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A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Abstract
Trapoxin is a microbially derived cyclotetrapeptide that inhibits histone deacetylation in vivo and causes mammalian cells to arrest in the cell cycle. A trapoxin affinity matrix was used to isolate two nuclear proteins that copurified with histone deacetylase activity. Both proteins were identified by peptide microsequencing, and a complementary DNA encoding the histone deacetylase catalytic subunit (HD1) was cloned from a human Jurkat T cell library. As the predicted protein is very similar to the yeast transcriptional regulator Rpd3p, these results support a role for histone deacetylase as a key regulator of eukaryotic transcription.
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“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 [31]
Citations
Cites
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635
The ancient regulatory-protein family of WD-repeat proteins
Neer, E. J., Schmidt, C. J., Nambudripad, R., & Smith, T. F. (1994) · Nature · doi:10.1038/371297a0 · Cited by 1,491
A positive role for histone acetylation in transcription factor access to nucleosomal DNA
Lee, D. Y., Hayes, J. J., Pruss, D., & Wolffe, A. P. (1993) · Cell · doi:10.1016/0092-8674(93)90051-q · Cited by 1,122
Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Preprint
Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D., & Broach, J. R. (1993) · Genes & Development · doi:10.1101/gad.7.4.592 · Cited by 791
Hecht, A., Laroche, T., Strahl‐Bolsinger, S., Gasser, S. M., & Grunstein, M. R. (1995) · Cell · doi:10.1016/0092-8674(95)90512-x · Cited by 780
Yoshida, M., Horinouchi, S., & Beppu, T. (1995) · BioEssays · doi:10.1002/bies.950170510 · Cited by 715
Aparicio, O. M., Billington, B. L., & Gottschling, D. E. (1991) · Cell · doi:10.1016/0092-8674(91)90049-5 · Cited by 697
Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S., & Beppu, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41547-5 · Cited by 516
Identification of a Gene Encoding a Yeast Histone H4 Acetyltransferase
Kleff, S., Andrulis, E. D., Anderson, C. W., & Sternglanz, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24674 · Cited by 353
Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation
Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M. (1990) · Science · doi:10.1126/science.2106160 · Cited by 349
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Milstein, C. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199911)21:11 · Cited by 97
Allen, H. F., Wade, P. A., & Kutateladze, T. G. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1256-2 · Cited by 205
Small-molecule-mediated G-quadruplex isolation from human cells
Müller, S., Kumari, S., Rodriguez, R., & Balasubramanian, S. (2010) · Nature Chemistry · doi:10.1038/nchem.842 · Cited by 214
WUSCHEL acts as an auxin response rheostat to maintain apical stem cells in Arabidopsis
Ma, Y., Miotk, A., Šutiković, Z., Ermakova, O., Wenzl, C., Medzihradszky, A., Gaillochet, C., Forner, J., Utan, G., Brackmann, K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13074-9 · Cited by 209
Stockwell, B. R., Haggarty, S. J., & Schreiber, S. L. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80004-0 · Cited by 203
Self-citationIntegrative regulation of physiology by histone deacetylase 3
Emmett, M. J., & Lazar, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0076-0 · Cited by 202
Hat1: the emerging cellular roles of a type B histone acetyltransferase
Parthun, M. R. (2007) · Oncogene · doi:10.1038/sj.onc.1210602 · Cited by 202
Histone acetylation as an epigenetic determinant of long-term transcriptional competence
Turner, B. M. (1998) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050122 · Cited by 202
Duplication and Maintenance of Heterochromatin Domains
Taddei, A., Roche, D. M. J., Sibarita, J., Turner, B. M., & Almouzni, G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.6.1153 · Cited by 202
Biotin and biotinidase deficiency
Zempleni, J., Hassan, Y. I., & Wijeratne, S. S. K. (2008) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.3.6.715 · Cited by 201
Covalent modifications of histones: expression from chromatin templates
Davie, J. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80138-x · Cited by 201
Haggarty, S. J., Koeller, K. M., Wong, J. C., Butcher, R. A., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00095-4 · Cited by 201
Self-citationTsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 201
What does ‘chromatin remodeling’ mean?
