Evidence map›Paper›PMID 29237846›Full record

ArticleJournal of virology2018

The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α.

Damien Morger, Franziska Zosel, Martin Bühlmann, Sara Züger, Maximilian Mittelviefhaus, Benjamin Schuler, Jeremy Luban, Markus G Grütter

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2018. 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
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019
    Review
  16. Article
  17. Role of the Ubiquitin Proteasome System (UPS) in the HIV-1 Life Cycle.International journal of molecular sciences · 2019
    Review
  18. Review
  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

8 authors at 2 institutions in 2 countries.

Damien MorgerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Franziska ZoselDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Martin BühlmannDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Sara ZügerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Maximilian MittelviefhausDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Benjamin SchulerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Jeremy LubanProgram in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Markus G GrütterDepartment of Biochemistry, University of Zurich, Zurich, Switzerland gruetter@bioc.uzh.ch.
University of Zurich · CHUniversity of Massachusetts Chan Medical School · US

Funding

Human Genes that Influence HIV-1 Replication, Pathogenesis, and Immunity in IVDUsDP1DA034990 · NIDA · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUBAN, JEREMY · 2012 to 2016
$4.1M
Boosting cell-intrinsic innate immune recognition of HIV-1 by dendritic cellsR01AI111809 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUBAN, JEREMY · 2014 to 2017
$2.4M
NIAID NIH HHS R01 AI111809NIDA NIH HHS DP1 DA034990
6 · The paper itself

Abstract

Rhesus TRIM5α (rhTRIM5α) potently restricts replication of human immunodeficiency virus type 1 (HIV-1). Restriction is mediated through direct binding of the C-terminal B30.2 domain of TRIM5α to the assembled HIV-1 capsid core. This host-pathogen interaction involves multiple capsid molecules within the hexagonal HIV-1 capsid lattice. However, the molecular details of this interaction and the precise site at which the B30.2 domain binds remain largely unknown. The human orthologue of TRIM5α (hsTRIM5α) fails to block infection by HIV-1 both

Indexed as

AnimalsAntiviral Restriction FactorsCapsid ProteinsCarrier ProteinsCrystallography, X-RayCyclophilin AHIV-1Host-Pathogen InteractionsHumansMacaca mulattaModels, MolecularMutationProtein BindingProtein ConformationProtein Interaction Domains and MotifsProteinsAntiviral Restriction FactorsCapsid ProteinsCarrier ProteinsCyclophilin AProteinsRecombinant ProteinsTRIM5(alpha) protein, rhesus monkeyTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesaffinityB30.2bindingcapsidCypAHIV-1interactionspecies specificityTRIM5TRIM5α

Identifiers

PMID29237846
PMCPMC5809731
OpenAlexW2774934462

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.