نتایج جستجو برای: e2 glycoprotein

تعداد نتایج: 112753  

Journal: :Journal of virology 1997
T C Hobman H F Lemon K Jewell

Rubella virus contains three structural proteins, capsid, E2, and E1. E2 and E1 are type I membrane glycoproteins that form a heterodimer in the endoplasmic reticulum (ER) before they are transported to and retained in the Golgi complex, where virus assembly occurs. The bulk of unassembled E2 and E1 subunits are not transported to the Golgi complex. We have recently shown that E2 contains a Gol...

2012
Zhen-yong Keck Jinming Xia Yong Wang Wenyan Wang Thomas Krey Jannick Prentoe Thomas Carlsen Angela Ying-Jian Li Arvind H. Patel Stanley M. Lemon Jens Bukh Felix A. Rey Steven K. H. Foung

The majority of broadly neutralizing antibodies to hepatitis C virus (HCV) are against conformational epitopes on the E2 glycoprotein. Many of them recognize overlapping epitopes in a cluster, designated as antigenic domain B, that contains residues G530 and D535. To gain information on other regions that will be relevant for vaccine design, we employed yeast surface display of antibodies that ...

Journal: :Journal of immunology 2012
Nirjal Bhattarai James H McLinden Jinhua Xiang Thomas M Kaufman Jack T Stapleton

GB virus type C (GBV-C) viremia is associated with reduced CD4+ T cell expansion following IL-2 therapy and with a reduction in T cell activation in HIV-infected individuals. The mechanism(s) by which GBV-C might alter T cell activation or IL-2 signaling have not been studied. In this study, we assess IL-2 release, IL-2R expression, IL-2 signaling, and cell proliferation in tet-off Jurkat cells...

Journal: :The Journal of general virology 1999
A Choukhi A Pillez H Drobecq C Sergheraert C Wychowski J Dubuisson

Hepatitis C virus (HCV) encodes two glycoproteins, E1 and E2, which assemble in oligomeric structures. Studies of HCV glycoprotein assembly using heterologous expression systems have shown that these glycoproteins can follow two pathways: a productive pathway leading to the formation of a non-covalent heterodimer; and a non-productive pathway leading to the formation of large disulfide-linked a...

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