Aalfs, J. D., & Kingston, R. E. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01689-3 · Cited by 198
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BUGGY, J. J., SIDERIS, M. L., MAK, P., LORIMER, D. D., MCINTOSH, B., & CLARK, J. M. (2000) · Biochemical Journal · doi:10.1042/bj3500199 · Cited by 197
Waltregny, D., Glénisson, W., Tran, S. L., North, B. J., Verdin, E. M., Colige, A., & Castronovo, V. (2005) · The FASEB Journal · doi:10.1096/fj.04-2303fje · Cited by 197
Kwon, H. J., Owa, T., Hassig, C. A., Shimada, J., & Schreiber, S. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3356 · Cited by 197
Self-citationRegulation of histone deacetylase 2 by protein kinase CK2
Tsai, S.-C., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204149200 · Cited by 196
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Murn, J., & Shi, Y. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.35 · Cited by 205
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Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195
Chromatin remodeling and transcriptional activation: the cast (in order of appearance)
Urnov, F. D., & Wolffe, A. P. (2001) · Oncogene · doi:10.1038/sj.onc.1204323 · Cited by 195
Taunton, J., Collins, J. L., & Schreiber, S. L. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9615841 · Cited by 194
Self-citationJenke, R., Reßing, N., Hansen, F. K., Aigner, A. M., & Büch, T. (2021) · Cancers · doi:10.3390/cancers13040634 · Cited by 198
UPTAKE, LOCALIZATION, AND NONCARBOXYLASE ROLES OF BIOTIN
Zempleni, J. (2005) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.25.121304.131724 · Cited by 193
Unhavaithaya, Y., Shin, T. H., Miliaras, N. B., Lee, J., Oyama, T., & Mello, C. C. (2002) · Cell · doi:10.1016/s0092-8674(02)01202-3 · Cited by 192
Beckers, T. L., Burkhardt, C., Wieland, H., Gimmnich, P., Ciossek, T., Maier, T. M., & Sanders, K. (2007) · International Journal of Cancer · doi:10.1002/ijc.22751 · Cited by 191
Walton, J. D. (2006) · Phytochemistry · doi:10.1016/j.phytochem.2006.05.033 · Cited by 200
Target Identification in Chemical Genetics
Burdine, L. J., & Kodadek, T. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.05.001 · Cited by 191
Histone Deacetylase Inhibitors: An Attractive Therapeutic Strategy Against Breast Cancer
Damaskos, C., Valsami, S. I., Kontos, M. C., Spartalis, E. D., Kalampokas, T., Kalampokas, E., Athanasiou, A., Moris, D., Daskalopoulou, A., Davakis, S., et al. (2017) · Anticancer Research · doi:10.21873/anticanres.11286 · Cited by 190
Attenuation of a phosphorylation-dependent activator by an HDAC–PP1 complex
Canettieri, G., Morantte, I. G., Guzmán, E., Asahara, H., Herzig, S., Anderson, S., Yates, J. R., & Montminy, M. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb895 · Cited by 194
Quantitative Chemical Proteomics for Identifying Candidate Drug Targets
Oda, Y., Owa, T., Sato, T., Boucher, B., Daniels, S. B., Yamanaka, H., Shinohara, Y., Yokoi, A., Kuromitsu, J., & Nagasu, T. (2003) · Analytical Chemistry · doi:10.1021/ac026196y · Cited by 188
Recent developments in epigenetic cancer therapeutics: clinical advancement and emerging trends
Nepali, K., & Liou, J. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00721-x · Cited by 187
Grewal, S. I. S., Bonaduce, M. J., & Klar, A. J. S. (1998) · Genetics · doi:10.1093/genetics/150.2.563 · Cited by 185
The Balance between Acetylation and Deacetylation Controls Smad7 Stability
Simonsson, M., Heldin, C., Ericsson, J., & Gronroos, E. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503134200 · Cited by 184
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Hung, D. T., Jamison, T. F., & Schreiber, S. L. (1996) · Chemistry & Biology · doi:10.1016/s1074-5521(96)90129-5 · Cited by 183
Self-citationLai, A., Kennedy, B. K., Barbie, D. A., Bertos, N., Yang, X. J., Théberge, M.-C., Tsai, S., Seto, E., Zhang, Y., Kuzmichev, A., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.8.2918-2932.2001 · Cited by 183
How Chemoproteomics Can Enable Drug Discovery and Development
Moellering, R. E., & Cravatt, B. F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.001 · Cited by 182
Histone deacetylases—an important class of cellular regulators with a variety of functions
