Evidence map›Paper›PMID 12584357›Full record

ArticleJournal of virology2003

Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation.

David A Davis, Cara A Brown, Fonda M Newcomb, Emily S Boja, Henry M Fales, Joshua Kaufman, Stephen J Stahl, Paul Wingfield, Robert Yarchoan

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 51 citations in OpenAlex.

  1. SARS-CoV-2 MNature communications · 2024
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  10. The cellular redox environment alters antigen presentation.The Journal of biological chemistry · 2014
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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

9 authors at 3 institutions in 1 country.

David A DavisHIV and AIDS Malignancy Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. dadavis@helix.nih.gov
Cara A Brown
Fonda M Newcomb
Emily S Boja
Henry M Fales
Joshua Kaufman
Stephen J Stahl
Paul Wingfield
Robert Yarchoan
Center for Cancer Research · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · USNational Heart Lung and Blood Institute · US

Funding

Production Of HIV And HIV Related Proteins For Structural StudiesZIAAR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2025
$16.9M
Novel Therapies for HIV Inf. &AIDS-Related MalignanciesZ01SC006737 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI YARCHOAN, ROBERT · 1996 to 2008
$3.1M
Development of Preventive Strategies and Therapy for HIV InfectionZIASC006737 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI YARCHOAN, ROBERT · 2009 to 2025
$3.0M
RECOMBINANT DNA PRODUCED HIV PROTEINS--PURIFICATION/STRUCTURAL CHARACTERZ01AR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 1996 to 2008
$889k
STRUCTURE OF NATURAL PRODUCTS USING INSTRUMENTAL METHODSZ01HL001003 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FALES, HENRY M · 1985 to 2008
$875k
Analysis Of Peptides, Proteins, And Metabolites Using Mass SpectrometryZIAHL001003 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FALES, HENRY · 2009 to 2010
$264k
6 · The paper itself

Abstract

Human immunodeficiency virus protease activity can be regulated by reversible oxidation of a sulfur-containing amino acid at the dimer interface. We show here that oxidation of this amino acid in human immunodeficiency virus type 1 protease prevents dimer formation. Moreover, we show that human T-cell leukemia virus type 1 protease can be similarly regulated through reversible glutathionylation of its two conserved cysteine residues. Based on the known three-dimensional structures and multiple sequence alignments of retroviral proteases, it is predicted that the majority of retroviral proteases have sulfur-containing amino acids at the dimer interface. The regulation of protease activity by the modification of a sulfur-containing amino acid at the dimer interface may be a conserved mechanism among the majority of retroviruses.

Indexed as

Gene Expression Regulation, ViralAmino Acid SequenceAnimalsAspartic Acid EndopeptidasesCatsCattleDimerizationEndopeptidasesEnzyme ActivationHIV ProteaseHumansMiceMolecular Sequence DataOxidation-ReductionRetroviridaeSequence AlignmentAspartic Acid EndopeptidasesEndopeptidasesHIV ProteaseHTLV-1 protease

Identifiers

PMID12584357
PMCPMC149757
OpenAlexW2087349275

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.