Evidence map›Paper›PMID 19457992›Full record

ArticleJournal of virology2009

Modulation of human immunodeficiency virus type 1 protease autoprocessing by charge properties of surface residue 69.

Liangqun Huang, Jane M Sayer, Marie Swinford, John M Louis, Chaoping Chen

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

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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 3 institutions in 1 country.

Liangqun HuangDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Jane M Sayer
Marie Swinford
John M Louis
Chaoping Chen
Colorado State University · USNational Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Isolation and Characterization of Aptamers Targeted to Inhibit HIV Protease MaturR21AI080351 · NIAID · COLORADO STATE UNIVERSITY · PI CHEN, CHAOPING · 2009 to 2010
$400k
Intramural NIH HHS Z99 DK999999NIAID NIH HHS R21 AI080351
6 · The paper itself

Abstract

Mature, fully active human immunodeficiency virus protease (PR) is liberated from the Gag-Pol precursor via regulated autoprocessing. A chimeric protease precursor, glutathione S-transferase-transframe region (TFR)-PR-FLAG, also undergoes N-terminal autocatalytic maturation when it is expressed in Escherichia coli. Mutation of the surface residue H69 to glutamic acid, but not to several neutral or basic amino acids, impedes protease autoprocessing in bacteria and mammalian cells. Only a fraction of mature PR with an H69E mutation (PR(H69E)) folds into active enzymes, and it does so with an apparent Kd (dissociation constant) significantly higher than that of the wild-type protease, corroborating the marked retardation of the in vitro N-terminal autocatalytic processing of TFR-PR(H69E) and suggesting a folding defect in the precursor.

Indexed as

Mutation, MissenseProtein Processing, Post-TranslationalHIV-1HIV ProteaseHumansProtein FoldingHIV Protease

Identifiers

PMID19457992
PMCPMC2708634
OpenAlexW2158462100

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.