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Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Open accessAbstract
An important event in gene expression is the covalent modification of histone proteins. We have found that the mammalian transcriptional repressor Sin3 (mSin3) exists in a complex with histone deacetylases HDAC1 and HDAC2. Consistent with the observation that mSin3-mediated repression of transcription involves the modification of histone polypeptides, we found that the mSin3-containing complex includes polypeptides that tether the mSin3 complex to core histone proteins. In addition, two novel mSin3-associated polypeptides, SAP18 and SAP30, were identified. We isolated a cDNA encoding human SAP18 and found that SAP18 is a component of an mSin3-containing complex in vivo. Moreover, we demonstrate a direct interaction between SAP18 and mSin3. SAP18 represses transcription in vivo when tethered to the promoter, consistent with the ability of SAP18 to interact with mSin3.
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“RBBP4 and RBBP7 are present in many protein complexes other than the NuRD complex (Sin3 complex, PRC2), which also could explain their observed dynamic behavior [21,22].”
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Cites
Ashburner, M. (1989) · Cold Spring Harbor Laboratory eBooks · Cited by 6,756
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
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
The CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,828
Brownell, J. E., Zhou, J., Ranalli, T. A., Kobayashi, R., Edmondson, D. G., Dent, S., & Allis, C. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81063-6 · Cited by 1,636
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
A direct link between core histone acetylation and transcriptionally active chromatin.
Hebbes, T. R., Thorne, A. W., & Crane‐Robinson, C. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02956.x · Cited by 921
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
The TAFII250 Subunit of TFIID Has Histone Acetyltransferase Activity
Mizzen, C. A., Yang, X., Kokubo, T., Brownell, J. E., Bannister, A. J., Owen‐Hughes, T., Workman, J. L., Wang, L., Berger, S. L., Kouzarides, T., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81821-8 · Cited by 724
Cited by
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Items 301–400 of 578
Drosophila SIN3 Isoforms Interact with Distinct Proteins and Have Unique Biological Functions
Spain, M. M., Caruso, J. A., Swaminathan, A., & Pile, L. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.130245 · Cited by 47
Rodor, J., Pan, Q., Blencowe, B. J., Eyras, E., & Cáceres, J. F. (2016) · RNA · doi:10.1261/rna.057158.116 · Cited by 50
Vermeulen, M., Carrozza, M. J., Lasonder, E., Workman, J. L., Logie, C., & Stunnenberg, H. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2364-2372.2004 · Cited by 50
Singh, K. K., Erkelenz, S., Rattay, S., Dehof, A. K., Hildebrandt, A., Schulze‐Osthoff, K., Schaal, H., & Schwerk, C. (2010) · RNA · doi:10.1261/rna.2304410 · Cited by 46
Kim, M., Lu, F., & Zhang, Y. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.003 · Cited by 47
Self-citationSignal-dependent N-CoR Requirement for Repression by the Ski Oncoprotein
Ueki, N., & Hayman, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303447200 · Cited by 46
Takami, Y., Kikuchi, H., & Nakayama, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23977 · Cited by 46
Dorland, S., Deegenaars, M. L., & Stillman, D. J. (2000) · Genetics · doi:10.1093/genetics/154.2.573 · Cited by 44
Regulating the Regulators: The Role of Histone Deacetylase 1 (HDAC1) in Erythropoiesis
Kim, M. Y., Yan, B., Huang, S., & Qiu, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228460 · Cited by 47
Effects of Cell Density and Trichostatin A on the Expression ofHDAC1andp57Kip2in Hep 3B Cells
Gray, S. G., & Ekström, T. J. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8449 · Cited by 44
Transcriptional Anti-repression
Yang, Z., Hong, S.-H., & Privalsky, M. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37131 · Cited by 44
Khorashad, J. S., Eiring, A. M., Mason, C. C., Gantz, K. C., Bowler, A. D., Redwine, H. M., Yu, F., Kraft, I. L., Pomicter, A. D., Reynolds, K. R., et al. (2015) · Blood · doi:10.1182/blood-2014-08-588855 · Cited by 43
