Evidence map›Paper›PMID 19022262›Full record

ReviewJournal of molecular biology2009

Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition.

Stefan G Sarafianos, Bruno Marchand, Kalyan Das, Daniel M Himmel, Michael A Parniak, Stephen H Hughes, Eddy Arnold

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 280 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
280citing papers in PubMed, 1 pooled it
14.6field-weighted citation impact, top 1% 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

280 citing papers in PubMed, 1 synthesis or guideline pooled it, 513 citations in OpenAlex.

  1. Pooled it
  2. Mechanism of HIV-1 capsid rupture and uncoating by reverse transcription.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  9. Review
  10. Article
  11. Mechanism of HIV-1 Capsid Rupture and Uncoating by Reverse Transcription.bioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structure and mechanism of antiphage retron Eco2.Nature structural & molecular biology · 2026
    Article
  18. Review
  19. Article
  20. Review

220 more citing papers are in PubMed but not listed here.

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

7 authors at 4 institutions in 1 country.

Stefan G SarafianosChristopher Bond Life Sciences Center, Department of Molecular Microbiology & Immunology, University of Missouri School of Medicine, Columbia, MO 65211, USA.
Bruno Marchand
Kalyan Das
Daniel M Himmel
Michael A Parniak
Stephen H Hughes
Eddy Arnold
Rutgers, The State University of New Jersey · USUniversity of Missouri · USNational Cancer Institute · USUniversity of Pittsburgh · 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
STRUCTURES OF HIV REVERSE TRANSCRIPTASE WITH SUBSTRATESR37AI027690 · NIAID · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI ARNOLD, EDWARD · 1999 to 2018
$14.4M
Synthesis of alkylthio derivatized DNA &RNA fragmentsP01GM066671 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI ARNOLD, EDWARD V · 2002 to 2006
$5.0M
Gene Therapy for HIV Using Aptamers that Target Reverse TranscriptaseR01AI074389 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI BURKE, DONALD H · 2008 to 2017
$4.5M
HIV RNase H Natural Product Inhibitors Structural and Computational BiologyU19AI073975 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PARNIAK, MICHAEL A · 2007 to 2011
$4.5M
STRUCTURES OF HIV REVERSE TRANSCRIPTASE WITH SUBSTRATESR01AI027690 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI EDWARD ARNOLD · 1989 to 2026
$4.3M
Ultrapotent Inhibitors of Wild-type and Multi-drug Resistant HIVR01AI076119 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI SARAFIANOS, STEFAN G · 2008 to 2018
$4.1M
Ultrapotent Inhibitors of Wild-type and Multi-drug Resistant HIVR37AI076119 · NIAID · EMORY UNIVERSITY · PI Stefan G Sarafianos · 2020 to 2026
$3.6M
Bisphosphonate inhibitors of NRTI excisionR01AI060452 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PARNIAK, MICHAEL A · 2004 to 2008
$2.7M
Microbicide properties of RT inhibitor combinationsR33AI079801 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PARNIAK, MICHAEL A · 2010 to 2012
$1.4M
Microbicide properties of RT inhibitor combinationsR21AI079801 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PARNIAK, MICHAEL A · 2008 to 2009
$421k
Intramural NIH HHSNIAID NIH HHS AI060452NIAID NIH HHS AI074389NIAID NIH HHS AI076119NIAID NIH HHS AI07980NIAID NIH HHS AI079801NIAID NIH HHS AI27690NIAID NIH HHS AI73975NIAID NIH HHS R01 AI027690NIAID NIH HHS R01 AI060452NIAID NIH HHS R01 AI074389NIAID NIH HHS R01 AI076119NIAID NIH HHS R21 AI079801NIAID NIH HHS R33 AI079801NIAID NIH HHS R37 AI027690NIAID NIH HHS R37 AI076119NIAID NIH HHS U19 AI073975NIGMS NIH HHS P01 GM 066671NIGMS NIH HHS P01 GM066671
6 · The paper itself

Abstract

The rapid replication of HIV-1 and the errors made during viral replication cause the virus to evolve rapidly in patients, making the problems of vaccine development and drug therapy particularly challenging. In the absence of an effective vaccine, drugs are the only useful treatment. Anti-HIV drugs work; so far drug therapy has saved more than three million years of life. Unfortunately, HIV-1 develops resistance to all of the available drugs. Although a number of useful anti-HIV drugs have been approved for use in patients, the problems associated with drug toxicity and the development of resistance means that the search for new drugs is an ongoing process. The three viral enzymes, reverse transcriptase (RT), integrase (IN), and protease (PR) are all good drug targets. Two distinct types of RT inhibitors, both of which block the polymerase activity of RT, have been approved to treat HIV-1 infections, nucleoside analogs (NRTIs) and nonnucleosides (NNRTIs), and there are promising leads for compounds that either block the RNase H activity or block the polymerase in other ways. A better understanding of the structure and function(s) of RT and of the mechanism(s) of inhibition can be used to generate better drugs; in particular, drugs that are effective against the current drug-resistant strains of HIV-1.

Indexed as

BiopolymersHIV-1HIV Reverse TranscriptaseModels, MolecularReverse Transcriptase InhibitorsStructure-Activity RelationshipVirus ReplicationBiopolymersHIV Reverse Transcriptasereverse transcriptase, Human immunodeficiency virus 1Reverse Transcriptase Inhibitors

Identifiers

PMID19022262
PMCPMC2881421
OpenAlexW1991492628

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.