UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate-Reference-Cited by-同舟云学术

UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate

Published:2009-11-24 Issue:6 Volume:78 Page:1441-1456
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Foucault Marine,Mayol Katia,Receveur-Bréchot Véronique,Bussat Marie-Claire,Klinguer-Hamour Christine,Verrier Bernard,Beck Alain,Haser Richard,Gouet Patrice,Guillon Christophe

Funder

Agence Nationale de Recherche sur le Sida

Europrise Network of Excellence

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.22661/fullpdf

Reference73 articles.

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2. Structural and functional characterization of human immunodeficiency virus tat protein;Ruben;J Virol,1989

3. HIV-1 tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure;Dingwall;Embo J,1990

4. HIV-1 tat trans-activation requires the loop sequence within TAR;Feng;Nature,1988

5. Control of RNA initiation and elongation at the HIV-1 promoter;Jones;Annu Rev Biochem,1994

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