Evidence map›Paper›PMID 24771554›Full record

ArticleProteins2014

The p66 immature precursor of HIV-1 reverse transcriptase.

Naima G Sharaf, Eric Poliner, Ryan L Slack, Martin T Christen, In-Ja L Byeon, Michael A Parniak, Angela M Gronenborn, Rieko Ishima

Open access · bronzeAbstract read
In one paragraph

Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Relative domain orientation of the L289K HIV-1 reverse transcriptase monomer.Protein science : a publication of the Protein Society · 2022
    Article
  5. Review
  6. Article
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  10. Review
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  18. Quantitative Resolution of Monomer-Dimer Populations by Inversion Modulated DEER EPR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016
    Article
  19. Review
  20. 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

8 authors at 1 institution in 1 country.

Naima G SharafDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, 15260.
Eric Poliner
Ryan L Slack
Martin T Christen
In-Ja L Byeon
Michael A Parniak
Angela M Gronenborn
Rieko Ishima
University of Pittsburgh · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2007 to 2018
$48.1M
Project 9P50GM103368 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ARNOLD, EDWARD · 2012 to 2016
$20.0M
Conformational Dynamics and inhibitor responses of HIV-1 RT RNase H in solutionR01GM105401 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ISHIMA, RIEKO · 2013 to 2016
$1.4M
NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50GM082251NIGMS NIH HHS P50 GM103368NIGMS NIH HHS P50GM103368NIGMS NIH HHS R01 GM105401
6 · The paper itself

Abstract

In contrast to the wealth of structural data available for the mature p66/p51 heterodimeric human immunodeficiency virus type 1 reverse transcriptase (RT), the structure of the homodimeric p66 precursor remains unknown. In all X-ray structures of mature RT, free or complexed, the processing site in the p66 subunit, for generating the p51 subunit, is sequestered into a β-strand within the folded ribonuclease H (RNH) domain and is not readily accessible to proteolysis, rendering it difficult to propose a simple and straightforward mechanism of the maturation step. Here, we investigated, by solution NMR, the conformation of the RT p66 homodimer. Our data demonstrate that the RNH and Thumb domains in the p66 homodimer are folded and possess conformations very similar to those in mature RT. This finding suggests that maturation models which invoke a complete or predominantly unfolded RNH domain are unlikely. The present study lays the foundation for further in-depth mechanistic investigations at the atomic level.

Indexed as

Binding SitesHIV Reverse TranscriptaseHumansModels, MolecularProtein ConformationProtein MultimerizationProtein PrecursorsRibonuclease HHIV Reverse TranscriptaseProtein Precursorsreverse transcriptase, Human immunodeficiency virus 1Ribonuclease HdynamicsenzymematurationNMRproteinproteolysisstructure

Identifiers

PMID24771554
PMCPMC4441793
OpenAlexW2098638598

What OpenQuestion holds

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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.