Sin3a regulates epithelial progenitor cell fate during lung development
Yao, C., Carraro, G., Konda, B. M., Guan, X., Mizuno, T., Chiba, N., Kostelny, M., Kurkciyan, A., David, G., McQualter, J. L., et al. (2017) · Development · doi:10.1242/dev.149708 · Cited by 39
McGarry, L., Winnie, J. N., & Ozanne, B. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207687 · Cited by 43
Zhao, C., York, A. J., Yang, F., Forsthoefel, D. J., Davé, V., Fu, D., Zhang, D., Corado, M., Small, S., Seeger, M. A., et al. (2002) · Development · doi:10.1242/dev.129.7.1669 · Cited by 43
Life with nucleosomes: chromatin remodelling in gene regulation
Gregory, P. D., & Hörz, W. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80009-4 · Cited by 43
Smirnov, D. A., Hou, S., & Ricciardi, R. P. (2000) · Virology · doi:10.1006/viro.1999.0181 · Cited by 43
Fujita, T., & Fujii, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103084 · Cited by 42
Lysine Deacetylase (KDAC) Regulatory Pathways: an Alternative Approach to Selective Modulation
Dyke, M. W. V. (2014) · ChemMedChem · doi:10.1002/cmdc.201300444 · Cited by 42
Modulation of YY1 activity by SAP30
Huang, N. E., Lin, C.-H., Lin, Y.-S., & Yu, W. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00966-5 · Cited by 42
The t(3;21) fusion product, AML1/Evi-1 blocks AML1-induced transactivation by recruiting CtBP
Izutsu, K., Kurokawa, M., Imai, Y., Ichikawa, M., Asai, T., Maki, K., Mitani, K., & Hirai, H. (2002) · Oncogene · doi:10.1038/sj.onc.1205356 · Cited by 41
Targeting succinylation-mediated metabolic reprogramming as a potential approach for cancer therapy
Liu, Z., Wang, R., Wang, Y., Duan, Y., & Zhan, H. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115713 · Cited by 43
The MTG proteins: chromatin repression players with a passion for networking
Rossetti, S., Hoogeveen, A. T., & Sacchi, N. (2004) · Genomics · doi:10.1016/j.ygeno.2004.02.011 · Cited by 41
Liberati, N. T., Moniwa, M., Borton, A. J., Davie, J., & Wang, X. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010778200 · Cited by 41
The homeobox gene Mohawk represses transcription by recruiting the sin3A/HDAC co‐repressor complex
Anderson, D. M., Beres, B. J., Wilson‐Rawls, J., & Rawls, A. (2009) · Developmental Dynamics · doi:10.1002/dvdy.21873 · Cited by 39
Histone deacetylases in replicative senescence: evidence for a senescence‐specific form of HDAC‐2
Wagner, M., Brosch, G., Zwerschke, W., Seto, E., Loidl, P., & Jansen‐Dürr, P. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02524-8 · Cited by 39
SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus
Viiri, K. M. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl401 · Cited by 39
Kwok, R. S., Li, Y. H., Lei, A. J., Edery, I., & Chiu, J. C. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005307 · Cited by 37
Miao, M., Yu, F., Wang, D.-Y., Tong, Y., Yang, L., Xu, J., Qiu, Y., Zhou, X., & Zhao, X. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00131-2 · Cited by 37
Histone H4 acetylation during interleukin‐2 stimulation of mouse T cells
Taplick, J., Kurtev, V., Egger, G., & Seiser, C. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01164-8 · Cited by 37
Xie, T., He, Y., Korkeamäki, H., Zhang, Y., Imhoff-Manuel, R. D., Lohi, O., & Radhakrishnan, I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252494 · Cited by 36
Self-citationExtension of the Binding Motif of the Sin3 Interacting Domain of the Mad Family Proteins,
van Ingen, H., Lasonder, E., Jansen, J. F. A., Kaan, A., Spronk, C. A. E. M., Stunnenberg, H. G., & Vuister, G. W. (2003) · Biochemistry · doi:10.1021/bi0355645 · Cited by 34
Guan, L., Li, G., Chen, C.-C., Liu, L.-Q., & Wang, Z. (2001) · International Journal of Cancer · doi:10.1002/ijc.1338 · Cited by 34
Identification of Drosophila Bicoid-interacting proteins using a custom two-hybrid selection
Zhu, W., & Hanes, S. D. (2000) · Gene · doi:10.1016/s0378-1119(00)00048-2 · Cited by 34
A SAGA of histone acetylation and gene expression
Hampsey, M. (1997) · Trends in Genetics · doi:10.1016/s0168-9525(97)01292-4 · Cited by 34
