Evidence map›Paper›PMID 26093496›Full record

ArticleVirology2015

Mutations in human immunodeficiency virus type 1 reverse transcriptase that make it sensitive to degradation by the viral protease in virions are selected against in patients.

Linda L Dunn, Paul L Boyer, Mary Jane McWilliams, Steven J Smith, Stephen H Hughes

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. 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

5 authors at 1 institution in 1 country.

Linda L DunnHIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Paul L BoyerHIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Mary Jane McWilliamsHIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Steven J SmithHIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Stephen H HughesHIV Drug Resistance Program, National Cancer Institute, National Institutes of Health, Frederick, MD, USA. Electronic address: hughesst@mail.nih.gov.
National Institutes of Health · US

Funding

Structure and Function of HIV-1 Reverse TranscriptaseZIABC010481 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HUGHES, STEPHEN H · 2009 to 2022
$15.7M
Retroviral Replication and Vector DesignZ01BC010482 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HUGHES, STEPHEN H · 2003 to 2008
$2.3M
Intramural NIH HHS Z01 BC010482
6 · The paper itself

Abstract

Mutations in the thumb subdomain of reverse transcriptase (RT) of HIV-1 can cause this enzyme to be degraded in virions by the viral protease (PR). Many of these mutations confer a temperature-sensitive phenotype on RT and viral replication. The degradation of RT by PR appears to take place after Gag-Pol has been processed. We show here that mutations in other parts of RT, including the RNase H domain, can make RT PR-sensitive and temperature-sensitive. These data explain why some mutations in the RNase H domain, which had little or no effect on the polymerase activity of purified recombinant RT, had a profound effect on viral titer. Because the PR-sensitive phenotype significantly reduced viral titer, we previously suggested that these mutations would be selected against in patients. We also show that RT mutations that are known to confer a temperature sensitive phenotype are rarely found in the Stanford database.

Indexed as

Mutation, MissenseSelection, GeneticCell LineHIV-1HIV ProteaseHIV Reverse TranscriptaseHumansHydrolysisMutant ProteinsViral LoadHIV ProteaseHIV Reverse TranscriptaseMutant Proteinsp16 protease, Human immunodeficiency virus 1reverse transcriptase, Human immunodeficiency virus 1Gag-PolHIVProteaseRNase HRTTemperature sensitive

Identifiers

PMID26093496
PMCPMC4887144
OpenAlexW592377966

What OpenQuestion holds

Textmetadata
LicenceTDM
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.