The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops-Reference-Cited by-同舟云学术

The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops

Published:2015-07 Issue: Volume:2 Page:160-165
ISSN:2405-5808
Container-title:Biochemistry and Biophysics Reports
language:en
Short-container-title:Biochemistry and Biophysics Reports

Author:

Kuiper Benjamin D.,Keusch Bradley J.,Dewdney Tamaria G.,Chordia Poorvi,Ross Kyla,Brunzelle Joseph S.,Kovari Iulia A.,MacArthur Rodger,Salimnia Hossein,Kovari Ladislau C.

Funder

National Institutes of Health, USA

DOE, USA

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference29 articles.

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3. Factors associated with the selection of mutations conferring resistance to protease inhibitors (PIs) in PI-experienced patients displaying treatment failure on darunavir;Lambert-Niclot;Antimicrob. Agents Chemother.,2008

4. Human immunodeficiency virus reverse transcriptase and protease sequence database;Rhee;Nucleic Acids Res.,2003

5. The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynami;Chordia;Discoveries,2014

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