Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded (Q42985720)

12 November 2017

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded (English)

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12 November 2017

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6

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12 November 2017

Jean-Michel Wieruszeski

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object named as

Jean-Michel Wieruszeski

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Xavier Hanoulle

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Xavier Hanoulle

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Dries Verdegem

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author name string

Aurélie Badillo

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12 November 2017

François Penin

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12 November 2017

language of work or name

English

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publication date

26 February 2009

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Biochemical and Biophysical Research Communications

12 November 2017

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12 November 2017

381

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634-638

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4

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Graphical interpretation of Boolean operators for protein NMR assignments.

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Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites

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Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line

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Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded.

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Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein

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Replication of hepatitis C virus

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Natively unfolded proteins: a point where biology waits for physics

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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Essential Role of Domain III of Nonstructural Protein 5A for Hepatitis C Virus Infectious Particle Assembly

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Regulation of Hepatitis C Virion Production via Phosphorylation of the NS5A Protein

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Sequence complexity of disordered protein

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The NS5A protein of hepatitis C virus is a zinc metalloprotein

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Insertion and deletion analyses identify regions of non-structural protein 5A of Hepatitis C virus that are dispensable for viral genome replication.

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Intrinsically unstructured proteins

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Accepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau Protein

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National Institutes of Health Consensus Development Conference: management of hepatitis C: 2002.

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Structural biology of hepatitis C virus

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Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A.

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NPS@: network protein sequence analysis

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Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy

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Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase

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Hepatitis C virus infection protein network

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euHCVdb: the European hepatitis C virus database

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Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein

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An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A

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Identifiers

DOI

10.1016/J.BBRC.2009.02.108

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12 November 2017

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