Evidence map›Paper›PMID 27528606›Full record

ArticleThe Journal of biological chemistry2016

Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins.

Michael Soniat, Tolga Cağatay, Yuh Min Chook

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    Review
  14. Nucleosome proteostasis and histone turnover.Frontiers in molecular biosciences · 2022
    Review
  15. Article
  16. Article
  17. Article
  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

3 authors at 1 institution in 1 country.

Michael SoniatFrom the Department of Pharmacology, University of Texas Southwestern, Dallas, Texas 75390.
Tolga CağatayFrom the Department of Pharmacology, University of Texas Southwestern, Dallas, Texas 75390.
Yuh Min ChookFrom the Department of Pharmacology, University of Texas Southwestern, Dallas, Texas 75390 yuhmin.chook@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

UT Southwestern Medical Center Simmons Comprehensive Cancer CenterP30CA142543 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI Sandi Leigh Pruitt · 2010 to 2026
$53.7M
Structures and Mechanisms of Nuclear Import and ExportR01GM069909 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 2004 to 2020
$5.8M
Nucleocytoplasmic transport: a target for cellular controlU01GM098256 · NIGMS · ROCKEFELLER UNIVERSITY · PI AITCHISON, JOHN D., ROUT, MICHAEL P · 2011 to 2014
$3.0M
NCI NIH HHS P30 CA142543NIGMS NIH HHS R01 GM069909NIGMS NIH HHS U01 GM098256
6 · The paper itself

Abstract

N-terminal tails of histones H3 and H4 are known to bind several different Importins to import the histones into the cell nucleus. However, it is not known what binding elements in the histone tails are recognized by the individual Importins. Biochemical studies of H3 and H4 tails binding to seven Importins, Impβ, Kapβ2, Imp4, Imp5, Imp7, Imp9, and Impα, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kapβ2 and Imp5 with K

Indexed as

Cell Cycle ProteinsHistonesHumansKaryopherinsMolecular ChaperonesMutagenesisProtein BindingProtein DomainsASF1B protein, humanCell Cycle ProteinsHistonesKaryopherinsMolecular Chaperoneschromatin regulationhistonehistone acetylationimportinkaryopherinnuclear importnuclear localization signalnuclear transportprotein import

Identifiers

PMID27528606
PMCPMC5076525
OpenAlexW2507939558

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.