Evidence map›Paper›PMID 17537865›Full record

ArticleJournal of virology2007

X-ray crystal structures of human immunodeficiency virus type 1 protease mutants complexed with atazanavir.

Herbert E Klei, Kevin Kish, Pin-Fang M Lin, Qi Guo, Jacques Friborg, Ronald E Rose, Yaqun Zhang, Valentina Goldfarb, David R Langley, Michael Wittekind and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  7. Article
  8. Heteroaromatic π-stacking energy landscapes.Journal of chemical information and modeling · 2014
    Article
  9. Automating crystallographic structure solution and refinement of protein-ligand complexes.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  10. Ligand placement based on prior structures: the guided ligand-replacement method.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Atazanavir: its role in HIV treatment.Expert review of anti-infective therapy · 2008
    Review
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 3 countries.

Herbert E KleiMacromolecular Crystallography, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA. herbert.klei@bms.com
Kevin Kish
Pin-Fang M Lin
Qi Guo
Jacques Friborg
Ronald E Rose
Yaqun Zhang
Valentina Goldfarb
David R Langley
Michael Wittekind
Steven Sheriff
Bristol-Myers Squibb (United States) · USInstitute of Crystallography · ITProtein Express (United States) · USInstitute of Macromolecular Chemistry · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atazanavir, which is marketed as REYATAZ, is the first human immunodeficiency virus type 1 (HIV-1) protease inhibitor approved for once-daily administration. As previously reported, atazanavir offers improved inhibitory profiles against several common variants of HIV-1 protease over those of the other peptidomimetic inhibitors currently on the market. This work describes the X-ray crystal structures of complexes of atazanavir with two HIV-1 protease variants, namely, (i) an enzyme optimized for resistance to autolysis and oxidation, referred to as the cleavage-resistant mutant (CRM); and (ii) the M46I/V82F/I84V/L90M mutant of the CRM enzyme, which is resistant to all approved HIV-1 protease inhibitors, referred to as the inhibitor-resistant mutant. In these two complexes, atazanavir adopts distinct bound conformations in response to the V82F substitution, which may explain why this substitution, at least in isolation, has yet to be selected in vitro or in the clinic. Because of its nearly symmetrical chemical structure, atazanavir is able to make several analogous contacts with each monomer of the biological dimer.

Indexed as

Atazanavir SulfateCrystallography, X-RayDrug Resistance, ViralHIV ProteaseHIV Protease InhibitorsModels, MolecularMutationOligopeptidesProtein Structure, TertiaryPyridinesAtazanavir SulfateHIV ProteaseHIV Protease InhibitorsOligopeptidesPyridines

Identifiers

PMID17537865
PMCPMC1951392
OpenAlexW2066908344

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.