ArticleBiomolecular NMR assignments2013
Backbone ¹H, ¹³C, and ¹⁵N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.
Article in Biomolecular NMR assignments, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Spin labeling and Double Electron-Electron Resonance (DEER) to Deconstruct Conformational Ensembles of HIV Protease.Methods in enzymology · 2015Article
- Effects of PRE and POST therapy drug-pressure selected mutations on HIV-1 protease conformational sampling.FEBS letters · 2014Article
- The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics.The Journal of biological chemistry · 2014Article
- Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease.Biochemical and biophysical research communications · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
HIV-1 protease (HIV-1PR) is an essential drug target in the treatment of patients infected with HIV-1. Mutations are found to arise in over 38 of 99 amino acid sites in this protein in response to drug therapy or natural selection, where many are found combinations that alter enzyme kinetics or inhibitor susceptibility without a clear structural mechanism. In efforts to understand how these mutations alter the flexibility and dynamics of HIV-1PR, we report the backbone (1)H, (13)C, and (15)N chemical shift assignments for subtypes C, circulating recombinant form CRF01_AE and a multi-drug resistant variant MDR 769. These assignments are essential for future work aimed at characterizing backbone dynamics, exchange dynamics and dynamics of protein/substrate or protein/inhibitor interactions.
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