Hildmann, C., Riester, D., & Schwienhorst, A. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-0911-2 · Cited by 182
Deciphering post‐translational modification codes
Lothrop, A. P., Torres, M. P., & Fuchs, S. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.047 · Cited by 192
The emerging role of class II histone deacetylases
Fischle, W., Kiermer, V., Dequiedt, F., & Verdin, E. M. (2001) · Biochemistry and Cell Biology · doi:10.1139/bcb-79-3-337 · Cited by 182
Tong, J. J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.5.1114 · Cited by 181
The Role of Dietary Histone Deacetylases (HDACs) Inhibitors in Health and Disease
Bassett, S. A., & Barnett, M. P. G. (2014) · Nutrients · doi:10.3390/nu6104273 · Cited by 184
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
Trievel, R. C., Rojas, J. R., Sterner, D. E., Venkataramani, R. N., Wang, L. Y., Zhou, J., Allis, C. D., Berger, S. L., & Marmorstein, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.8931 · Cited by 181
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Wang, A. H., & Yang, X. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5992-6005.2001 · Cited by 180
Catalytic activity of the yeast SWI/SNF complex on reconstituted nucleosome arrays
Logie, C., & Peterson, C. L. (1997) · The EMBO Journal · doi:10.1093/emboj/16.22.6772 · Cited by 179
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Schirle, M., Bantscheff, M., & Küster, B. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.002 · Cited by 184
Histone Deacetylase Inhibitors In The Treatment Of Cancer: Overview And Perspectives
Giannini, G., Cabri, W., Fattorusso, C., & Rodriquez, M. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.80 · Cited by 182
Systematic Approaches to Toxicology in the Zebrafish
Peterson, R. T., & MacRae, C. A. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134751 · Cited by 178
Histone Acetylation Modifiers in the Pathogenesis of Malignant Disease
Mahlknecht, U., & Hoelzer, D. F. (2000) · Molecular Medicine · doi:10.1007/bf03402044 · Cited by 179
Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response
Kao, G. D., McKenna, W. G., Guenther, M. G., Muschel, R. J., Lazar, M. A., & Yen, T. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209065 · Cited by 178
Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions
Brand, M. J. D., Measures, A. M., Wilson, B. G., Cortopassi, W. A., Alexander, R. P., Höss, M., Hewings, D. S., Rooney, T. P. C., Paton, R. S., & Conway, S. J. (2014) · ACS Chemical Biology · doi:10.1021/cb500996u · Cited by 177
Li, D., Yea, S., Li, S., Zhu, C. X., Narla, G., Banck, M. S., Laborda, J., Tan, S., Friedman, J. M., Friedman, S. L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500463200 · Cited by 177
Rediscovering the sweet spot in drug discovery
Brown, D., & Superti‐Furga, G. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02902-7 · Cited by 180
Visualizing biologically active small molecules in cells using click chemistry
Cañeque, T., Müller, S., & Rodriguez, R. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0030-x · Cited by 185
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Patra, S. K., Patra, A., & Dahiya, R. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5639 · Cited by 176
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Anders, L., Guenther, M. G., Qi, J., Fan, Z. P., Marineau, J., Rahl, P. B., Lovén, J., Sigova, A. A., Smith, W. B., Lee, T. I., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2776 · Cited by 182
Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana
Wu, K., Tian, L., Malik, K., Brown, D. C., & Miki, B. L. A. (2000) · The Plant Journal · doi:10.1046/j.1365-313x.2000.00711.x · Cited by 174
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Ramakrishnan, V. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.83 · Cited by 174
Histone modifications and chromatin dynamics: a focus on filamentous fungi
Brosch, G., Loidl, P., & Graessle, S. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00100.x · Cited by 180
Bourguignon, L., Xia, W., & Wong, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806708200 · Cited by 175
Histone Deacetylase: A Potential Therapeutic Target for Fibrotic Disorders
