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Cited by 938

The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.

Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression

Open access
Laherty, Carol D, Yang, Wen-Ming, Sun, Jian-Min, Davie, James R, Seto, Edward, Eisenman, Robert N·1997·Cell

Abstract

Transcriptional repression by Mad-Max heterodimers requires interaction of Mad with the corepressors mSin3A/B. Sin3p, the S. cerevisiae homolog of mSin3, functions in the same pathway as Rpd3p, a protein related to two recently identified mammalian histone deacetylases, HDAC1 and HDAC2. Here, we demonstrate that mSin3A and HDAC1/2 are associated in vivo. HDAC2 binding requires a conserved region of mSin3A capable of mediating transcriptional repression. In addition, Mad1 forms a complex with mSin3 and HDAC2 that contains histone deacetylase activity. Trichostatin A, an inhibitor of histone deacetylases, abolishes Mad repression. We propose that Mad-Max functions by recruiting the mSin3-HDAC corepressor complex that deacetylates nucleosomal histones, producing alterations in chromatin structure that block transcription.

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Metadata

Authors
Laherty, C. D., Yang, W.-M., Sun, J.-M., Davie, J. R., Seto, E., & Eisenman, R. N.
Venue
Cell
Publisher
Elsevier BV
Published
1997-05
Volume
89
Issue
3
Pages
349-356
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2104788426
Cited by
938
References
48
FWCI
31.27
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80215-9
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Laherty, C. D., Yang, W.-M., Sun, J.-M., Davie, J. R., Seto, E., & Eisenman, R. N. (1997). Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression. Cell. https://doi.org/10.1016/s0092-8674(00)80215-9

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