Structural determinants that target the hepatitis C virus core protein to lipid droplets. - Test2 - elhamkhani - TriplyDB

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

http://www.wikidata.org/entity/Q43000172

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Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assembly The hepatitis C virus core protein contains a BH3 domain that regulates apoptosis through specific interaction with human Mcl-1 Hepatitis C virus proteins Hepatitis C virus hijacks host lipid metabolism The antiviral protein, viperin, localizes to lipid droplets via its N-terminal amphipathic alpha-helix Modulation of host lipid metabolism by hepatitis C virus: Role of new therapies Trafficking of hepatitis C virus core protein during virus particle assembly Septin 9 induces lipid droplets growth by a phosphatidylinositol-5-phosphate and microtubule-dependent mechanism hijacked by HCV Alanine Scanning of the Hepatitis C Virus Core Protein Reveals Numerous Residues Essential for Production of Infectious Virus RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae Visualization of Double-Stranded RNA in Cells Supporting Hepatitis C Virus RNA Replication The genotype 3-specific hepatitis C virus core protein residue phenylalanine 164 increases steatosis in an in vitro cellular model Essential Role of Domain III of Nonstructural Protein 5A for Hepatitis C Virus Infectious Particle Assembly Specific Polymorphisms in Hepatitis C Virus Genotype 3 Core Protein Associated with Intracellular Lipid Accumulation Recombinant adenoviruses expressing Steatosis-associated Hepatitis C virus genotype 3 Core protein produce intracellular lipid accumulation in cultured and primary hepatocytes Initiation of Hepatitis C Virus Infection Requires the Dynamic Microtubule Network: ROLE OF THE VIRAL NUCLEOCAPSID PROTEIN Characterization of Hepatitis C Virus Core Protein Multimerization and Membrane Envelopment: Revelation of a Cascade of Core-Membrane Interactions Dengue Virus Capsid Protein Usurps Lipid Droplets for Viral Particle Formation Domain 3 of Hepatitis C Virus Core Protein Is Sufficient for Intracellular Lipid Accumulation Palmitoylation of Hepatitis C Virus Core Protein Is Important for Virion Production Functional characterization of core genes from patients with acute hepatitis C virus infection Structural Analysis of Hepatitis C Virus Core-E1 Signal Peptide and Requirements for Cleavage of the Genotype 3a Signal Sequence by Signal Peptide Peptidase Oxidative stress, a trigger of hepatitis C and B virus-induced liver carcinogenesis Direct binding of a hepatitis C virus inhibitor to the viral capsid protein HCV core residues critical for infectivity are also involved in core-NS5A complex formation Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein.Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity.Hepatitis C Virus Is Released via a Noncanonical Secretory Route.Hepatitis C virus core protein binding to lipid membranes: the role of domains 1 and 2.Altered expression patterns of lipid metabolism genes in an animal model of HCV core-related, nonobese, modest hepatic steatosis.Properties and Functions of the Dengue Virus Capsid Protein.Production and pathogenicity of hepatitis C virus core gene products.Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins.NS2 protein of hepatitis C virus interacts with structural and non-structural proteins towards virus assembly.Maintenance of dimer conformation by the dengue virus core protein α4-α4' helix pair is critical for nucleocapsid formation and virus production.Requirement of cellular DDX3 for hepatitis C virus replication is unrelated to its interaction with the viral core protein.Kinetic analysis of the nucleic acid chaperone activity of the hepatitis C virus core protein.A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly.Dual N- and C-terminal helices are required for endoplasmic reticulum and lipid droplet association of alcohol acetyltransferases in Saccharomyces cerevisiae

P2860

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P2860

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

http://www.wikidata.org/entity/Q43000172

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

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2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh-hant

name

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@en

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@nl

type

label

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@en

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@nl

prefLabel

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@en

Structural determinants that target the hepatitis C virus core protein to lipid droplets.

@nl

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P1433

Journal of Biological Chemistry

P1476

Structural determinants that target the hepatitis C virus core protein to lipid droplets

@en

P2093

Francois Penin

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

Jean-Pierre Lavergne

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John McLauchlan

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Maxime Ratinier

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R Graham Hope

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Roland Montserret

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P2860

Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7

Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets

Robust hepatitis C virus infection in vitro.

Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features.

Analysis of antigenicity and topology of E2 glycoprotein present on recombinant hepatitis C virus-like particles.

Subcellular localization of hepatitis C virus structural proteins in a cell culture system that efficiently replicates the virus

Hepatitis C virus core protein shows a cytoplasmic localization and associates to cellular lipid storage droplets

Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR

Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding

Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr

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22236-22247

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scholarly article

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10.1074/JBC.M601031200

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P407

P433

31

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P478

281

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Paul Targett-Adams

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2006-05-16T00:00:00Z

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7076624

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16704979

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