The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family
Open accessAbstract
Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated. Analysis of the predicted amino acid sequence of HDAC3 revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa. The HDAC3 protein is 50% identical in DNA sequence and 53% identical in protein sequence compared with the previously cloned human HDAC1. Comparison of the HDAC3 sequence with human HDAC2 also yielded similar results, with 51% identity in DNA sequence and 52% identity in protein sequence. The expressed HDAC3 protein is functionally active because it possesses histone deacetylase activity, represses transcription when tethered to a promoter, and binds transcription factor YY1. Similar to HDAC1 and HDAC2, HDAC3 is ubiquitously expressed in many different cell types.
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Cited by
Phiel, C. J., Zhang, F., Huang, E. Y., Guenther, M. G., Lazar, M. A., & Klein, P. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101287200 · Cited by 1,758
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Self-citationGregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456
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A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
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Metadata
- Authors
- Yang, W.-M., Yao, Y.-L., Sun, J.-M., Davie, J. R., & Seto, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-10
- Volume
- 272
- Issue
- 44
- Pages
- 28001-28007
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2063460322
- Cited by
- 438
- References
- 36
- FWCI
- 10.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Yang, W.-M., Yao, Y.-L., Sun, J.-M., Davie, J. R., & Seto, E. (1997). Isolation and Characterization of cDNAs Corresponding to an Additional Member of the Human Histone Deacetylase Gene Family. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.44.28001
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
