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 101–200 of 1,001
Upregulation and Nuclear Recruitment of HDAC1 in Hormone Refractory Prostate Cancer
Halkidou, K., Gaughan, L., Cook, S., Leung, H. Y., Neal, D. E., & Robson, C. N. (2004) · The Prostate · doi:10.1002/pros.20022 · Cited by 515
The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
Yang, X. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh252 · Cited by 538
Coregulator codes of transcriptional regulation by nuclear receptors
Rosenfeld, M. G., & Glass, C. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100041200 · Cited by 509
Epigenetic regulation in metabolic diseases: mechanisms and advances in clinical study
Wu, Y., Lin, Z., Li, C., Lin, X. J., Shan, S., Guo, B., Zheng, M.-H., Li, F., Yuan, L., & Li, Z. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01333-7 · Cited by 549
CoREST is an integral component of the CoREST- human histone deacetylase complex
You, A., Tong, J. K., Grozinger, C. M., & Schreiber, S. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1454 · Cited by 500
Self-citationSignals and Combinatorial Functions of Histone Modifications
Suganuma, T., & Workman, J. L. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-175347 · Cited by 508
Gelmetti, V., Zhang, J., Fanelli, M., Minucci, S., Pelicci, P. G., & Lazar, M. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7185 · Cited by 492
SATB1 targets chromatin remodelling to regulate genes over long distances
Yasui, D. H., Miyano, M., Cai, S., Varga‐Weisz, P., & Kohwi-shigematsu, T. (2002) · Nature · doi:10.1038/nature01084 · Cited by 487
FR901228, a Potent Antitumor Antibiotic, Is a Novel Histone Deacetylase Inhibitor
Nakajima, H., Kim, Y. B., Terano, H., Yoshida, M., & Horinouchi, S. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4027 · Cited by 489
The p300/CBP family: integrating signals with transcription factors and chromatin
Shiama, N. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01048-9 · Cited by 488
The human Mi-2/NuRD complex and gene regulation
Denslow, S. A., & Wade, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210611 · Cited by 479
BCoR, a novel corepressor involved in BCL-6 repressionPreprint
Huynh, K. D., Fischle, W., Verdin, E. M., & Bardwell, V. J. (2000) · Genes & Development · doi:10.1101/gad.14.14.1810 · Cited by 475
Histone acetylation: chromatin in action
Wade, P. A., Pruss, D., & Wolffe, A. P. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01016-5 · Cited by 468
Unlocking the mechanisms of transcription factor YY1: are chromatin modifying enzymes the key?
Thomas, M. J. N., & Seto, E. (1999) · Gene · doi:10.1016/s0378-1119(99)00261-9 · Cited by 469
Köhler, C., Hennig, L., Bouveret, R., Gheyselinck, J., Grossniklaus, U., & Gruissem, W. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg444 · Cited by 452
Chen, G., Fernandez, J., Mische, S. M., & Courey, A. J. (1999) · Genes & Development · doi:10.1101/gad.13.17.2218 · Cited by 444
Parthun, M. R., Widom, J., & Gottschling, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81325-2 · Cited by 440
HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
Saha, R. N., & Pahan, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401769 · Cited by 439
Vigushin, D. M., Ali, S., Pace, P., Mirsaidi, N., Ito, K., Adcock, I. M., & Coombes, R. C. (2001) · PubMed · Cited by 439
Wade, P. A., Jones, P. L., Vermaak, D., & Wolffe, A. P. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70328-8 · Cited by 433
Yang, W., Yao, Y., Sun, J.-M., Davie, J., & Seto, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.28001 · Cited by 433
ETO, a Target of t(8;21) in Acute Leukemia, Interacts with the N-CoR and mSin3 Corepressors
Lutterbach, B. A., Westendorf, J. J., Linggi, B. E., Patten, A. K., Moniwa, M., Davie, J., Huynh, K. D., Bardwell, V. J., Lavinsky, R. M., Rosenfeld, M. G., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7176 · Cited by 432
Regulation of Transcription Factor YY1 by Acetylation and Deacetylation
Yao, Y., Yang, W., & Seto, E. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5979-5991.2001 · Cited by 439
Milazzo, G., Mercatelli, D., Muzio, G. D., Triboli, L., Rosa, P. D., Perini, G., & Giorgi, F. M. (2020) · Genes · doi:10.3390/genes11050556 · Cited by 448
Everything you have ever wanted to know about Yin Yang 1......
