The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
Cloning and Characterization of a Novel Human Class I Histone Deacetylase That Functions as a Transcription Repressor
Open accessAbstract
Histone acetylation alters chromatin state by modifying lysines on histone and plays an important role in modulating gene transcription. A dynamic balance of histone acetylation/deacetylation is maintained by histone acetyltransferases and histone deacetylases. Emerging evidence suggests that a family of histone deacetylases may exist to regulate diverse cellular functions, including chromatin structure, gene expression, cell cycle progression, and oncogenesis. We describe here a novel human histone deacetylase, named HDAC8, cloned from human kidney. HDAC8 encodes 377 amino acid residues and shares extensive homology to several known HDACs, in particular a histone deacetylase from Arabidopsis thaliana. Northern blot analyses revealed that HDAC8 expression pattern for HDAC8 is distinct from that for HDAC1 and HDAC3, and expression of HDAC8 mRNA occurs in multiple organs including heart, lung, kidney, and pancreas. HDAC8 mRNA was also observed in several cell lines derived from cancerous tissues. When expressed in HEK293 cells, HDAC8 exhibited deacetylase activity toward acetylated histone, indicating that this protein is a bona fide histone deacetylase. Its histone deacetylase activity was inhibited by trichostatin and other known histone deacetylase inhibitors. Furthermore, active recombinant HDAC8 was expressed and purified from Escherichia coli. When ectopically expressed in cells, HDAC8 was found to be localized to the nucleus. Co-transfection experiments demonstrated that expression of HDAC8 repressed a viral SV40 early promoter activity. These results indicate that HDAC8 is a novel member of the histone deacetylase family, which may play a role in the development of a broad range of tissues and potentially in the etiology of cancer.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Of these, only HDAC8 is a fully functional enzyme in isolation5,6.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [5]
Experimental — accuracy not yet measuredIn the citing paper
“The finding of a direct involvement of K+ ions in the architecture of the active site and in the stabilization of structural elements of HDAC8 could rationalize previously observed potassium dependence of the activity of this enzyme ([12](#ref12)) and of other subtypes (P.G., unpublished results).”
From Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor (2004) · cites this paper as [12]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
[6] Use of T7 RNA polymerase to direct expression of cloned genes
Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S. A., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,398
Yoshida, M., Kijima, M., Akita, M., & Beppu, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44885-x · Cited by 1,856
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
Flagged first, then by citations
Research works printed but not linked: 3
- Innis, 1983, Mol. Cell. Biol., 3, 2203
- Redner, 1999, Blood, 94, 417, 10.1182/blood.V94.2.417 · DOI
- Saunders, 1999, Cancer Res., 59, 399
Cited by
Sorted by citations
Items 301–318 of 318
Ramos‐Morales, E. (2021) · theses.fr (ABES) · doi:10.70675/c6b28473zf6b6z4024z99bfz05629f0484d7
Nuclear cGAS inhibits stimulation-induced inflammatory gene transcription via HDAC1
高, 尚., Li, H. P., Yan, S., Hou, S., & Yin, H. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2601665123
Histone deacetylases, the erasers of the code
Lamberti, M. J., Vera, R. E., Mentucci, F. M., Vittar, N. B. R., & Schneider, G. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-19001-8.00012-x
BindingDB Entry 50022755: HDAC8 as a target in drug discovery: Function, structure and design.
BindingDB (2026) · UC San Diego · doi:10.7270/q25x2frg
BindingDB (2010) · UC San Diego · doi:10.7270/q2mp5398
BindingDB (2020) · UC San Diego · doi:10.7270/q2125w99
Modulation of Folate Receptor Beta for Drug Targeting in Acute Myelogenous Leukemia
Qi, H. (2005) · OhioLink ETD Center (Ohio Library and Information Network)
Clinical Trials of Epigenetic Modifiers in the Treatment of Myelodysplastic Syndrome
Suarez, L., & Gore, S. D. (2011) · Springer eBooks · doi:10.1007/978-1-84882-644-1_15
Metadata
- Authors
- Hu, E., Chen, Z., Fredrickson, T., Zhu, Y., Kirkpatrick, R., Zhang, G.-F., Johanson, K., Sung, C.-M., Liu, R., & Winkler, J.
- Corresponding author
- Hu, Erding
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 20
- Pages
- 15254-15264
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2061360494
- Cited by
- 309
- References
- 80
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 11 · 2023: 22 · 2022: 12 · 2021: 8 · 2020: 18 · 2019: 8 · 2018: 9 · 2017: 10 · 2016: 10 · 2015: 14 · 2014: 12 · 2013: 11 · 2012: 14
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- HDAC8, histone deacetylase, class I histone deacetylases, transcriptional repression, histone acetylation, chromatin regulation, gene expression regulation, histone deacetylase inhibitors, SV40 early promoter, nuclear localization, tissue-specific gene expression, cancer
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Histone Deacetylases, Humans, Kidney, Molecular Sequence Data, Organ Specificity, Phylogeny, Recombinant Proteins, Repressor Proteins, RNA, Messenger, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Sequence Alignment, 3T3 Cells, Arabidopsis, Sequence Homology, Amino Acid, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
