Evidence map›Paper›PMID 19490099›Full record

ReviewThe FEBS journal2009

Piecing together the structure of retroviral integrase, an important target in AIDS therapy.

Mariusz Jaskolski, Jerry N Alexandratos, Grzegorz Bujacz, Alexander Wlodawer

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Complex Relationships between HIV-1 Integrase and Its Cellular Partners.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Retroviral DNA Integration.Chemical reviews · 2016
    Review
  17. Article
  18. C-Terminal Domain of Integrase Binds between the Two Active Sites.Journal of chemical theory and computation · 2015
    Article
  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

4 authors at 3 institutions in 2 countries.

Mariusz JaskolskiDepartment of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Poznan, Poland.
Jerry N Alexandratos
Grzegorz Bujacz
Alexander Wlodawer
National Cancer Institute · USInstitute of Bioorganic Chemistry, Polish Academy of Sciences · PLUniversity of Łódź · PL

Funding

Protein StructureZIABC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2009 to 2025
$27.5M
PROTEIN STRUCTUREZ01BC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2000 to 2008
$3.2M
Intramural NIH HHS Z01 BC010348
6 · The paper itself

Abstract

Integrase (IN) is one of only three enzymes encoded in the genomes of all retroviruses, and is the one least characterized in structural terms. IN catalyzes processing of the ends of a DNA copy of the retroviral genome and its concerted insertion into the chromosome of the host cell. The protein consists of three domains, the central catalytic core domain flanked by the N-terminal and C-terminal domains, the latter being involved in DNA binding. Although the Protein Data Bank contains a number of NMR structures of the N-terminal and C-terminal domains of HIV-1 and HIV-2, simian immunodeficiency virus and avian sarcoma virus IN, as well as X-ray structures of the core domain of HIV-1, avian sarcoma virus and foamy virus IN, plus several models of two-domain constructs, no structure of the complete molecule of retroviral IN has been solved to date. Although no experimental structures of IN complexed with the DNA substrates are at hand, the catalytic mechanism of IN is well understood by analogy with other nucleotidyl transferases, and a variety of models of the oligomeric integration complexes have been proposed. In this review, we present the current state of knowledge resulting from structural studies of IN from several retroviruses. We also attempt to reconcile the differences between the reported structures, and discuss the relationship between the structure and function of this enzyme, which is an important, although so far rather poorly exploited, target for designing drugs against HIV-1 infection.

Indexed as

Protein Structure, TertiaryAcquired Immunodeficiency SyndromeAmino Acid SequenceHumansIntegrasesModels, MolecularMolecular Sequence DataRetroviridaeSequence Homology, Amino AcidViral ProteinsIntegrasesViral Proteins

Identifiers

PMID19490099
PMCPMC2747025
OpenAlexW2146058166

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.