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Structural characterization of recombinant human CD81 produced in Pichia pastoris

Structural characterization of recombinant human CD81 produced in Pichia pastoris

http://www.wikidata.org/entity/Q41943770

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Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81 Expression and Subcellular Distribution of GFP-Tagged Human Tetraspanin Proteins in Saccharomyces cerevisiae Hepatitis C virus induces CD81 and claudin-1 endocytosis.Production, purification and characterization of recombinant, full-length human claudin-1.In silico directed mutagenesis identifies the CD81/claudin-1 hepatitis C virus receptor interface.A role for CD81 and hepatitis C virus in hepatoma mobility.Structural characterization of CD81-Claudin-1 hepatitis C virus receptor complexes.G-protein coupled receptor solubilization and purification for biophysical analysis and functional studies, in the total absence of detergent.PCSK9 impedes hepatitis C virus infection in vitro and modulates liver CD81 expression.A new panel of epitope mapped monoclonal antibodies recognising the prototypical tetraspanin CD81.

P2860

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P2860

Structural characterization of recombinant human CD81 produced in Pichia pastoris

http://www.wikidata.org/entity/Q41943770

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Structural characterization of recombinant human CD81 produced in Pichia pastoris

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type

label

Structural characterization of recombinant human CD81 produced in Pichia pastoris

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prefLabel

Structural characterization of recombinant human CD81 produced in Pichia pastoris

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P356

J.PEP.2007.10.013

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Protein Expression and Purification

P1476

Structural characterization of recombinant human CD81 produced in Pichia pastoris

@en

P2093

Mohammed Jamshad

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Sundaresan Rajesh

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Zania Stamataki

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P2860

Binding of hepatitis C virus to CD81

TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins

Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2.

Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes

Structural organization and interactions of transmembrane domains in tetraspanin proteins

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily.

CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs.

Diverse CD81 Proteins Support Hepatitis C Virus Infection

Hepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particles

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206-216

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scholarly article

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10.1016/J.PEP.2007.10.013

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Jane A. McKeating

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