Evidence map›Paper›PMID 15837933›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors.

Anna Codina, James D Love, Yun Li, Mitchell A Lazar, David Neuhaus, John W R Schwabe

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

64 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. Epigenetics.Advances in experimental medicine and biology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. 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
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Integrative regulation of physiology by histone deacetylase 3.Nature reviews. Molecular cell biology · 2019
    Review

4 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

6 authors at 3 institutions in 2 countries.

Anna CodinaMedical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom.
James D Love
Yun Li
Mitchell A Lazar
David Neuhaus
John W R Schwabe
University of Pennsylvania · USMedical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

REV-ERB Nuclear Receptors in Circadian Rhythm and MetabolismR01DK045586 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1992 to 2026
$12.0M
THYROID HORMONE RECEPTORS-REGULATION AND FUNCTIONR37DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI LAZAR, MITCHELL A. · 1998 to 2017
$8.8M
THYROID HORMONE RECEPTORS--REGULATION AND FUNCTIONR01DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1991 to 2026
$4.9M
NIDDK NIH HHS DK43806NIDDK NIH HHS DK45586NIDDK NIH HHS R01 DK043806NIDDK NIH HHS R01 DK045586NIDDK NIH HHS R37 DK043806
6 · The paper itself

Abstract

SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) and NCoR (nuclear receptor corepressor) are transcriptional corepressors that play an essential role in the regulation of development and metabolism. This role is achieved, in part, through the recruitment of a key histone deacetylase (HDAC3), which is itself indispensable for cell viability. The assembly of HDAC3 with the deacetylase activation domain (DAD) of SMRT and NCoR is required for activation of the otherwise inert deacetylase. The DAD comprises an N-terminal DAD-specific motif and a C-terminal SANT (SWI3/ADA2/NCoR/TFIIIB)-like domain. We report here the solution structure of the DAD from SMRT, which reveals a four-helical structure. The DAD differs from the SANT (and MYB) domains in that (i) it has an additional N-terminal helix and (ii) there is a notable hydrophobic groove on the surface of the domain. Structure-guided mutagenesis, combined with interaction assays, showed that residues in the vicinity of the hydrophobic groove are required for interaction with (and hence activation of) HDAC3. Importantly, one surface-exposed lysine is required for activation of HDAC3, but not for interaction. This lysine may play a uniquely important role in the mechanism of activating HDAC3.

Indexed as

Amino Acid SequenceCalorimetryEnzyme ActivationEscherichia coliHistone Deacetylase 3Histone DeacetylasesKineticsModels, MolecularMolecular Sequence DataNuclear ProteinsNuclear Receptor Co-Repressor 1Protein ConformationProtein Structure, SecondaryRecombinant ProteinsRepressor ProteinsSequence AlignmentHistone Deacetylase 3Histone DeacetylasesNuclear ProteinsNuclear Receptor Co-Repressor 1Recombinant ProteinsRepressor Proteins

Identifiers

PMID15837933
PMCPMC1087922
OpenAlexW2160093177

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.