Bainor, A. J., Saini, S., Calderon, A., Casado-Polanco, R., Giner-Ramirez, B., Moncada, C., Cantor, D. J., Ernlund, A. W., Litovchick, L., & David, G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.024 · Cited by 35
Histone deacetylase complexes: functional entities or molecular reservoirs
Khochbin, S., & Kao, H. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02327-4 · Cited by 33
Endothelial Ribonuclease 1 in Cardiovascular and Systemic Inflammation
Bedenbender, K., & Schmeck, B. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576491 · Cited by 32
Resolving the deceptive isoform and complex selectivity of HDAC1/2 inhibitors
Payne, N. C., & Mazitschek, R. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.03.002 · Cited by 33
Rb-Associated Protein 46 (RbAp46) Inhibits Transcriptional Transactivation Mediated by BRCA1
Chen, G.-C., Guan, L., Yu, J., Li, G., Kim, H.-R. C., & Wang, Z. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5003 · Cited by 32
Hug, B. A., Lee, S. Y. D., Kinsler, E. L., Zhang, J., & Lazar, M. A. (2002) · PubMed · Cited by 32
Xu, Y., Harton, J. A., & Smith, B. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707180200 · Cited by 31
Fukumura, K., Wakabayashi, S., Kataoka, N., Sakamoto, H., Suzuki, Y., Nakai, K., Mayeda, A., & Inoue, K. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081153 · Cited by 32
Deka, B., & Singh, K. K. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.18649 · Cited by 26
Sichtig, N., Körfer, N., & Steger, G. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.08.015 · Cited by 29
Natsume, T., Tsutsui, Y., Sutani, T., Dunleavy, E. M., Pidoux, A. L., Iwasaki, H., Shirahige, K., Allshire, R. C., & Yamao, F. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002221 · Cited by 29
Banks, C. A. S., Thornton, J. L., Kempf, C. G., Adams, M. K., Miah, S., Boanca, G., Liu, X., Katt, M. L., Parmely, T. J., Florens, L. A., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.000661 · Cited by 29
Survival Motor Neuron (SMN) Protein Interacts with Transcription Corepressor mSin3A
Zou, J., Barahmand-Pour, F., Blackburn, M. L., Matsui, Y., Chansky, H. A., & Yang, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309218200 · Cited by 29
Avian erythroleukemia: a model for corepressor function in cancer
RIETVELD, L. E. G., Caldenhoven, E., & Stunnenberg, H. G. (2001) · Oncogene · doi:10.1038/sj.onc.1204335 · Cited by 29
Searching for the Magic Bullet Against Cancer: The Butyrate Saga
Sontini, V., Gozzini, A., Scappini, B., Grossi, A., & Ferrini, P. R. (2001) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428190109064584 · Cited by 29
Loss of the SIN3 transcriptional corepressor results in aberrant mitochondrial function
Barnes, V. L., Strunk, B. S., Lee, I., Hüttemann, M., & Pile, L. A. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-26 · Cited by 28
Suryadinata, R., Sadowski, M. C., Steel, R., & Šarčević, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.198473 · Cited by 28
Banach‐Orlowska, M., Pilecka, I., Toruń, A., Pyrzyńska, B., & Miączyńska, M. (2009) · Biochemical Journal · doi:10.1042/bj20090086 · Cited by 28
Li, G., Guan, L., & Wang, Z. (2003) · International Journal of Cancer · doi:10.1002/ijc.11148 · Cited by 28
Dynamics of epigenetic modifications in leukemia
Uribesalgo, I., & Croce, L. D. (2011) · Briefings in Functional Genomics · doi:10.1093/bfgp/elr002 · Cited by 29
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Wen, P., Quan, Z., & Xi, R. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23730 · Cited by 27
Creekmore, A. L., Walt, K. A., Schultz-Norton, J. R., Ziegler, Y., McLeod, I. X., Yates, J. R., & Nardulli, A. M. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.05.016 · Cited by 27
Miner, S. J., & Alarid, E. T. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-263 · Cited by 27
Farhana, L., Dawson, M. I., Xu, L., Dannenberg, J., & Fontana, J. A. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0964 · Cited by 27
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Ma, P., Lin, S., Bartolomei, M. S., & Schultz, R. M. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.110.086397 · Cited by 26
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Lange, M., Demajo, S., Jain, P., & Croce, L. D. (2011) · Epigenomics · doi:10.2217/epi.11.83 · Cited by 28
