The unexpected structures of hepatitis C virus envelope proteins

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The unexpected structures of hepatitis C virus envelope proteins

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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The unexpected structures of hepatitis C virus envelope proteins

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The unexpected structures of hepatitis C virus envelope proteins

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The unexpected structures of hepatitis C virus envelope proteins

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P1476

The unexpected structures of hepatitis C virus envelope proteins

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P2093

Haihong Zhu

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

Jing Wang

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

Shanshan Wu

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

Yunyun Wang

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P2860

Protein 3D structure computed from evolutionary sequence variation

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

The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum.

Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins

Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.

Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins.

The Neutralizing Activity of Anti-Hepatitis C Virus Antibodies Is Modulated by Specific Glycans on the E2 Envelope Protein

Characterization of Fusion Determinants Points to the Involvement of Three Discrete Regions of Both E1 and E2 Glycoproteins in the Membrane Fusion Process of Hepatitis C Virus

Expression and Characterization of a Minimal Hepatitis C Virus Glycoprotein E2 Core Domain That Retains CD81 Binding

The hepatitis C sequence database in Los Alamos

P304

1859-1865

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P31

scholarly article

P356

10.3892/ETM.2017.4745

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P433

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

P478

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

P577

2017-07-09T00:00:00Z

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

P698

28962094

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P932

5609170

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