Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A.
about
The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5AThe Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and PhosphorylationHepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro.Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.An introduction to biological NMR spectroscopy.Discovery and characterization of distinct simian pegiviruses in three wild African Old World monkey species.Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.Insights into the complexity and functionality of hepatitis C virus NS5A phosphorylation.Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Serine phosphorylation of the hepatitis C virus NS5A protein controls the establishment of replication complexes.A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationThe C terminus of NS5A domain II is a key determinant of hepatitis C virus genome replication, but is not required for virion assembly and release.A novel hepacivirus with an unusually long and intrinsically disordered NS5A protein in a wild Old World primate.Phosphorylation of Serine 225 in Hepatitis C Virus NS5A Regulates Protein-Protein Interactions.Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.The Casein Kinase 2-Dependent Phosphorylation of NS5A Domain 3 from Hepatitis C Virus Followed by Time-Resolved NMR Spectroscopy.Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1.The intrinsic disorder status of the human hepatitis C virus proteome.BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins.Analysis of the Bin1 SH3 interaction with peptides derived from the hepatitis C virus protein NS5A and c-Myc reveals that NS5A can competitively displace c-Myc in vitro.The non-structural protein 5A (NS5A) of hepatitis C virus interacts with the SH3 domain of human Bin1 using non-canonical binding sites.
P2860
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P2860
Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A.
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@ast
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@en
type
label
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@ast
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@en
prefLabel
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@ast
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@en
P2093
P50
P1476
Transient structure and SH3 in ...... epatitis C virus protein NS5A.
@en
P2093
Adrien Favier
Amine Aladag
Zsofia Solyom
P304
P356
10.1016/J.JMB.2012.04.023
P407
P577
2012-04-26T00:00:00Z