Evidence map›Paper›PMID 15958388›Full record

ArticleThe Journal of biological chemistry2005

Processing of viral DNA ends channels the HIV-1 integration reaction to concerted integration.

Min Li, Robert Craigie

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

77 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. The Integrase: An Overview of a Key Player Enzyme in the Antiviral Scenario.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Foamy Virus Integrase in Development of Viral Vector for Gene Therapy.Journal of microbiology and biotechnology · 2020
    Review
  11. Efficient Nonviral Stable Transgenesis Mediated by Retroviral Integrase.Molecular therapy. Methods & clinical development · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Retroviral DNA Integration.Chemical reviews · 2016
    Review
  18. Article
  19. Article
  20. Review

17 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

2 authors at 2 institutions in 1 country.

Min LiLaboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.
Robert Craigie
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

STUDIES ON THE MECHANISM OF RETROVIRAL DNA INTEGRATIONZ01DK036108 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI CRAIGIE, ROBERT · 1988 to 2006
–
Intramural NIH HHS Z99 DK999999
6 · The paper itself

Abstract

Retroviral DNA made by reverse transcription is blunt-ended, and the viral integrase protein must remove two nucleotides from each 3' end prior to integration into chromosomal DNA. Under most reaction conditions for integration in vitro, the majority of the reaction products are "half-site" products that result from integration of only one viral DNA end into one strand of the target DNA. Preprocessed DNA substrates are more efficient substrates for half-site reactions than are blunt-ended substrates, which require the removal of two nucleotides prior to integration. In contrast, we find that blunt-ended DNA is a better substrate for the biologically relevant reaction of concerted integration of pairs of viral DNA ends. The reaction pathway is channeled to concerted integration, and half-site integration products are reduced with blunt-ended DNA substrate that must first be processed by integrase. In addition, the terminal nucleotide requirements for concerted integration are more stringent than for the half-site reaction. Longer DNA is more efficient for the concerted reaction than is shorter DNA that is capable of efficient half-site integration. This suggests that nonspecific interactions of integrase with viral DNA distant from the termini contribute to the assembly of a complex that is competent for concerted integration. Finally, differential effects of mutation of a residue in the C-terminal domain of integrase on concerted versus half-site integration implicate protein-protein interactions involving this domain as important for concerted integration.

Indexed as

DNA, ViralVirus IntegrationDNADose-Response Relationship, DrugEscherichia coliHIV-1HIV IntegraseModels, GeneticMutationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRetroviridaeSaltsDNADNA, ViralHIV IntegraseSalts

Identifiers

PMID15958388
PMCPMC8742673
OpenAlexW2061205853

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.