The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
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 [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
Cited by
Sorted by citations
Items 401–500 of 1,001
Genome wide analysis of nucleosome density histone acetylation and HDAC function in fission yeast
Wirén, M., Silverstein, R. A., Sinha, I., Walfridsson, J., Lee, H.-M., Laurenson, P., Pillus, L., Robyr, D., Grunstein, M. R., & Ekwall, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600758 · Cited by 159
Choi, C. Y., Kim, Y. H., Kwon, H. J., & Kim, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33194 · Cited by 155
Drosophila NURF-55, a WD repeat protein involved in histone metabolism
Martínez‐Balbás, M. A., Tsukiyama, T., Gdula, D. A., & Wu, C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.132 · Cited by 154
Total Synthesis of the Antitumor Depsipeptide FR-901,228
Li, K. W., Wu, J. J., Xing, W., & Simon, J. A. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9613724 · Cited by 154
Hepworth, S. R., Friesen, H., & Segall, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5750 · Cited by 154
Structural basis of histone H4 recognition by p55Preprint
Song, J., Garlick, J. D., & Kingston, R. E. (2008) · Genes & Development · doi:10.1101/gad.1653308 · Cited by 153
Role of Histone Acetylation in the Assembly and Modulation of Chromatin Structures
Annunziato, A. T., & Hansen, J. C. (2001) · Gene Expression · doi:10.3727/000000001783992687 · Cited by 152
Singh, S. B., Zink, D. L., Liesch, J. M., Mosley, R. T., Dombrowski, A. W., Bills, G. F., Darkin‐Rattray, S. J., Schmatz, D. M., & GOETZ, M. A. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo016088w · Cited by 150
Chakrabarti, S. R., & Nucifora, G. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1605 · Cited by 149
Wong, J., Shi, Y., & Wolffe, A. P. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3158 · Cited by 148
Roles of Histone Deacetylases and Inhibitors in Anticancer Therapy
Verza, F. A., Das, U., Fachin, A. L., Dimmock, J. R., & Marins, M. (2020) · Cancers · doi:10.3390/cancers12061664 · Cited by 149
Histone deacetylase inhibitors open new doors in cancer therapy
McLaughlin, F., & Thangue, N. B. L. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.034 · Cited by 147
Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases
Porter, N. J., & Christianson, D. W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.01.004 · Cited by 146
Biochemical Methods for Analysis of Histone Deacetylases
Kölle, D., Brosch, G., Lechner, T., Lusser, A., & Loidl, P. (1998) · Methods · doi:10.1006/meth.1998.0636 · Cited by 146
The Histone Deacetylase 9 Gene Encodes Multiple Protein Isoforms
Petrie, K. R., Guidez, F., Howell, L., Healy, L. E., Waxman, S., Greaves, M. F., & Zelent, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212935200 · Cited by 147
Chromatin Remodeling and Transcriptional Regulation
Luo, R., & Dean, D. C. (1999) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/91.15.1288 · Cited by 147
Histone deacetylase interacts directly with DNA topoisomerase II
Tsai, S., Valkov, N. I., Yang, W., Gump, J. L., Sullivan, D. M., & Seto, E. (2000) · Nature Genetics · doi:10.1038/81671 · Cited by 145
Komatsu, Y., Tomizaki, K., Tsukamoto, M., Kato, T., Nishino, N., Sato, S., Yamori, T., Tsuruo, T., Furumai, R., Yoshida, M., et al. (2001) · PubMed · Cited by 145
Doyle, K. J., & Fitzpatrick, F. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.089250 · Cited by 145
Cloning and characterization of human histone deacetylase 8
Van den Wyngaert, I., de Vries, W., Kremer, A., Neefs, J.-M., Verhasselt, P., Luyten, W. H. M. L., & Kass, S. U. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01813-5 · Cited by 143
Chemical genomics reveals histone deacetylases are required for core regulatory transcription
Gryder, B. E., Wu, L., Woldemichael, G. M., Pomella, S., Quinn, T. R., Park, P. M. C., Cleveland, A. H., Stanton, B. Z., Song, Y., Rota, R., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11046-7 · Cited by 146
Metabolism and selected functions of sphingolipids in the yeast Saccharomyces cerevisiae
Dickson, R. C., & Lester, R. L. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00068-2 · Cited by 143
LSD1 and the chemistry of histone demethylation
Culhane, J. C., & Cole, P. A. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.07.014 · Cited by 143
