The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
NuRD and SIN3
Abstract
Transcription repression mediated through histone deacetylase (HDAC) complexes is widespread, and mechanisms by which HDAC complexes act have been revealed by extensive studies in vitro and in cell culture. However, until recently, little has been known about the developmental roles of histone deacetylation. Mutants now exist for a number of members of the two major HDAC complexes (NuRD and SIN3) and some associated proteins. The emerging picture is that these complexes have specific functions in development, rather than being required for most cellular processes.
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In the citing paper
“Generally, when histones are acetylated, chromatin becomes loosely packed euchromatin and gene expression is activated. In contrast, deacetylated histones lead to condensed heterochromatin and repressed gene expression [25].”
From Stem Cell Factor SALL4 Represses the Transcriptions of PTEN and SALL1 through an Epigenetic Repressor Complex (2009) · cites this paper as [25]
In the citing paper
“This is consistent with the fact that both genes encode proteins involved in histone modification and chromatin remodeling [21,23-25,30-33].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [30]
Citations
Cites
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Retinoblastoma protein recruits histone deacetylase to repress transcription
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Nuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
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Cited by
Sorted by citations
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Cooperation between Complexes that Regulate Chromatin Structure and Transcription
Narlikar, G. J., Fan, H.-Y., & Kingston, R. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00654-2 · Cited by 1,486
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,275
HDAC family: What are the cancer relevant targets?
Witt, O., Deubzer, H. E., Milde, T., & Oehme, I. (2009) · Cancer Letters · doi:10.1016/j.canlet.2008.08.016 · Cited by 1,069
Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783
Metadata
- Authors
- Ahringer, J.
- Affiliations
- Wellcome Trust (GB)
- Corresponding author
- Ahringer, Julie
- ORCID
- Ahringer, Julie
- Venue
- Trends in Genetics
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 16
- Issue
- 8
- Pages
- 351-356
- ISSN
- 0168-9525 (ISSN-L)
- OpenAlex
- W2027297574
- Cited by
- 388
- References
- 63
- Citations by year
- 2026: 8 · 2025: 5 · 2024: 2 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 7 · 2019: 8 · 2018: 4 · 2017: 11 · 2016: 8 · 2015: 13 · 2014: 15 · 2013: 16 · 2012: 16
- FWCI
- 2.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Genetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (054523)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- NuRD complex, histone deacetylase complex, transcriptional repression, histone deacetylation, developmental gene regulation, chromatin regulation
- MeSH terms
- Animals, Histone Deacetylases, Humans, Models, Biological, Receptors, Cell Surface, Transcription, Genetic, Arabidopsis, ras Proteins, Macromolecular Substances, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Sin3 Histone Deacetylase and Corepressor Complex
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