Pang, M., & Zhuang, S. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.168385 · Cited by 173
The ADA Complex Is a Distinct Histone Acetyltransferase Complex in Saccharomyces cerevisiae
Eberharter, A., Sterner, D. E., Schieltz, D. M., Hassan, A. H., Yates, J. R., Berger, S. L., & Workman, J. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6621 · Cited by 173
Lehár, J., Stockwell, B. R., Giaever, G., & Nislow, C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.120 · Cited by 172
Nakajima, H., Sato, B., Fujita, T., Takase, S., Terano, H., & OKUHARA, M. (1996) · The Journal of Antibiotics · doi:10.7164/antibiotics.49.1196 · Cited by 172
Parbin, S., Kar, S., Shilpi, A., Sengupta, D., Deb, M., Rath, S. K., & Patra, S. K. (2013) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155413506582 · Cited by 174
Mammalian DNA repair: HATs and HDACs make their mark through histone acetylation
Gong, F., & Miller, K. M. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.002 · Cited by 175
MSI1-like proteins: an escort service for chromatin assembly and remodeling complexes
Hennig, L., Bouveret, R., & Gruissem, W. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.04.004 · Cited by 171
Xiao, H., Hasegawa, T., & Isobe, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1371 · Cited by 171
Aron, J. L., Parthun, M. R., Marcucci, G., Kitada, S., Mone, A. P., Davis, M. E., Shen, T., Murphy, T. J., Wickham, J., Kanakry, C. G., et al. (2003) · Blood · doi:10.1182/blood-2002-12-3794 · Cited by 171
Transcription factors vs nucleosomes: regulation of the PH05 promoter in yeast
Svaren, J. P. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01001-3 · Cited by 171
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Wang, M., & Lin, H. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-082520-125411 · Cited by 174
Genes determining yeast replicative life span in a long-lived genetic background
Kaeberlein, M. R., Kirkland, K. T., Fields, S., & Kennedy, B. K. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.10.007 · Cited by 170
Functional genomics to new drug targets
Kramer, R. S., & Cohen, D. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1552 · Cited by 169
Lai, A., Lee, J. M., Yang, W., DeCaprio, J. A., Kaelin, W. G., Seto, E., & Branton, P. E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6632 · Cited by 169
Role of the LXCXE Binding Site in Rb Function
Dahiya, A., Gavin, M., Luo, R. X., & Dean, D. C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6799-6805.2000 · Cited by 169
Unique forms of human and mouse nuclear receptor corepressor SMRT.
Ordentlich, P., Downes, M., Xie, W., Genin, A., Spinner, N., & Evans, R. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.6.2639 · Cited by 183
The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes
Grant, P. A., Sterner, D. E., Duggan, L. J., Workman, J. L., & Berger, S. L. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01263-x · Cited by 169
Pfannenstiel, B. T., & Keller, N. P. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.02.001 · Cited by 176
Leipe, D. D., & Landsman, D. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.18.3693 · Cited by 168
Kaufman, P. D., Cohen, J. L., & Osley, M. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4793 · Cited by 168
Molecular Characterization of Propionyllysines in Non-histone Proteins
Cheng, Z., Tang, Y., Chen, Y., Kim, S., Liu, H., Li, S. S. ‐., Gu, W. J., & Zhao, Y. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800224-mcp200 · Cited by 170
A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegansPreprint
Shi, Y., & Mello, C. C. (1998) · Genes & Development · doi:10.1101/gad.12.7.943 · Cited by 170
Moradei, O. M., Mallais, T. C., Frechette, S., Paquin, I., Tessier, P. E., Leit, S. M., Fournel, M., Bonfils, C., Trachy-Bourget, M.-C., Liu, J., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701079h · Cited by 166
Bowers, A., West, N., Taunton, J., Schreiber, S. L., Bradner, J. E., & Williams, R. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8033763 · Cited by 165
Self-citationRecent Advances in the Development of Polyamine Analogues as Antitumor Agents
Casero, R. A., & Woster, P. M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900187v · Cited by 165
Epigenetic aberrations and cancer.