Shi, Y., Lee, J.-S., & Galvin, K. M. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(96)00044-3 · Cited by 432
Ng (2000) · doi:10.1016/s0968-0004(00)01551-6 · Cited by 427
Target deconvolution strategies in drug discovery
Terstappen, G. C., Schlüpen, C., Raggiaschi, R., & Gaviraghi, G. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2410 · Cited by 431
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 429
A Brief History of EpigeneticsPreprint
Felsenfeld, G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018200 · Cited by 420
Genomewide studies of histone deacetylase function in yeast
Bernstein, B., Tong, J. K., & Schreiber, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250477697 · Cited by 419
Self-citationClass II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 428
Chemical genetics: ligand-based discovery of gene function
Stockwell, B. R. (2000) · Nature Reviews Genetics · doi:10.1038/35038557 · Cited by 418
Histone Deacetylases Specifically Down-regulate p53-dependent Gene Activation
Juan, L.-J., Shia, W.-J., Chen, M.-H., Yang, W., Seto, E., Lin, Y.-S., & Wu, C.-W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000202200 · Cited by 415
Epigenetics at the Epicenter of Modern Medicine
Feinberg, A. P. (2008) · JAMA · doi:10.1001/jama.299.11.1345 · Cited by 424
Epigenetics of the depressed brain: role of histone acetylation and methylation
Sun, H., Kennedy, P. J., & Nestler, E. J. (2013) · Neuropsychopharmacology · doi:10.1038/npp.2012.73 · Cited by 413
Furumai, R., Komatsu, Y., Nishino, N., Khochbin, S., Yoshida, M., & Horinouchi, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.87 · Cited by 412
Ryan, Q. C., Headlee, D. J., Acharya, M. R., Sparreboom, A., Trepel, J. B., Ye, Z., Figg, W. D., Hwang, K., Chung, E. J., Murgo, A. J., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.02.188 · Cited by 412
Chemical genetics resulting from a passion for synthetic organic chemistry
Schreiber, S. L. (1998) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(98)00126-6 · Cited by 409
Self-citationMcKenna, N. J., Xu, J., Nawaz, Z., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (1999) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(98)00144-7 · Cited by 408
Massively multiplex chemical transcriptomics at single-cell resolution
Srivatsan, S. R., McFaline-Figueroa, J. L., Ramani, V., Saunders, L., Cao, J., Packer, J., Pliner, H. A., Jackson, D. L., Daza, R. M., Christiansen, L., et al. (2020) · Science · doi:10.1126/science.aax6234 · Cited by 401
Lau, O. D., Kundu, T. K., Soccio, R. E., Ait‐Si‐Ali, S., Khalil, E. M., Vassilev, A. P., Wolffe, A. P., Nakatani, Y., Roeder, R. G., & Cole, P. A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80452-9 · Cited by 401
Histone Deacetylase 1 Can Repress Transcription by Binding to Sp1
Doetzlhofer, A., Rotheneder, H., Egger, G., Koranda, M., Kurtev, V., Brosch, G., Wintersberger, E., & Seiser, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5504 · Cited by 396
Signaling Network Model of Chromatin
Schreiber, S. L., & Bernstein, B. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 399
Self-citationThe Vitamin D Receptor and the Syndrome of Hereditary 1,25-Dihydroxyvitamin D-Resistant Rickets
Malloy, P. J., Pike, J. W., & Feldman, D. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.2.0359 · Cited by 394
Sambucetti, L. C., Fischer, D. D., Zabludoff, S., Kwon, P. O., Chamberlin, H., Trogani, N., Xu, H. W., & Cohen, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34940 · Cited by 390
Click Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 392
Ryan, R. F., Schultz, D., Ayyanathan, K., Singh, P. B., Friedman, J. R., Fredericks, W. J., & Rauscher, F. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4366 · Cited by 382
Kaufman, P. D., Kobayashi, R., & Stillman, B. (1997) · Genes & Development · doi:10.1101/gad.11.3.345 · Cited by 380
The histone deacetylase-3 complex contains nuclear receptor corepressors
Wen, Y.-D., Perissi, V., Staszewski, L. M., Yang, W.-M., Krones, A., Glass, C. K., Rosenfeld, M. G., & Seto, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7202 · Cited by 378
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 383
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369
Functional significance of histone deacetylase diversity
Khochbin, S., Verdel, A., Lemercier, C., & Seigneurin-Berny, D. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00174-x · Cited by 366
