Subunit-specific Protein Footprinting Reveals Significant Structural Rearrangements and a Role for N-terminal Lys-14 of HIV-1 Integrase during Viral DNA Binding-Reference-Cited by-同舟云学术

Subunit-specific Protein Footprinting Reveals Significant Structural Rearrangements and a Role for N-terminal Lys-14 of HIV-1 Integrase during Viral DNA Binding

Published:2008-02 Issue:9 Volume:283 Page:5632-5641
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Zhao Zhuojun,McKee Christopher J.,Kessl Jacques J.,Santos Webster L.,Daigle Janet E.,Engelman Alan,Verdine Gregory,Kvaratskhelia Mamuka

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference61 articles.

1. HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase

2. Diketo acid inhibitor mechanism and HIV-1 integrase: Implications for metal binding in the active site of phosphotransferase enzymes

3. Inhibitors of Strand Transfer That Prevent Integration and Inhibit HIV-1 Replication in Cells

4. A naphthyridine carboxamide provides evidence for discordant resistance between mechanistically identical inhibitors of HIV-1 integrase

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