Evidence map›Paper›PMID 8223451›Full record

ArticleThe EMBO journal1993

The alpha-helical rod domain of human lamins A and C contains a chromatin binding site.

C A Glass, J R Glass, H Taniura, K W Hasel, J M Blevitt, L Gerace

Abstract read
In one paragraph

Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.1field-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

44 citing papers in PubMed, 157 citations in OpenAlex.

  1. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
    Article
  2. Cells · 2025
    Review
  3. Epigenetics inCells · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Spatial chromatin organization and gene regulation at the nuclear lamina.Current opinion in genetics & development · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  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

6 authors at 1 institution in 1 country.

C A GlassScripps Research Institute, Department of Cell Biology, La Jolla, CA 92037.
J R Glass
H Taniura
K W Hasel
J M Blevitt
L Gerace
Scripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined regions of human lamins A and C involved in binding to surfaces of mitotic chromosomes. An Escherichia coli expression system was used to produce full-length lamin A and lamin C, and truncated lamins retaining the central alpha-helical rod domain (residues 34-388) but lacking various amounts of the amino-terminal 'head' and carboxy-terminal 'tail' domains. We found that lamin A, lamin C and lamin fragments lacking the head domain and tail sequences distal to residue 431 efficiently assembled into paracrystals and strongly associated with mitotic chromosomes. Furthermore, the lamin rod domain also associated with chromosomes, although efficient chromosome coating required the pH 5-6 conditions needed to assemble the rod into higher order structures. Biochemical assays showed that chromosomes substantially reduced the critical concentration for assembly of lamin polypeptides into pelletable structures. Association of the lamin rod with chromosomes was abolished by pretrypsinization of chromosomes, and was not seen for vimentin (which possesses a similar rod domain). These data demonstrate that the alpha-helical rod of lamins A and C contains a specific chromosome binding site. Hence, the central rod domain of intermediate filament proteins can be involved in interactions with other cellular structures as well as in filament assembly.

Indexed as

AnimalsCHO CellsChromatinChromosomesCricetinaeDNA Mutational AnalysisHumansHydrogen-Ion ConcentrationIntermediate FilamentsLaminsLamin Type AMicroscopy, ElectronMitosisNuclear ProteinsPeptide FragmentsProtein ConformationChromatinlamin CLaminsLamin Type ANuclear ProteinsPeptide FragmentsRecombinant Fusion ProteinsTrypsinVimentin

Identifiers

PMID8223451
PMCPMC413739
OpenAlexW2175346537

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.