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 375
A role for histone deacetylase activity in HDAC1-mediated transcriptional repression
Hassig, C. A., Tong, J. K., Fleischer, T. C., Owa, T., Grable, P. G., Ayer, D. E., & Schreiber, S. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3519 · Cited by 365
Self-citationWang, C., Fu, M., Angeletti, R. H., Siconolfi-Baez, L., Reutens, A. T., Albanese, C., Lisanti, M. P., Katzenellenbogen, B. S., Kato, S., Hopp, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100800200 · Cited by 375
Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs
Hassig, C. A., & Schreiber, S. L. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80066-x · Cited by 364
Self-citationThe Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy
Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 364
Dueñas‐González, A., Candelaria, M., Pérez‐Plasencia, C., Pérez‐Cárdenas, E., la Cruz-Hernández, E. N. D., & Herrera, L. A. (2008) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2007.11.003 · Cited by 362
A Green Chemistry Approach to Asymmetric Catalysis: Solvent-Free and Highly Concentrated Reactions
Walsh, P. J., Li, H., & de Parrodi, C. A. (2007) · Chemical Reviews · doi:10.1021/cr0509556 · Cited by 360
The emerging role of mass spectrometry-based proteomics in drug discovery
Meissner, F., Geddes‐McAlister, J., Mann, M., & Bantscheff, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00409-3 · Cited by 373
Review: Chromatin Structural Features and Targets That Regulate Transcription
Wolffe, A. P., & Guschin, D. Y. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4217 · Cited by 360
Identification of Novel Isoform-Selective Inhibitors within Class I Histone Deacetylases
Hu, E., Dul, E., Sung, C.-M., Chen, Z., Kirkpatrick, R. B., Zhang, G., Johanson, K., Liu, R., Lago, A. M., Hofmann, G. A., et al. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.055541 · Cited by 350
Retinoblastoma protein partners
(2001) · Advances in Cancer Research · doi:10.1016/s0065-230x(01)82001-7 · Cited by 349
HDAC inhibitors: Clinical update and mechanism-based potential
Glaser, K. B. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.04.007 · Cited by 349
Nathan, D., Ingvarsdottir, K., Sterner, D. E., Bylebyl, G. R., Dokmanovic, M., Dorsey, J. A., Whelan, K. A., Krsmanovic, M. L., Lane, W. S., Meluh, P. B., et al. (2006) · Genes & Development · doi:10.1101/gad.1404206 · Cited by 345
Identification of a small molecule inhibitor of Sir2p
Bedalov, A., Gatbonton, T., Irvine, W. P., Gottschling, D. E., & Simon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261574398 · Cited by 344
Coull, J. J., Romerio, F., Sun, J.-M., Volker, J. L., Galvin, K. M., Davie, J., Shi, Y., Hansen, U. M., & Margolis, D. M. (2000) · Journal of Virology · doi:10.1128/jvi.74.15.6790-6799.2000 · Cited by 343
Transcriptional regulation and the role of diverse coactivators in animal cells
Roeder, R. G. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.007 · Cited by 355
Fournel, M., Bonfils, C., Hou, Y., Yan, P. T., Trachy-Bourget, M.-C., Kalita, A., Liu, J., Lu, A., Zhou, N. Z., Robert, M., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2026 · Cited by 343
Huang, B., Laban, M., Leung, C. H.-W., Lee, L., Lee, C. K., Salto‐Tellez, M., Raju, G. C., & Hooi, S. C. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401567 · Cited by 337
Host-Selective Toxins: Agents of Compatibility
Walton, J. D. (1996) · The Plant Cell · doi:10.1105/tpc.8.10.1723 · Cited by 336
Humphrey, G. W., Wang, Y., Russanova, V. R., Hirai, T., Qin, J., Nakatani, Y., & Howard, B. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007372200 · Cited by 331
Fields, P. E., Kim, S. T., & Flavell, R. A. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.2.647 · Cited by 334
Programming off and on states in chromatin: mechanisms of Polycomb and trithorax group complexes
Simon, J. A., & Tamkun, J. W. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00288-5 · Cited by 328
BRCA1 interacts with components of the histone deacetylase complex
Yarden, R. I., & Brody, L. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4983 · Cited by 328
Transcriptional Repression by Blimp-1 (PRDI-BF1) Involves Recruitment of Histone Deacetylase
Yu, J. C., Angelin‐Duclos, C., Greenwood, J., Liao, J., & Calame, K. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2592-2603.2000 · Cited by 327
