A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication
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Chaperones in hepatitis C virus infectionMy Cousin, My Enemy: quasispecies suppression of drug resistanceBinding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and ExperimentNMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Interaction study between HCV NS5A-D2 and NS5B using 19F NMR.NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II.Atomistic molecular dynamics simulations of bioactive engrailed 1 interference peptides (EN1-iPeps).
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P2860
A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication
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2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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name
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@ast
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@en
type
label
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@ast
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@en
prefLabel
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@ast
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@en
P2093
P2860
P50
P356
P1476
A Proline-Tryptophan Turn in t ...... atitis C Virus RNA Replication
@en
P2093
Arnaud Leroy
François Penin
Marie Dujardin
Puneet Ahuja
Roland Montserret
Vanesa Madan
P2860
P304
19104-19120
P356
10.1074/JBC.M115.644419
P407
P577
2015-06-17T00:00:00Z