Evidence map›Paper›PMID 10860984›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

The histone deacetylase-3 complex contains nuclear receptor corepressors.

Y D Wen, V Perissi, L M Staszewski, W M Yang, A Krones, C K Glass, M G Rosenfeld, E Seto

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.

0numbers the graph read from it
0cells of the map it votes in
171citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

171 citing papers in PubMed, 378 citations in OpenAlex.

  1. Article
  2. Article
  3. HDAC3 Regulates Transcriptional Networks Governing Decidualization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
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  5. Article
  6. Review
  7. Article
  8. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Epigenetics as a versatile regulator of fibrosis.Journal of translational medicine · 2023
    Review
  18. Article
  19. Balanced control of thermogenesis by nuclear receptor corepressors in brown adipose tissue.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Review

111 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

8 authors at 3 institutions in 1 country.

Y D WenDepartment of Chemistry, H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, FL 33612, USA.
V Perissi
L M Staszewski
W M Yang
A Krones
C K Glass
M G Rosenfeld
E Seto
University of South Florida · USHoward Hughes Medical Institute · USMoffitt Cancer Center · US

Funding

FUNCTIONAL ANALYSIS OF MAMMALIAN HISTONE DEACETYLASESR01GM058486 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI SETO, EDWARD · 1999 to 2006
$2.3M
REGULATION OF METALLOTHIONEIN GENE EXPRESSIONR01ES009262 · NIEHS · UNIVERSITY OF SOUTH FLORIDA · PI SETO, EDWARD · 1998 to 2002
$698k
NIEHS NIH HHS ES09262NIGMS NIH HHS GM58486NIGMS NIH HHS R01 GM058486
6 · The paper itself

Abstract

Acetylation and deacetylation of nucleosomal histones have profound effects on gene transcription in all eukaryotes. In humans, three highly homologous class I and four class II histone deacetylase (HDAC) enzymes have been identified to date. The class I deacetylases HDAC1 and HDAC2 are components of multisubunit complexes, one of which could associate with the nuclear hormone receptor corepressor, N-CoR. N-CoR also interacts with class II deacetylases HDAC4, HDAC5, and HDAC7. In comparison with HDAC1 and HDAC2, HDAC3 remains relatively uncharacterized, and very few proteins have been shown to interact with HDAC3. Using an affinity purification approach, we isolated an enzymatically active HDAC3 complex that contained members of the nuclear receptor corepressor family. Deletion analysis of N-CoR revealed that HDAC3 binds multiple N-CoR regions in vitro and that all of these regions are required for maximal binding in vivo. The N-CoR domains that interact with HDAC3 are distinct from those that bind other HDACs. Transient overexpression of HDAC3 and microinjection of Abs against HDAC3 showed that a component of transcriptional repression mediated by N-CoR depends on HDAC3. Interestingly, data suggest that interaction with a region of N-CoR augments the deacetylase activity of HDAC3. These results provide a possible molecular mechanism for HDAC3 regulation and argue that N-CoR is a platform in which distinct domains can interact with most of the known HDACs.

Indexed as

AcetylationAmino Acid SequenceHeLa CellsHistone DeacetylasesHumansMolecular Sequence DataReceptors, Cytoplasmic and NuclearSignal TransductionHistone DeacetylasesReceptors, Cytoplasmic and Nuclear

Identifiers

PMID10860984
PMCPMC16523
OpenAlexW2092349389

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.