ArticleProtein science : a publication of the Protein Society2022
Relative domain orientation of the L289K HIV-1 reverse transcriptase monomer.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Small-angle X-ray scattering studies of enzymes.Current opinion in chemical biology · 2023Review
- Relative domain orientation of the L289K HIV-1 reverse transcriptase monomer.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
HIV-1 reverse transcriptase (RT) is a heterodimer comprised p66 and p51 subunits (p66/p51). Several single amino acid substitutions in RT, including L289K, decrease p66/p51 dimer affinity, and reduce enzymatic functioning. Here, small-angle X-ray scattering (SAXS) with proton paramagnetic relaxation enhancement (PRE),
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.