:00:00Z