Evidence map›Paper›PMID 9291093›Full record

ReviewMolecular biology reports1997

Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin.

J R Davie

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.7field-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

20 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
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  13. Review
  14. Review
  15. Multiple subnuclear targeting signals of the leukemia-related AML1/ETO and ETO repressor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  16. Article
  17. Article
  18. Article
  19. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  20. Intranuclear targeting of AML/CBFalpha regulatory factors to nuclear matrix-associated transcriptional domains.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

1 author at 1 institution in 1 country.

J R DavieDepartment of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Canada.
University of Manitoba · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear matrix, the RNA-protein skeleton of the nucleus, has a role in the organization and function of nuclear DNA. Nuclear processes associated with the nuclear matrix include transcription, replication and dynamic histone acetylation. Nuclear matrix proteins, which are tissue and cell type specific, are altered with transformation and state of differentiation. Transcription factors are associated with the nuclear matrix, with the spectra of nuclear matrix bound factors being cell type specific. There is compelling evidence that the transcription machinery is anchored to the nuclear matrix, and the chromatin fiber is spooled through this complex. Transcriptionally active chromatin domains are associated with dynamically acetylated histones. The energy exhaustive process of dynamic histone acetylation has several functions. Acetylation of the N-terminal tails of the core histones alters nucleosome and higher order chromatin structure, aiding transcriptional elongation and facilitating the binding of transcription factors to nucleosomes associated with regulatory DNA sequences. Histone acetylation can manipulate the interactions of regulatory proteins that bind to the N-terminal tails of the core histones. Lastly, dynamic acetylation may contribute to the transient attachment of transcriptionally active chromatin to the nuclear matrix. Reversible histone acetylation is catalyzed by histone acetyltransferase and deacetylase, enzymes associated with the nuclear matrix. The recent isolation and characterization of histone acetyltransferase and deacetylase reveals that these enzymes are related to transcriptional regulators, providing us with new insights about how these enzymes are targeted to nuclear matrix sites engaged in transcription.

Indexed as

Saccharomyces cerevisiae ProteinsTranscription, GeneticAcetylationAcetyltransferasesAnimalsChickensChromatinDNA ReplicationHistone AcetyltransferasesHistone DeacetylasesHistonesHumansNuclear MatrixNucleosomesRNATetrahymenaAcetyltransferasesChromatinHistone AcetyltransferasesHistone DeacetylasesHistonesNucleosomesRNASaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID9291093
OpenAlexW78763444

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.