Chaperones in hepatitis C virus infection - Test2 - elhamkhani - TriplyDB

Chaperones in hepatitis C virus infection

Chaperones in hepatitis C virus infection

http://www.wikidata.org/entity/Q26771251

about

Detection of HCV genotypes 1b and 2a by a reverse transcription loop-mediated isothermal amplification assay.Perturbation of Wound Healing, Cytoskeletal Organization and Cellular Protein Networks during Hazara Virus Infection.Heat shock proteins HSPB8 and DNAJC5B have HCV antiviral activity.

P2860

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P2860

Chaperones in hepatitis C virus infection

http://www.wikidata.org/entity/Q26771251

description

2016 nî lūn-bûn

@nan

2016 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

name

Chaperones in hepatitis C virus infection

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Chaperones in hepatitis C virus infection

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Chaperones in hepatitis C virus infection

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type

label

Chaperones in hepatitis C virus infection

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Chaperones in hepatitis C virus infection

@en

Chaperones in hepatitis C virus infection

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prefLabel

Chaperones in hepatitis C virus infection

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Chaperones in hepatitis C virus infection

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Chaperones in hepatitis C virus infection

@nl

P1433

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P1433

World journal of hepatology

P1476

Chaperones in hepatitis C virus infection

@en

P2093

Ronik Khachatoorian

http://www.w3.org/2001/XMLSchema#string

Samuel W French

http://www.w3.org/2001/XMLSchema#string

P2860

Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B

The human protein disulfide isomerase gene family

B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts

Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKR

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor

Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK

Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells

Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization

The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones

Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A

P304

9-35

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P31

scholarly article

P356

10.4254/WJH.V8.I1.9

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P407

P433

1

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P478

8

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P577

2016-01-08T00:00:00Z

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P5875

289554082

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P698

26783419

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P921

molecular chaperones

P932

4705456

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