Evidence map›Paper›PMID 38267583›Full record

ArticleNature2024

HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor.

Liran Fu, Erika N Weiskopf, Onno Akkermans, Nicholas A Swanson, Shiya Cheng, Thomas U Schwartz, Dirk Görlich

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
19.6field-weighted citation impact, top 1% 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

59 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. MX2 Mediates Collapse of the HIV-1 Capsid.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  18. Article
  19. Article
  20. Review
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

7 authors at 3 institutions in 2 countries.

Liran Fu *Department of Cellular Logistics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0009-0005-2980-5165
Erika N Weiskopf *Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0003-2098-9824
Onno Akkermans *Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-8436-2281
Nicholas A SwansonDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0001-6808-6750
Shiya ChengDepartment of Meiosis, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0000-0001-8643-8748
Thomas U SchwartzDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA. tus@mit.edu.ORCID 0000-0001-8012-1512
Dirk GörlichDepartment of Cellular Logistics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. goerlich@mpinat.mpg.de.ORCID 0000-0002-4343-5210
Massachusetts Institute of Technology · USMax Planck Institute for Multidisciplinary SciencesMax Planck Institute for the Study of Religious and Ethnic Diversity · DE

Funding

Structure-Function of Nucleo-Cytoplasmic CommunicationR35GM141834 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2021 to 2025
$2.0M
Mechanism of nuclear pore passage of the HIV-1 capsidR21AI179432 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2023 to 2024
$434k
NIAID NIH HHS R21 AI179432NIGMS NIH HHS R35 GM141834
6 · The paper itself

Abstract

HIV-1 infection requires nuclear entry of the viral genome. Previous evidence suggests that this entry proceeds through nuclear pore complexes (NPCs), with the 120 × 60 nm capsid squeezing through an approximately 60-nm-wide central channel

Indexed as

CapsidCapsid ProteinsGlycineHIV-1Nuclear PoreNuclear Pore Complex ProteinsPhenylalanineActive Transport, Cell NucleusHumansPermeabilitySolubilityVirus InternalizationCapsid ProteinsGlycineNuclear Pore Complex ProteinsPhenylalanine

Identifiers

PMID38267583
PMCPMC10881386
OpenAlexW4391160417

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.