Evidence map›Paper›PMID 22872640›Full record

ArticleThe Journal of biological chemistry2012

Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2).

Ross Larue, Kushol Gupta, Christiane Wuensch, Nikolozi Shkriabai, Jacques J Kessl, Eric Danhart, Lei Feng, Oliver Taltynov, Frauke Christ, Gregory D Van Duyne and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

42 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Complex Relationships between HIV-1 Integrase and Its Cellular Partners.International journal of molecular sciences · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  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

13 authors at 5 institutions in 2 countries.

Ross LarueCenter for Retrovirus Research and Comprehensive Cancer Center, College of Pharmacy, The Ohio State University, Columbus, Ohio 43210, USA.
Kushol Gupta
Christiane Wuensch
Nikolozi Shkriabai
Jacques J Kessl
Eric Danhart
Lei Feng
Oliver Taltynov
Frauke Christ
Gregory D Van Duyne
Zeger Debyser
Mark P Foster
Mamuka Kvaratskhelia
Comprehensive Blood & Cancer Center · USKU Leuven · BEThe Ohio State University · USHoward Hughes Medical Institute · USUniversity of Pennsylvania · US

Funding

Structure and function of HIV-1 integraseR01AI062520 · NIAID · UNIVERSITY OF COLORADO DENVER · PI KVARATSKHELIA, MAMUKA · 2006 to 2020
$5.3M
MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
Structural and Dynamics in Allosteric Gene RegulationR01GM077234 · NIGMS · OHIO STATE UNIVERSITY · PI FOSTER, MARK P. · 2007 to 2010
$1.2M
Inhibitors Targeting HIV Integrase MultimersR21AI097044 · NIAID · OHIO STATE UNIVERSITY · PI KESSL, JACQUES J. · 2011 to 2012
$419k
NIAID NIH HHS AI062520NIAID NIH HHS AI097044NIAID NIH HHS R01 AI062520NIAID NIH HHS R21 AI097044NIGMS NIH HHS GM077234NIGMS NIH HHS R01 GM077234
6 · The paper itself

Abstract

Transportin 3 (TNPO3 or TRN-SR2) has been shown to be an important cellular factor for early steps of lentiviral replication. However, separate studies have implicated distinct mechanisms for TNPO3 either through its interaction with HIV-1 integrase or capsid. Here we have carried out a detailed biophysical characterization of TNPO3 and investigated its interactions with viral proteins. Biophysical analyses including circular dichroism, analytical ultracentrifugation, small-angle x-ray scattering, and homology modeling provide insight into TNPO3 architecture and indicate that it is highly structured and exists in a monomer-dimer equilibrium in solution. In vitro biochemical binding assays argued against meaningful direct interaction between TNPO3 and the capsid cores. Instead, TNPO3 effectively bound to the functional intasome but not to naked viral DNA, suggesting that TNPO3 can directly engage the HIV-1 IN tetramer prebound to the cognate DNA. Mass spectrometry-based protein footprinting and site-directed mutagenesis studies have enabled us to map several interacting amino acids in the HIV-1 IN C-terminal domain and the cargo binding domain of TNPO3. Our findings provide important information for future genetic analysis to better understand the role of TNPO3 and its interacting partners for HIV-1 replication.

Indexed as

beta KaryopherinsCircular DichroismDNA, ViralHIV-1HIV IntegraseHumansMass SpectrometryProtein BindingProtein Structure, TertiaryScattering, Small AngleVirus ReplicationX-Ray Diffractionbeta KaryopherinsDNA, ViralHIV IntegraseTNPO3 protein, human

Identifiers

PMID22872640
PMCPMC3464514
OpenAlexW1969924129

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.