Mulligan, P., Westbrook, T. F., Ottinger, M., Pavlova, N. N., Chang, B., Macia, E., Shi, Y.-J., Barretina, J. G., Liu, J., Howley, P. M., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.025 · Cited by 143
Wachsman, J. T. (1997) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(97)00003-1 · Cited by 143
Syntheses of Discodermolides Useful for Investigating Microtubule Binding and Stabilization
Hung, D. T., Nerenberg, J. B., & Schreiber, S. L. (1996) · Journal of the American Chemical Society · doi:10.1021/ja961374o · Cited by 143
Self-citationNF-Y Is Associated with the Histone Acetyltransferases GCN5 and P/CAF
Currie, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1430 · Cited by 143
Zhao, T., Cheng, G., Zhang, L., TSENG, Y., & PADBURY, J. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.08.010 · Cited by 142
Ma, P., Pan, H., Montgomery, R. L., Olson, E. N., & Schultz, R. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118403109 · Cited by 147
Effect of posttranslational modifications on enzyme function and assembly
Ryšlavá, H., Hýsková, V., Kavan, D., & Vaněk, O. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.03.025 · Cited by 153
The Diversity of Histone Versus Nonhistone Sirtuin Substrates
Martínez‐Redondo, P., & Vaquero, A. (2013) · Genes & Cancer · doi:10.1177/1947601913483767 · Cited by 145
A Large Protein Complex Containing the Yeast Sin3p and Rpd3p Transcriptional Regulators
Kasten, M. M., Dorland, S., & Stillman, D. J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4852 · Cited by 142
FR901464: Total Synthesis, Proof of Structure, and Evaluation of Synthetic Analogues
Thompson, C. F., Jamison, T. F., & Jacobsen, E. N. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016615t · Cited by 142
Epigenetic control of gene regulation in plants
Lauria, M., & Rossi, V. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.03.002 · Cited by 146
Functional Interaction between Class II Histone Deacetylases and ICP0 of Herpes Simplex Virus Type 1
Lomonte, P., Thomas, J., Texier, P., Caron, C., Khochbin, S., & Epstein, A. L. (2004) · Journal of Virology · doi:10.1128/jvi.78.13.6744-6757.2004 · Cited by 146
Chemical genetic approaches for the elucidation of signaling pathways
Alaimo, P. J., Shogren‐Knaak, M. A., & Shokat, K. M. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00215-5 · Cited by 140
Sternson, S. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2001) · Organic Letters · doi:10.1021/ol016915f · Cited by 139
Self-citationA human homologue of yeast anti‐silencing factor has histone chaperone activity
Munakata, T., Adachi, N., Yokoyama, N., Kuzuhara, T., & Horikoshi, M. (2000) · Genes to Cells · doi:10.1046/j.1365-2443.2000.00319.x · Cited by 139
Suzuki, J., Chen, Y., Scott, G. K., DeVries, S., Chin, K., Benz, C. C., Waldman, F. M., & Hwang, E. S. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2319 · Cited by 139
A Conserved Family of WD-40 Proteins Binds to the Retinoblastoma Protein in Both Plants and Animals
Ach, R. A., Taranto, P., & Gruissem, W. (1997) · The Plant Cell · doi:10.1105/tpc.9.9.1595 · Cited by 139
Tan, D. S., Foley, M. A., Stockwell, B. R., Shair, M. D., & Schreiber, S. L. (1999) · Journal of the American Chemical Society · doi:10.1021/ja992144n · Cited by 139
Self-citationChemical Genetic Approaches to Plant Biology
Blackwell, H. E., & Zhao, Y. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.031138 · Cited by 138
Retinoblastoma: the disease, gene and protein provide critical leads to understand cancer
DiCiommo, D. P., Gallie, B. L., & Bremner, R. (2000) · Seminars in Cancer Biology · doi:10.1006/scbi.2000.0326 · Cited by 138
Resident vascular progenitor cells
Torsney, E., & Xu, Q. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.09.006 · Cited by 139
Subunits of the Yeast SWI/SNF Complex Are Members of the Actin-related Protein (ARP) Family
Peterson, C. L., Zhao, Y., & Chait, B. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.23641 · Cited by 136
Chromatin: Histone acetyltransferases in control
Wade, P. A., & Wolffe, A. P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00042-x · Cited by 136
Histone Deacetylation: An Important Mechanism in Inflammatory Lung Diseases
Adcock, I. M., Ito, K., & Barnes, P. J. (2005) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1080/15412550500346683 · Cited by 136
Display cloning: functional identification of natural product receptors using cDNA-phage display
Sche, P. P., McKenzie, K. M., White, J. D., & Austin, D. J. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(00)80018-6 · Cited by 135