Ducasse, M., & Brown, M. A. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-60 · Cited by 170
Histone deacetylases and their functions in plants
Ma, X., Lv, S., Zhang, C., & Yang, C. (2013) · Plant Cell Reports · doi:10.1007/s00299-013-1393-6 · Cited by 170
El‐Osta, A., & Wolffe, A. P. (2001) · Gene Expression · doi:10.3727/000000001783992731 · Cited by 165
Mad Proteins Contain a Dominant Transcription Repression Domain
Ayer, D. E., Laherty, C. D., Lawrence, Q. A., Armstrong, A. P., & Eisenman, R. N. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5772 · Cited by 163
Identification of the cellular targets of bioactive small organic molecules using affinity reagents
Leslie, B. J., & Hergenrother, P. J. (2008) · Chemical Society Reviews · doi:10.1039/b702942j · Cited by 163
Histone Deacetylases in Bone Development and Skeletal Disorders
Bradley, E. W., Shull, L. C., van Wijnen, A. J., McGee‐Lawrence, M. E., & Westendorf, J. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00004.2015 · Cited by 163
Smith, E., & Frenkel, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406294200 · Cited by 165
Calcium Regulates Transcriptional Repression of Myocyte Enhancer Factor 2 by Histone Deacetylase 4
Youn, H., Grozinger, C. M., & Liu, J. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000304200 · Cited by 163
Wong, J., Patterton, D., Imhof, A., Guschin, D. Y., Shi, Y., & Wolffe, A. P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.520 · Cited by 162
HDAC1 and HDAC2 control the transcriptional program of myelination and the survival of Schwann cells
Jacob, C., Christen, C. N., Pereira, J. A., Somandin, C., Baggiolini, A., Lötscher, P., Özçelik, M., Tricaud, N., Meijer, D., Yamaguchi, T., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2762 · Cited by 161
Youn, H., & Liu, J. O. (2000) · Immunity · doi:10.1016/s1074-7613(00)00010-8 · Cited by 161
Shankar, S., & Srivastava, R. K. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-1-4020-6554-5_13 · Cited by 160
Thompson, P. R., & Fast, W. L. (2006) · ACS Chemical Biology · doi:10.1021/cb6002306 · Cited by 157
Expression of HDAC1 and CBP/p300 in human colorectal carcinomas
Ishihama, K., Yamakawa, M., Semba, S., Takeda, H., Kawata, S., Kimura, S., & Kimura, W. (2007) · Journal of Clinical Pathology · doi:10.1136/jcp.2005.029165 · Cited by 157
Histone deacetylases: target enzymes for cancer therapy
Mottet, D., & Castronovo, V. (2007) · Clinical & Experimental Metastasis · doi:10.1007/s10585-007-9131-5 · Cited by 158
Metadata
- Authors
- Taunton, J., Hassig, C. A., & Schreiber, S. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Schreiber, Stuart L.
- Venue
- Science
- Published
- 1996-04-19
- Volume
- 272
- Issue
- 5260
- Pages
- 408-411
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1974112332
- Cited by
- 1,829
- References
- 20
- Citations by year
- 2026: 31 · 2025: 31 · 2024: 33 · 2023: 52 · 2022: 36 · 2021: 48 · 2020: 54 · 2019: 47 · 2018: 64 · 2017: 45 · 2016: 46 · 2015: 56 · 2014: 44 · 2013: 49 · 2012: 61
- FWCI
- 36.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- 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
- histone deacetylase, cell cycle arrest, transcriptional regulation, yeast homolog, nuclear proteins, Jurkat cells, protein purification
- MeSH terms
- Amino Acid Sequence, Animals, Anti-Bacterial Agents, Cattle, Cell Cycle, Cloning, Molecular, Enzyme Inhibitors, Fungal Proteins, Gene Expression Regulation, Histone Deacetylases, Humans, Hydroxamic Acids, Molecular Sequence Data, Molecular Weight, Peptides, Saccharomyces cerevisiae, T-Lymphocytes, Transcription Factors, Transcription, Genetic, Tumor Cells, Cultured, Saccharomyces cerevisiae Proteins, Histone Deacetylase Inhibitors
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