Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers-Reference-Cited by-同舟云学术

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Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers

Published:2010-07-28 Issue:10 Volume:19 Page:1877-1896
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Lu Jun-Xia,Sharpe Simon,Ghirlando Rodolfo,Yau Wai-Ming,Tycko Robert

Funder

Intramural Research Program

National Institute of Diabetes and Digestive and Kidney Diseases

National Institutes of Health

NIH Intramural AIDS Targeted Antiviral Program

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.474/fullpdf

Reference74 articles.

1. Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1;Marassi;Proc Natl Acad Sci USA,1999

2. The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains;Schubert;J Virol,1996

3. A novel gene of HIV-1, Vpu, and its 16-kilodalton product;Strebel;Science,1988

4. A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif;Margottin;Mol Cell,1998

5. Interaction between the cytoplasmic domains of HIV-1 Vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation;Margottin;Virology,1996

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