Conserved GXXXG- and S/T-Like Motifs in the Transmembrane Domains of NS4B Protein Are Required for Hepatitis C Virus Replication (Q35077451)

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scientific article published on April 20, 2011

Language	Label	Description	Also known as
English	Conserved GXXXG- and S/T-Like Motifs in the Transmembrane Domains of NS4B Protein Are Required for Hepatitis C Virus Replication	scientific article published on April 20, 2011

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replication (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Conserved GXXXG- and S/T-Like Motifs in the Transmembrane Domains of NS4B Protein Are Required for Hepatitis C Virus Replication (English)

1 reference

10.1128/JVI.02298-10

https://api.crossref.org/works/10.1128/JVI.02298-10

30 November 2024

transmembrane protein

0 references

Hepatitis C virus

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

amino acid motifs

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

author name string

Qingxia Han

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Jason Aligo

2

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

David Manna

3

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Kerry Belton

4

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Yoojin Hong

6

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Sree V. Chintapalli

5

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

Randen L. Patterson

7

1 reference

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

Damian B. van Rossum

8

0000-0003-1011-2586

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

Kouacou V. Konan

9

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

language of work or name

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publication date

20 April 2011

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6 August 2017

full work available at URL

https://jvi.asm.org/content/jvi/85/13/6464.full.pdf

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Europe PubMed Central

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30 November 2024

https://europepmc.org/articles/PMC3126491

online access status

content deliverer

Europe PubMed Central

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

https://europepmc.org/articles/PMC3126491?pdf=render

Portable Document Format

online access status

content deliverer

Europe PubMed Central

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

https://doi.org/10.1128/jvi.02298-10

online access status

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21507970

30 November 2024

https://journals.asm.org/doi/pdf/10.1128/JVI.02298-10

1 reference

10.1128/JVI.02298-10

https://api.crossref.org/works/10.1128/JVI.02298-10

30 November 2024

Journal of Virology

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Europe PubMed Central

PubMed publication ID

6 August 2017

85

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

13

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

6464-6479

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

New opportunities in anti-hepatitis C virus drug discovery: Targeting NS4B

1 reference

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Consensus motif for integrin transmembrane helix association

1 reference

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Formation and function of hepatitis C virus replication complexes require residues in the carboxy-terminal domain of NS4B protein

1 reference

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An Amphipathic -Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane Association

1 reference

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Interaction and conformational dynamics of membrane-spanning protein helices

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Hepatitis C virus NS4B carboxy terminal domain is a membrane binding domain

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Interaction of Hepatitis C Virus Nonstructural Protein 5A with Core Protein Is Critical for the Production of Infectious Virus Particles

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NS3 Helicase Domains Involved in Infectious Intracellular Hepatitis C Virus Particle Assembly

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Comparative protein structure modeling using MODELLER

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Comparative protein structure modeling using Modeller

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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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Visualization of Double-Stranded RNA in Cells Supporting Hepatitis C Virus RNA Replication

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The nucleotide binding motif of hepatitis C virus NS4B can mediate cellular transformation and tumor formation without Ha-ras co-transfection

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Hepatitis C virus molecular clones and their replication capacity in vivo and in cell culture

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Allelic Variation in the Hepatitis C Virus NS4B Protein Dramatically Influences RNA Replication

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GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.

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Participation of Rab5, an Early Endosome Protein, in Hepatitis C Virus RNA Replication Machinery

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Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus Entry

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Compensatory Mutations in E1, p7, NS2, and NS3 Enhance Yields of Cell Culture-Infectious Intergenotypic Chimeric Hepatitis C Virus

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Persistent Hepatitis C Virus Infection In Vitro: Coevolution of Virus and Host

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Mutations of the Hepatitis C virus protein NS4B on either side of the ER membrane affect the efficiency of subgenomic replicons

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Palmitoylation and Polymerization of Hepatitis C Virus NS4B Protein

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Development and characterization of a transient-replication assay for the genotype 2a hepatitis C virus subgenomic replicon

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Complete replication of hepatitis C virus in cell culture

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Robust hepatitis C virus infection in vitro

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A nucleotide binding motif in hepatitis C virus (HCV) NS4B mediates HCV RNA replication

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Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral proteins and RNA.

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Motifs of serine and threonine can drive association of transmembrane helices

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Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups

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27 September 2018

Identifiers

10.1128/JVI.02298-10

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Sitelinks

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