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Akbar Ali
Researcher at University of Massachusetts Medical School
Publications - 67
Citations - 3021
Akbar Ali is an academic researcher from University of Massachusetts Medical School. The author has contributed to research in topics: Protease & HIV-1 protease. The author has an hindex of 28, co-authored 63 publications receiving 2687 citations. Previous affiliations of Akbar Ali include University of Maryland Biotechnology Institute.
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Journal ArticleDOI
Visualizing a correlation between siRNA localization, cellular uptake, and RNAi in living cells
TL;DR: It is suggested that interactions with RISC dictate siRNA localization even when siRNA is conjugated to TAT(47-57) peptide, which was distinctly different from nonconjugated free TAT peptide nucleolar localization.
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Small-molecule inhibition of HIV-1 Vif
Robin S. Nathans,Hong Cao,Natalia Sharova,Akbar Ali,Mark Sharkey,Ruzena Wiersum Stranska,Mario Stevenson,Tariq M. Rana,Tariq M. Rana +8 more
TL;DR: This work identifies a small molecule, RN-18, that antagonizes Vif function and inhibits HIV-1 replication only in the presence of A3G, and enhances Vif degradation only in a Vif-dependent manner and reduces viral infectivity by increasing A 3G incorporation into virions and enhances cytidine deamination of the viral genome.
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The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors.
Keith P. Romano,Akbar Ali,Cihan Aydin,Djade I. Soumana,Ayşegül Özen,Laura M. Deveau,Casey Silver,Hong Cao,Alicia Newton,Christos J. Petropoulos,Wei Huang,Celia A. Schiffer +11 more
TL;DR: The molecular basis of HCV N3/4A protease inhibitor resistance is defined and potential strategies for designing robust therapies against this rapidly evolving virus are provided.
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Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding.
TL;DR: A general model for predicting the susceptibility of protease inhibitors to resistance is suggested: drugs designed to fit within the substrate envelope will be less susceptible to resistance, as mutations affecting inhibitor binding would simultaneously interfere with the recognition of viral substrates.
Journal ArticleDOI
HIV-1 protease inhibitors from inverse design in the substrate envelope exhibit subnanomolar binding to drug-resistant variants.
Michael D. Altman,Akbar Ali,G. S. Kiran Kumar Reddy,Madhavi N. L. Nalam,Saima Ghafoor Anjum,Hong Cao,Sripriya Chellappan,Visvaldas Kairys,Miguel X. Fernandes,Michael K. Gilson,Celia A. Schiffer,Tariq M. Rana,Bruce Tidor +12 more
TL;DR: The results suggest that designing inhibitors using the substrate envelope may be a useful strategy in the development of therapeutics with low susceptibility to resistance, especially for especially high-affinity inhibitors.