Evidence map›Paper›PMID 23322775›Full record

ArticleThe Journal of biological chemistry2013

Architecture and assembly of HIV integrase multimers in the absence of DNA substrates.

Ravi Shankar Bojja, Mark D Andrake, George Merkel, Steven Weigand, Roland L Dunbrack, Anna Marie Skalka

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Porphobilinogen synthase: An equilibrium of different assemblies in human health.Progress in molecular biology and translational science · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Retroviral Integrase: Then and Now.Annual review of virology · 2015
    Review
  11. Article
  12. Article
  13. HIV-1 integrase multimerization as a therapeutic target.Current topics in microbiology and immunology · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

6 authors.

Ravi Shankar BojjaInstitute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA.
Mark D Andrake
George Merkel
Steven Weigand
Roland L Dunbrack
Anna Marie Skalka

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Dietmar J Kappes · 1985 to 2026
$138.8M
INTEGRATION OF RETROVIRAL DNA--ACCESSING HOST TARGET DNAR01CA071515 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI KATZ, RICHARD ALAN · 1996 to 2016
$7.6M
STRUCTURE/FUNCTION OF INTEGRASER01AI040385 · NIAID · RESEARCH INST OF FOX CHASE CAN CTR · PI ANDRAKE, MARK DAVID · 1997 to 2016
$7.1M
Bayesian Statistics and Algorithms for Homology ModelingR01GM084453 · NIGMS · RESEARCH INST OF FOX CHASE CAN CTR · PI DUNBRACK, ROLAND L · 2008 to 2016
$2.6M
NCI NIH HHS CA006927NCI NIH HHS CA71515NCI NIH HHS P30 CA006927NCI NIH HHS R01 CA071515NIAID NIH HHS AI40385NIAID NIH HHS R01 AI040385NIGMS NIH HHS R01 GM084453
6 · The paper itself

Abstract

We have applied small angle x-ray scattering and protein cross-linking coupled with mass spectrometry to determine the architectures of full-length HIV integrase (IN) dimers in solution. By blocking interactions that stabilize either a core-core domain interface or N-terminal domain intermolecular contacts, we show that full-length HIV IN can form two dimer types. One is an expected dimer, characterized by interactions between two catalytic core domains. The other dimer is stabilized by interactions of the N-terminal domain of one monomer with the C-terminal domain and catalytic core domain of the second monomer as well as direct interactions between the two C-terminal domains. This organization is similar to the "reaching dimer" previously described for wild type ASV apoIN and resembles the inner, substrate binding dimer in the crystal structure of the PFV intasome. Results from our small angle x-ray scattering and modeling studies indicate that in the absence of its DNA substrate, the HIV IN tetramer assembles as two stacked reaching dimers that are stabilized by core-core interactions. These models of full-length HIV IN provide new insight into multimer assembly and suggest additional approaches for enzyme inhibition.

Indexed as

Protein MultimerizationProtein Structure, TertiaryAmino Acid SubstitutionBiocatalysisCircular DichroismCross-Linking ReagentsDNAEdetic AcidEnzyme StabilityHIV IntegraseModels, MolecularMutationProtein BindingScattering, Small AngleSodium ChlorideSubstrate SpecificityCross-Linking ReagentsDNAEdetic AcidHIV IntegraseSodium ChlorideUrea

Identifiers

PMID23322775
PMCPMC3591645

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.