Evidence map›Paper›PMID 7559784›Full record

ArticleThe Journal of cell biology1995

A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones.

H Taniura, C Glass, L Gerace

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

117 citing papers in PubMed, 292 citations in OpenAlex.

  1. Review
  2. Review
  3. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
    Article
  4. Article
  5. Cells · 2025
    Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Three-dimensional chromatin organization in cardiac development and disease.Journal of molecular and cellular cardiology · 2021
    Review
  17. Review
  18. Close to the edge: Heterochromatin at the nucleolar and nuclear peripheries.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  19. Review
  20. Review

57 more citing papers are in PubMed but not listed here.

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.

H TaniuraDepartment of Cell Biology, Scripps Research Institute, La Jolla, California 92037, USA.
C Glass
L Gerace
Scripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interaction of chromatin with the nuclear envelope and lamina is thought to help determine higher order chromosome organization in the interphase nucleus. Previous studies have shown that nuclear lamins bind chromatin directly. Here we have localized a chromatin binding site to the carboxyl-terminal tail domains of both A- and B-type mammalian lamins, and have characterized the biochemical properties of this binding in detail. Recombinant glutathione-S-transferase fusion proteins containing the tail domains of mammalian lamins C, B1, and B2 were analyzed for their ability to associate with rat liver chromatin fragments immobilized on microtiter plate wells. We found that all three lamin tails specifically bind to chromatin with apparent KdS of 120-300 nM. By examining a series of deletion mutants, we have mapped the chromatin binding region of the lamin C tail to amino acids 396-430, a segment immediately adjacent to the rod domain. Furthermore, by analysis of chromatin subfractions, we found that core histones constitute the principal chromatin binding component for the lamin C tail. Through cooperativity, this lamin-histone interaction could be involved in specifying the high avidity attachment of chromatin to the nuclear envelope in vivo.

Indexed as

Lamin Type ALamin Type BAmino Acid SequenceAnimalsBinding SitesChromatinDNA-Binding ProteinsHistonesHumansLaminsLiverMolecular Sequence DataNuclear ProteinsRatsRecombinant Fusion ProteinsChromatinDNA-Binding ProteinsHistoneslamin CLaminsLamin Type ALamin Type BNuclear ProteinsRecombinant Fusion Proteins

Identifiers

PMID7559784
PMCPMC2120604
OpenAlexW1985092753

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.