(Q42996890)

12 November 2017

title

The domain 2 of the HCV NS5A protein is intrinsically unstructured (English)

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12 November 2017

5

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12 November 2017

Xavier Hanoulle

1

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Dries Verdegem

series ordinal

3

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author name string

Aurelie Badillo

series ordinal

2

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12 November 2017

François Penin

series ordinal

4

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12 November 2017

publication date

1 August 2010

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Protein and Peptide Letters

12 November 2017

published in

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12 November 2017

volume

17

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12 November 2017

issue

8

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12 November 2017

page(s)

1012-1018

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

12 November 2017

cites work

2 references

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Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase

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From structure to function: new insights into hepatitis C virus RNA replication

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

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5 May 2024

https://opencitations.net/index/api/v1/references/10.2174/092986610791498920

Preformed structural elements feature in partner recognition by intrinsically unstructured proteins

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

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Replication of hepatitis C virus

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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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Identification of cellular and viral factors related to anti-hepatitis C virus activity of cyclophilin inhibitor

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Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication

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From words to literature in structural proteomics

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The nonstructural 5A protein of hepatitis C virus genotype 1b does not contain an interferon sensitivity-determining region

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Sensitivity of hepatitis C virus to cyclosporine A depends on nonstructural proteins NS5A and NS5B.

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Hepatitis C virus RNA polymerase and NS5A complex with a SNARE-like protein

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Sequence complexity of disordered protein

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Identification of host proteins required for HIV infection through a functional genomic screen

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Hepatitis C virus (HCV) NS5A protein: role in HCV replication and resistance to interferon-alpha

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Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B

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Graphical interpretation of Boolean operators for protein NMR assignments.

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Production of infectious hepatitis C virus in tissue culture from a cloned viral genome

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Hepatitis C virus quasispecies variability modulates nonstructural protein 5A transcriptional activation, pointing to cellular compartmentalization of virus-host interactions

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5 May 2024

https://opencitations.net/index/api/v1/references/10.2174/092986610791498920

Hepatitis C virus infection protein network

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5 May 2024

https://opencitations.net/index/api/v1/references/10.2174/092986610791498920

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B

2 references

5 May 2024

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5 May 2024

https://opencitations.net/index/api/v1/citations/10.1074/JBC.M809244200

Identifiers

DOI

10.2174/092986610791498920

1 reference

12 November 2017

1 reference