A comprehensive manually-curated compendium of bovine transcription factors
de Souza, M. M., Vaquerizas, J. M., Zerlotini, A., Geistlinger, L., Hernández-Rodríguez, B., Tizioto, P. C., Taylor, J. F., Rocha, M. I., Diniz, W. J. S., Coutinho, L. L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-32146-2 · Cited by 26
Role of Histone Deacetylase Complexes in the Regulation of Chromatin Metabolism
Kuzmichev, A., & Reinberg, D. (2001) · Current topics in microbiology and immunology · doi:10.1007/978-3-662-10595-5_2 · Cited by 26
Self-citationTranscripts from a human primordial follicle cDNA library
Serafica, M. D., Goto, T., & Trounson, A. O. (2005) · Human Reproduction · doi:10.1093/humrep/dei030 · Cited by 26
Histone acetylation and the control of the cell cycle
Magnaghi-Jaulin, L., Ait‐Si‐Ali, S., & Harel‐Bellan, A. (2000) · Springer eBooks · doi:10.1007/978-1-4615-4253-7_4 · Cited by 26
MBP-1 Physically Associates with Histone Deacetylase for Transcriptional Repression
Ghosh, A. K., Steele, R., & Ray, R. B. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0921 · Cited by 26
Transcriptional control: Calling in histone deacetylase
Kiermaier, A. C., & Eilers, M. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00249-1 · Cited by 26
Lymphoid Transcription of the Murine CD21 Gene Is Positively Regulated by Histone Acetylation
Zabel, M. D., Weis, J. J., & Weis, J. H. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2697 · Cited by 26
Regulation of cell proliferation and wing development by Drosophila SIN3 and String
Swaminathan, A., & Pile, L. A. (2009) · Mechanisms of Development · doi:10.1016/j.mod.2009.10.003 · Cited by 25
Chen, S. L., Rooney, T. J., Hu, A., Beard, H. S., Garrett, W. M., Mangalath, L. M., Powers, J. J., Cooper, B., & Zhang, X. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01116 · Cited by 24
RBBP4 promotes colon cancer malignant progression via regulating Wnt/β-catenin pathway
Li, Y., Lv, Z., & Zhu, W. (2020) · World Journal of Gastroenterology · doi:10.3748/wjg.v26.i35.5328 · Cited by 25
Latypova, X., Vincent, M., Mollé, A., Adebambo, O. A., Fourgeux, C., Khan, T. N., Caro‐Llopis, A., Rosello, M., Orellana, C., Niyazov, D. M., et al. (2021) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2021.03.017 · Cited by 25
Sin3A-associated protein, 18 kDa, a novel binding partner of TRIB1, regulates MTTP expression [S]
Makishima, S., Boonvisut, S., Ishizuka, Y., Watanabe, K., Nakayama, K., & Iwamoto, S. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m057802 · Cited by 25
Yang, Y., Wang, X., Dong, T., Kim, E., Lin, W.-J., & Chang, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207116200 · Cited by 25
Shen, J., Wu, H., & Gudas, L. J. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4963 · Cited by 25
Autophagy-related intrinsically disordered proteins in intra-nuclear compartments
Na, I., Meng, F., Kurgan, L., & Uversky, V. N. (2016) · Molecular BioSystems · doi:10.1039/c6mb00069j · Cited by 24
Epigenetic targeting in breast cancer: Therapeutic impact and future direction
Lustberg, M. B., & Ramaswamy, B. (2009) · Drug News & Perspectives · doi:10.1358/dnp.2009.22.7.1405072 · Cited by 24
Singh, N., Zhu, W., & Hanes, S. D. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.11.011 · Cited by 24
Cloning and Characterization of the Mouse Histone Deacetylase-2 Gene
Zeng, Y., Tang, C.-M., Yao, Y., Yang, W., & Seto, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28921 · Cited by 24
List, H.-J., Smith, C. L., Rodriguez, O. C., Danielsen, M., & Riegel, A. T. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4638 · Cited by 24
Chromatin organisation and human disease
Urnov, F. D., & Wolffe, A. P. (2000) · Emerging Therapeutic Targets · doi:10.1517/14728222.4.5.665 · Cited by 24
αα-Hub domains and intrinsically disordered proteins: A decisive combo
Bugge, K., Staby, L., Salladini, E., Falbe-Hansen, R. G., Kragelund, B. B., & Skriver, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.012928 · Cited by 23
Nabeel‐Shah, S., Garg, J., Saettone, A., Ashraf, K., Lee, H., Wahab, S., Ahmed, N., Fine, J. L., Derynck, J., Pu, S., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab413 · Cited by 23
