Evidence map›Paper›PMID 34244677›Full record

ReviewNature reviews. Microbiology2022

Structure and function of retroviral integrase.

Goedele N Maertens, Alan N Engelman, Peter Cherepanov

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
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  15. Article
  16. The STAT Signaling Pathway in HIV-1 Infection: Roles and Dysregulation.International journal of molecular sciences · 2025
    Review
  17. Review
  18. Article
  19. Viral oncogenesis in cancer: from mechanisms to therapeutics.Signal transduction and targeted therapy · 2025
    Review
  20. Review

7 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

3 authors at 3 institutions in 2 countries.

Goedele N MaertensDepartment of Infectious Disease, Imperial College London, London, UK. g.maertens@imperial.ac.uk.ORCID 0000-0002-1963-8026
Alan N EngelmanDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA. alan_engelman@dfci.harvard.edu.ORCID 0000-0002-9709-2591
Peter CherepanovDepartment of Infectious Disease, Imperial College London, London, UK. peter.cherepanov@crick.ac.uk.ORCID 0000-0002-0634-538X
Harvard University · USNIHR Imperial Biomedical Research Centre · GBThe Francis Crick Institute · GB

Funding

Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIONG, YONG · 2019 to 2021
$14.1M
Integrase Structural VirologyR01AI070042 · NIAID · DANA-FARBER CANCER INST · PI ENGELMAN, ALAN N. · 2006 to 2020
$7.2M
Cancer Research UKMedical Research CouncilNIAID NIH HHS P50 AI150481NIAID NIH HHS R01 AI070042Wellcome Trust 107005/Z/15ZWellcome Trust FC001061
6 · The paper itself

Abstract

A hallmark of retroviral replication is establishment of the proviral state, wherein a DNA copy of the viral RNA genome is stably incorporated into a host cell chromosome. Integrase is the viral enzyme responsible for the catalytic steps involved in this process, and integrase strand transfer inhibitors are widely used to treat people living with HIV. Over the past decade, a series of X-ray crystallography and cryogenic electron microscopy studies have revealed the structural basis of retroviral DNA integration. A variable number of integrase molecules congregate on viral DNA ends to assemble a conserved intasome core machine that facilitates integration. The structures additionally informed on the modes of integrase inhibitor action and the means by which HIV acquires drug resistance. Recent years have witnessed the development of allosteric integrase inhibitors, a highly promising class of small molecules that antagonize viral morphogenesis. In this Review, we explore recent insights into the organization and mechanism of the retroviral integration machinery and highlight open questions as well as new directions in the field.

Indexed as

Virus IntegrationCrystallography, X-RayDNA, ViralHIV-1HIV IntegraseHumansIntegrasesModels, MolecularProtein ConformationRetroviridaeDNA, ViralHIV IntegraseIntegrases

Identifiers

PMID34244677
PMCPMC8671357
OpenAlexW3181480420

What OpenQuestion holds

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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.