Malavé, T. M., & Dent, S. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-073 · Cited by 135
Li, S., Moy, L. C., Pittman, N. S., Shue, G., Aufiero, B. M., Neufeld, E. J., LeLeiko, N. S., & Walsh, M. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7803 · Cited by 134
Chen, Y., Lopez-Sanchez, M., Savoy, D. N., Billadeau, D. D., Dow, G. S., & Kozikowski, A. P. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701606b · Cited by 134
Yao, Y., & Yang, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302955200 · Cited by 133
Chemoproteomics and Chemical Probes for Target Discovery
Drewes, G., & Knapp, S. (2018) · Trends in Biotechnology · doi:10.1016/j.tibtech.2018.06.008 · Cited by 132
Induction of γ-Globin by Histone Deacetylase Inhibitors
McCaffrey, P. G., Newsome, D. A., Fibach, E., Yoshida, M., & Su, M. S.-S. (1997) · Blood · doi:10.1182/blood.v90.5.2075 · Cited by 118
Iavarone, A., & Massagué, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.916 · Cited by 132
Epigenetic Mechanisms in Memory and Synaptic Function
Sultan, F. A., & Day, J. J. (2011) · Epigenomics · doi:10.2217/epi.11.6 · Cited by 133
Simple histone acetylation plays a complex role in the regulation of gene expression
Fukuda, H. (2006) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/ell032 · Cited by 133
Waltregny, D., de Leval, L., Glénisson, W., Tran, S. L., North, B. J., Bellahcène, A., Weidle, U. H., Verdin, E. M., & Castronovo, V. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63320-2 · Cited by 131
RPD3 is required for the inactivation of yeast ribosomal DNA genes in stationary phase
Sandmeier, J. J., French, S. L., Osheim, Y. N., Cheung, W. L., Gallo, C. M., Beyer, A. L., & Smith, J. S. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf498 · Cited by 131
Novel Receptor Interaction and Repression Domains in the Orphan Receptor SHP
Seol, W., Chung, M., & Moore, D. D. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.7126 · Cited by 131
Jung, K. H., Noh, J. H., Kim, J. K., Eun, J. W., Bae, H. J., Xie, H. J., Chang, Y. G., Kim, M., Park, H., Lee, J. Y., et al. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24090 · Cited by 135
Origins and evolutionary diversification of the nuclear receptor superfamily
Owen, G. I., & Zelent, A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050043 · Cited by 133
Differential localization of HDAC4 orchestrates muscle differentiation
Miska, E. A. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.16.3439 · Cited by 130
Gaudreau, L. R., Schmid, A., Blaschke, D., Ptashne, M., & Hörz, W. (1997) · Cell · doi:10.1016/s0092-8674(00)80182-8 · Cited by 130
Role of histone tails in nucleosome remodeling by Drosophila NURF
Georgel, P. T., Tsukiyama, T., & Wu, C. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4717 · Cited by 130
Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases
Iezzi, S., Cossu, G., Nervi, C., Sartorelli, V., & Puri, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112218599 · Cited by 129
Song, C., & Galbraith, D. W. (2006) · Plant Molecular Biology · doi:10.1007/s11103-005-3880-9 · Cited by 129
Target Identification by Diazirine Photo‐Cross‐Linking and Click Chemistry
MacKinnon, A. L., & Taunton, J. (2009) · Current Protocols in Chemical Biology · doi:10.1002/9780470559277.ch090167 · Cited by 128
Self-citationSato, S., Kwon, Y., Kamisuki, S., Srivastava, N., Mao, Q., Kawazoe, Y., & Uesugi, M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0655643 · Cited by 127
Myers, F. A., Evans, D. R., Clayton, A. L., Thorne, A. W., & Crane‐Robinson, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009472200 · Cited by 127
Tyler, J. K., Bulger, M., Kamakaka, R. T., Kobayashi, R., & Kadonaga, J. T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6149 · Cited by 127
Thyroid Hormone Receptor Coactivators and Corepressors
Koenig, R. J. (1998) · Thyroid · doi:10.1089/thy.1998.8.703 · Cited by 128
Genome-wide analysis of HDAC function
Ekwall, K. (2005) · Trends in Genetics · doi:10.1016/j.tig.2005.08.009 · Cited by 133
Yao, J., Lai, E., & Stifani, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.1962-1972.2001 · Cited by 126
Type B Histone Acetyltransferase Hat1p Participates in Telomeric Silencing
Kelly, T. J., Qin, S., Gottschling, D. E., & Parthun, M. R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7051-7058.2000 · Cited by 126
Chromatin-remodeling factors: machines that regulate?
