Evidence map›Paper›PMID 10077600›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

The tail domain of lamin Dm0 binds histones H2A and H2B.

M Goldberg, A Harel, M Brandeis, T Rechsteiner, T J Richmond, A M Weiss, Y Gruenbaum

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
    Article
  3. Cells · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Close to the edge: Heterochromatin at the nucleolar and nuclear peripheries.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Laminopathies: what can humans learn from fruit flies.Cellular & molecular biology letters · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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 2 institutions in 1 country.

M GoldbergDepartment of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
A Harel
M Brandeis
T Rechsteiner
T J Richmond
A M Weiss
Y Gruenbaum
Jerusalem College of Technology · ILHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In multicellular organisms, the higher order organization of chromatin during interphase and the reassembly of the nuclear envelope during mitosis are thought to involve an interaction between the nuclear lamina and chromatin. The nuclear distribution of lamins and of peripheral chromatin is highly correlated in vivo, and lamins bind specifically to chromatin in vitro. Deletion mutants of Drosophila lamin Dm0 were expressed to map regions of the protein that are required for its binding to chromosomes. The binding activity requires two regions in the lamin Dm0 tail domain. The apparent Kd of binding of the lamin Dm0 tail domain was found to be approximately 1 microM. Chromatin subfractions were examined to search for possible target molecules for the binding of lamin Dm0. Isolated polynucleosomes, nucleosomes, histone octamer, histone H2A/H2B dimer, and histones H2A or H2B displaced the binding of lamin Dm0 tail to chromosomes. This displacement was specific, because polyamines or proteins such as histones H1, H3, or H4 did not displace the binding of the lamin Dm0 tail to chromosomes. In addition, DNA sequences, including M/SARs, did not interfere with the binding of lamin Dm0 tail domain to chromosomes. Taken together, these results suggest that the interaction between the tail domain of lamin Dm0 and histones H2A and H2B may mediate the attachment of the nuclear lamina to chromosomes in vivo.

Indexed as

Drosophila ProteinsAmino Acid SequenceAnimalsBinding SitesDrosophilaHistonesLaminsMolecular Sequence DataNuclear ProteinsProtein BindingSequence DeletionDrosophila ProteinsHistonesLaminsLam protein, DrosophilaNuclear Proteins

Identifiers

PMID10077600
PMCPMC15858
OpenAlexW1979220220

What OpenQuestion holds

Texttitle and abstract
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.