Evidence map›Paper›PMID 17626089›Full record

ArticleJournal of virology2007

Molecular mechanisms by which human immunodeficiency virus type 1 integrase stimulates the early steps of reverse transcription.

Charles W Dobard, Marisa S Briones, Samson A Chow

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 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 19% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
  2. An interchangeable prion-like domain is required for Ty1 retrotransposition.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Review
  5. Viruses · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. Structure and function of retroviral integrase.Nature reviews. Microbiology · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Retroviral Integrase: Then and Now.Annual review of virology · 2015
    Review
  18. Multifunctional facets of retrovirus integrase.World journal of biological chemistry · 2015
    Review
  19. Article
  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

3 authors.

Charles W DobardDepartment of Molecular and Medical Pharmacology, School of Medicine, University of California-Los Angeles, CA 90095, USA.
Marisa S Briones
Samson A Chow

Funding

MOLECULAR MECHANISMS OF HIV1 DNA INTEGRATIONR01CA068859 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHOW, SAMSON A · 1995 to 2008
$2.5M
RESEARCH TRAINING IN PHARMACOLOGICAL SCIENCEST32GM008652 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HERSCHMAN, HARVEY R. · 1998 to 2005
$1.1M
NCI NIH HHS CA 68859NCI NIH HHS R01 CA068859NIGMS NIH HHS GM 08652NIGMS NIH HHS T32 GM008652
6 · The paper itself

Abstract

Reverse transcriptase (RT) and integrase (IN) are two essential enzymes that play a critical role in synthesis and integration of the retroviral cDNA, respectively. For human immunodeficiency virus type 1 (HIV-1), RT and IN physically interact and certain mutations and deletions of IN result in viruses defective in early steps of reverse transcription. However, the mechanism by which IN affects reverse transcription is not understood. We used a cell-free reverse transcription assay with different primers and compositions of deoxynucleoside triphosphates to differentially monitor the effect of IN on the initiation and elongation modes of reverse transcription. During the initiation mode, addition of IN stimulated RT-catalyzed reverse transcription by fourfold. The stimulation was specific to IN and could not be detected when the full-length IN was replaced with truncated IN derivatives. The IN-stimulated initiation was also restricted to the template-primer complex formed using tRNA(3)(Lys) or short RNA oligonucleotides as the primer and not those formed using DNA oligonucleotides as the primer. Addition of IN also produced a threefold stimulation during the elongation mode, which was not primer dependent. The stimulation of both initiation and elongation by IN was retained in the presence of an RT trap. Furthermore, IN had no effect on steps at or before template-primer annealing, including packaging of viral genomic RNA and tRNA(3)(Lys). Taken together, our results showed that IN acts at early steps of reverse transcription by increasing the processivity of RT and suppressing the formation of the pause products.

Indexed as

CatalysisCell-Free SystemDNA PrimersHIV-1HIV IntegraseHIV Reverse TranscriptaseHumansNucleotidesReverse TranscriptionRNA, Transfer, LysVirus IntegrationVirus ReplicationDNA PrimersHIV IntegraseHIV Reverse TranscriptaseNucleotidesRNA, Transfer, Lys

Identifiers

PMID17626089
PMCPMC2045400
OpenAlexW2090070116

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.