Histone modifying enzymes: Structures, mechanisms, and specificities
Marmorstein, R., & Trievel, R. C. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.07.009 · Cited by 341
The E7 oncoprotein associates with Mi2 and histone deacetylase activity to promote cell growth
Brehm, A., Nielsen, S. J., Miska, E. A., McCance, D. J., Reid, J. L., Bannister, A. J., & Kouzarides, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2449 · Cited by 325
Histone deacetylation in epigenetics: An attractive target for anticancer therapy
Mai, A., Massa, S., Rotili, D., Cerbara, I., Valente, S., Pezzi, R., Simeoni, S., & Ragno, R. (2005) · Medicinal Research Reviews · doi:10.1002/med.20024 · Cited by 328
Discovery of Novel Antitumor Sulfonamides Targeting G1 Phase of the Cell Cycle
Owa, T., Yoshino, H., Okauchi, T., Yoshimatsu, K., Ozawa, Y., Sugi, N. H., Nagasu, T., Koyanagi, N., & Kitoh, K. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm9902638 · Cited by 322
HDA6 is required for jasmonate response, senescence and flowering in Arabidopsis
Wu, K., Zhang, L., Zhou, C., Yu, C. W., & Chaikam, V. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/erm300 · Cited by 319
Lu, X., & Horvitz, H. R. (1998) · Cell · doi:10.1016/s0092-8674(00)81722-5 · Cited by 316
Mechanisms and Dynamics of Protein Acetylation in Mitochondria
Baeza, J., Smallegan, M. J., & Denu, J. M. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.006 · Cited by 318
Boutell, J. M., Thomas, P., Neal, J. W., Weston, V. J., Duce, J., Harper, P. S., & Lesley Jones, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.9.1647 · Cited by 310
Hu, E., Chen, Z., Fredrickson, T., Zhu, Y., Kirkpatrick, R., Zhang, G.-F., Johanson, K., Sung, C.-M., Liu, R., & Winkler, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908988199 · Cited by 309
Quantitation of HDAC1 mRNA Expression in Invasive Carcinoma of the Breast*
Zhang, Z., Yamashita, H., Toyama, T., Sugiura, H., Ando, Y., Mita, K., Hamaguchi, M., Hara, Y., Kobayashi, S., & Iwase, H. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-6001-1 · Cited by 307
Histone deacetylase inhibitors in cancer treatment
Vigushin, D. M., & Coombes, R. C. (2002) · Anti-Cancer Drugs · doi:10.1097/00001813-200201000-00001 · Cited by 301
Identification of Direct Protein Targets of Small Molecules
Lomenick, B., Olsen, R. W., & Huang, J. (2010) · ACS Chemical Biology · doi:10.1021/cb100294v · Cited by 305
Sin3: a flexible regulator of global gene expression and genome stability
Silverstein, R. A., & Ekwall, K. (2004) · Current Genetics · doi:10.1007/s00294-004-0541-5 · Cited by 300
Re-SET-ting heterochromatin by histone methyltransferases
Jenuwein, T. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02001-3 · Cited by 304
Kelly, R. D. W., & Cowley, S. M. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130010 · Cited by 297
Walsh, D. P., & Chang, Y. (2006) · Chemical Reviews · doi:10.1021/cr0404141 · Cited by 299
HDAC4, a Human Histone Deacetylase Related to Yeast HDA1, Is a Transcriptional Corepressor
Wang, A. H., Bertos, N. R., Vezmar, M., Pelletier, N., Crosato, M., Heng, H. H., Th’ng, J., Han, J., & Yang, X.-J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7816 · Cited by 294
Histone Deacetylase: A Regulator of Transcription
Wolffe, A. P. (1996) · Science · doi:10.1126/science.272.5260.371 · Cited by 293
Guidez, F., Ivins, S. M., Zhu, J., Söderström, M., Waxman, S., & Zelent, A. (1998) · Blood · doi:10.1182/blood.v91.8.2634.2634_2634_2642 · Cited by 292
Characterization of a human RPD3 ortholog, HDAC3
Emiliani, S., Fischle, W., Lint, C. M. V., Al-Abed, Y., & Verdin, E. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2795 · Cited by 292
Wang, H., Gao, X., Fukumoto, S., Tademoto, S., Sato, K., & Hirai, K. (1999) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199911)181:2 · Cited by 45
Jin, S. V., & Scotto, K. W. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4377 · Cited by 289
Zhang, Y., Sun, Z., Iratni, R., Erdjument‐Bromage, H., Tempst, P., Hampsey, M., & Reinberg, D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80102-1 · Cited by 288
Deregulation of HDAC1 by p25/Cdk5 in Neurotoxicity
Kim, D., Frank, C. L., Dobbin, M. M., Tsunemoto, R. K., Tu, W., Peng, P. L., Guan, J.-S., Lee, B.-H., Moy, L. Y., Giusti, P., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.015 · Cited by 286
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