Chen, Z., Zou, Y., Zhang, Y., Chen, Z., Wu, F., Shi, N., & Jin, H. (2021) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.24005 · Cited by 23
Self-citationHagelkrüys, A., Mattes, K., Moos, V., Rennmayr, M., Ringbauer, M., Sawicka, A., & Seiser, C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00639-15 · Cited by 23
Li, Y., Lv, Z., Xie, H., & Zheng, S. (2019) · Hepatobiliary & pancreatic diseases international · doi:10.1016/j.hbpd.2019.08.006 · Cited by 23
Molecular Mechanisms of Corepressor Function
Urnov, F. D., Wolffe, A. P., & Guschin, D. Y. (2001) · Current topics in microbiology and immunology · doi:10.1007/978-3-662-10595-5_1 · Cited by 23
Zabel, M. D., Byrne, B. L., Weis, J. J., & Weis, J. H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.8.4437 · Cited by 23
Human factors and pathways essential for mediating epigenetic gene silencing
Poleshko, A. S., Kossenkov, A. V., Shalginskikh, N., Pecherskaya, A., Pecherskaya, A., Einarson, M. B., Einarson, M. B., Skalka, A. M., Skalka, A. M., Katz, R. A., et al. (2014) · Epigenetics · doi:10.4161/epi.32088 · Cited by 22
Navigating the Global Protein–Protein Interaction Landscape Using iRefWeb
Turinsky, A. L., Razick, S., Turner, B., Donaldson, I. M., & Wodak, S. J. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-691-7_22 · Cited by 22
Lee, H. G., Hong, C., & Seo, P. J. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00171 · Cited by 21
Distinct Histone H3 Lysine 27 Modifications Dictate Different Outcomes of Gene Transcription
Konuma, T., & Zhou, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168376 · Cited by 25
Agnelli, L., Bicciato, S., Fabris, S., Baldini, L., Morabito, F. C., Intini, D., Verdelli, D., Callegaro, A., Bertoni, F., Lambertenghi‐Deliliers, G., et al. (2007) · Haematologica · doi:10.3324/haematol.10414 · Cited by 21
Literature-related discovery: common factors for Parkinson’s Disease and Crohn’s Disease
Kostoff, R. N. (2014) · Scientometrics · doi:10.1007/s11192-014-1298-3 · Cited by 21
Suppression of Sin3A activity promotes differentiation of pluripotent cells into functional neurons
Halder, D., Lee, C., Hyun, J. Y., Chang, G.-E., Cheong, E., & Shin, I. (2017) · Scientific Reports · doi:10.1038/srep44818 · Cited by 21
Germ-line mutations in WDR77 predispose to familial papillary thyroid cancer
Zhao, Y., Yu, T., Sun, J., Wang, F., Cheng, C., He, S.-R., Chen, L., Xie, D.-H., Fu, L., Guan, X., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026327118 · Cited by 20
Yang, Z., Tang, H., Huang, H. Y., & Deng, H. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004556 · Cited by 20
Ahmad, A., Takami, Y., & Nakayama, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.073 · Cited by 20
Khier, H., Bartl, S., Schuettengruber, B., & Seiser, C. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00203-1 · Cited by 20
Metadata
- Authors
- Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Reinberg, Danny
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 89
- Issue
- 3
- Pages
- 357-364
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2074096799
- Cited by
- 578
- References
- 44
- Citations by year
- 2026: 6 · 2025: 10 · 2024: 10 · 2023: 14 · 2022: 8 · 2021: 14 · 2020: 14 · 2019: 11 · 2018: 10 · 2017: 8 · 2016: 15 · 2015: 11 · 2014: 18 · 2013: 14 · 2012: 6
- FWCI
- 19.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01gm048518-05)
- National Cancer Institute (5P309CA08748)
- National Institute of General Medical Sciences (GM37120, GM-48518)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase, HDAC1, HDAC2, SAP18, SAP30, transcriptional repression, histone deacetylation, histone modifications, protein-protein interaction, core histones, transcriptional repressor
- MeSH terms
- Animals, Carrier Proteins, Cell Fractionation, HeLa Cells, Histone Deacetylases, Humans, Mammals, Molecular Sequence Data, Multienzyme Complexes, Nuclear Proteins, Precipitin Tests, Repressor Proteins, Retinoblastoma, Transcription Factors, Transcription, Genetic, Blotting, Western, RNA-Binding Proteins, Sequence Homology, Amino Acid, Saccharomyces cerevisiae Proteins, Retinoblastoma-Binding Protein 4, Retinoblastoma-Binding Protein 7, Co-Repressor Proteins
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