Varga‐Weisz, P., & Becker, P. B. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80010-0 · Cited by 126
Marine Natural Product Aurilide Activates the OPA1-Mediated Apoptosis by Binding to Prohibitin
Sato, S., Murata, A., Orihara, T., Shirakawa, T., Suenaga, K., Kigoshi, H., & Uesugi, M. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.10.017 · Cited by 127
Godschalk, R., van Schooten, F., & Bartsch, H. (2003) · BMB Reports · doi:10.5483/bmbrep.2003.36.1.001 · Cited by 131
CAF-1 and the inheritance of chromatin states: at the crossroads of DNA replication and repair
Ridgway, P., & Almouzni, G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.15.2647 · Cited by 125
Masumi, A., Wang, I.-M., Lefebvre, B., Yang, X.-J., Nakatani, Y., & Ozato, K. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1810 · Cited by 124
Transcription factor‐dependent regulation of CBP and P/CAF histone acetyltransferase activity
Soutoglou, E., Viollet, B., Vaxillaire, M., Yaniv, M., Pontoglio, M., & Talianidis, I. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1984 · Cited by 123
Histone acetylation: A possible mechanism for the inheritance of cell memory at mitosis
Jeppesen, P. (1997) · BioEssays · doi:10.1002/bies.950190111 · Cited by 123
Madsen, A. S., & Olsen, C. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203754 · Cited by 122
The Current State of NAD+‐Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets
Schiedel, M., Robaa, D., Rumpf, T., Sippl, W., & Jung, M. (2017) · Medicinal Research Reviews · doi:10.1002/med.21436 · Cited by 125
Transcriptional Activities of Retinoic Acid Receptors
Lefèbvre, P., Martin, P. J., Flajollet, S., Dedieu, S., Billaut, X., & Lefebvre, B. (2005) · Vitamins and hormones · doi:10.1016/s0083-6729(05)70007-8 · Cited by 129
Histone deacetylase inhibitors and genomic instability
Éot-Houllier, G., Fulcrand, G., Magnaghi-Jaulin, L., & Jaulin, C. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.06.005 · Cited by 127
Chromatin as an expansive canvas for chemical biology
Fierz, B., & Muir, T. W. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.938 · Cited by 125
Protein Acetylation in the Cardiorenal Axis
Bush, E. W., & McKinsey, T. A. (2010) · Circulation Research · doi:10.1161/circresaha.109.209338 · Cited by 121
Histone Deacetylase in Carcinogenesis and Its Inhibitors as Anti-cancer Agents
Kim, D. H., Kim, M., & Kwon, H.-J. (2003) · BMB Reports · doi:10.5483/bmbrep.2003.36.1.110 · Cited by 123
Zhou, X., Richon, V. M., Rifkind, R. A., & Marks, P. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1056 · Cited by 120
Sasaki, S., Lesoon‐Wood, L. A., Dey, A., Kuwata, T., Weintraub, B. D., Humphrey, G. W., Yang, W., Seto, E., Yen, P. M., Howard, B. H., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5389 · Cited by 120
Johnson, C. A., White, D. A., Lavender, J. S., O'Neill, L. P., & Turner, B. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107942200 · Cited by 119
Hos1 Deacetylates Smc3 to Close the Cohesin Acetylation Cycle
Borges, V., Lehane, C., Lopez‐Serra, L., Flynn, H. R., Skehel, M. J., Ben-Shahar, T. R., & Uhlmann, F. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.009 · Cited by 129
Functions and mechanisms of plant histone deacetylases
Chen, X., Ding, A. B., & Zhong, X. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-1587-x · Cited by 119
Chan, J. C., & Maze, I. S. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.009 · Cited by 126
RbAp48 Belongs to the Histone Deacetylase Complex That Associates with the Retinoblastoma Protein
Nicolas, E., Morales, V., Magnaghi-Jaulin, L., Harel‐Bellan, A., Richard‐Foy, H., & Trouche, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9797 · Cited by 119
Gregory, P. D., Schmid, A., Zavari, M., Lui, L., Berger, S. L., & Hörz, W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80050-7 · Cited by 119
Characterization of Receptor Interaction and Transcriptional Repression by the Corepressor SMRT
Li, H., Leo, C., Schroen, D. J., & Chen, J. D. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.13.0028 · Cited by 119
Biochemical Target Isolation for Novices: Affinity-Based Strategies
Sato, S., Murata, A., Shirakawa, T., & Uesugi, M. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.05.015 · Cited by 120
Chemical Genetics–Based Target Identification in Drug Discovery
Cong, F., Cheung, A. K., & Huang, S.-M. A. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134639 · Cited by 118
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
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