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Histona deacetilasa 1

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(Redirigido desde «HDAC1»)
Histona deacetilasa 1
Estructuras disponibles
PDB

Buscar ortólogos: PDBe, RCSB

 Lista de códigos PDB
4BKX
 Estructuras enzimáticas
RCSB PDB, PDBe, PDBsum
Identificadores
Símbolos HDAC1 (HGNC: 4852) DKFZp686H12203; GON-10; HD1; RPD3; RPD3L1
Identificadores
externos
 Bases de datos de enzimas
IntEnz: entrada en IntEnz
BRENDA: entrada en BRENDA
ExPASy: NiceZime view
KEGG: entrada en KEEG
PRIAM: perfil PRIAM
ExplorEnz: entrada en ExplorEnz
MetaCyc: vía metabólica
Número EC 3.5.1.98
Locus Cr. 1 p35.1
Patrón de expresión de ARNm
ancho=250px
Más información
Ortólogos
Especies
Humano Ratón
Entrez
3065 433759
Ensembl
Véase HS Véase MM
UniProt
Q13547 O09106
RefSeq
(ARNm)
NM_004964 NM_008228
RefSeq
(proteína) NCBI
NP_004955 NP_032254
Ubicación (UCSC)
Cr. 1:
32.76 – 32.8 Mb 		Cr. 4:
129.52 – 129.54 Mb
PubMed (Búsqueda)
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La histona deacetilasa 1 (HDAC1) es una enzima codificada en humanos por el gen HDAC1.[1]​

Función

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Las histonas juegan un papel crucial en la regulación de la transcripción, en la progresión del ciclo celular y en procesos de desarrollo. La acetilación/desacetilación de histonas altera la estructura del cromosoma, variando así la accesibilidad de los factores de transcripción al ADN. La proteína HDAC1 pertenece a la familia de histona deacetilasas acuc/alfa y es uno de los componentes del complejo histona deacetilasa. Esta proteína interacciona con la proteína del retinoblastoma formando un complejo que es un elemento clave en el control de la proliferación celular y la diferenciación celular. Junto con la proteína 2 asociada a metástasis, deacetila a p53 y modula su acción sobre la proliferación celular y la apoptosis.[2]​

Interacciones

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La histona deacetilasa 1 ha demostrado ser capaz de interaccionar con:

Véase también

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Referencias

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  1. ↑ Taunton, J.; Hassig, C.A.; Schreiber, S.L. (Mayo de 1996). «A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p». Science 272 (5260): 408-11. PMID 8602529. doi:10.1126/science.272.5260.408. 
  2. ↑ «Entrez Gene: HDAC1 histone deacetylase 1». 
  3. ↑ a b Cai, R. L.; Yan-Neale, Y.; Cueto, M. A.; Xu, H.; Cohen, D. (Septiembre de 2000). «HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins». J. Biol. Chem. (Estados Unidos) 275 (36): 27909-16. ISSN 0021-9258. PMID 10846170. doi:10.1074/jbc.M000168200. 
  4. ↑ Aapola, U.; Liiv, I.; Peterson, P. (Agosto de 2002). «Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity». Nucleic Acids Res. (Inglaterra) 30 (16): 3602-8. PMC 134241. PMID 12177302. doi:10.1093/nar/gkf474. 
  5. ↑ Deplus, R.; Brenner, C.; Burgers, W. A.; Putmans, P.; Kouzarides, T.; de Launoit, Y.; Fuks, F. (Septiembre de 2002). «Dnmt3L is a transcriptional repressor that recruits histone deacetylase». Nucleic Acids Res. (Inglaterra) 30 (17): 3831-8. PMC 137431. PMID 12202768. doi:10.1093/nar/gkf509. 
  6. ↑ a b c d e f g Yao, Y.; Yang, W. (Octubre de 2003). «The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity». J. Biol. Chem. (Estados Unidos) 278 (43): 42560-8. ISSN 0021-9258. PMID 12920132. doi:10.1074/jbc.M302955200. 
  7. ↑ Mazumdar, A.; Wang, R. A.; Mishra, S. K.; Adam, L.; Bagheri-Yarmand, R.; Mandal, M.; Vadlamudi, R. K.; Kumar, R. (Enero de 2001). «Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor». Nat. Cell Biol. (Inglaterra) 3 (1): 30-7. ISSN 1465-7392. PMID 11146623. doi:10.1038/35050532. 
  8. ↑ Yang, W. M.; Yao, Y. L.; Seto, E. (Septiembre de 2001). «The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1». EMBO J. (Inglaterra) 20 (17): 4814-25. ISSN 0261-4189. PMC 125595. PMID 11532945. doi:10.1093/emboj/20.17.4814. 
  9. ↑ a b c d e f Yoon, Y.; Baek, K.; Jeong, S.; Shin, H.; Ha, G.; Jeon, A.; Hwang, S.; Chun, J. et al. (Septiembre de 2004). «WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase». FEBS Lett. (Países Bajos) 575 (1-3): 23-9. ISSN 0014-5793. PMID 15388328. doi:10.1016/j.febslet.2004.07.089. 
  10. ↑ Wysocka, J.; Myers Michael, P.; Laherty, C. D.; Eisenman, R. N.; Herr, W. (Abril de 2003). «Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1». Genes Dev. (Estados Unidos) 17 (7): 896-911. ISSN 0890-9369. PMC 196026. PMID 12670868. doi:10.1101/gad.252103. 
  11. ↑ a b Fischer, Denise D; Cai Richard, Bhatia Umesh, Asselbergs Fred A M, Song Chuanzheng, Terry Robert, Trogani Nancy, Widmer Roland, Atadja Peter, Cohen Dalia (Feb. de 2002). «Isolation and characterization of a novel class II histone deacetylase, HDAC10». J. Biol. Chem. (United States) 277 (8): 6656-66. ISSN 0021-9258. PMID 11739383. doi:10.1074/jbc.M108055200. 
  12. ↑ Underhill, C; Qutob M S, Yee S P, Torchia J (Dec. de 2000). «A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1». J. Biol. Chem. (UNITED STATES) 275 (51): 40463-70. ISSN 0021-9258. PMID 11013263. doi:10.1074/jbc.M007864200. 
  13. ↑ a b Koipally, J; Renold A; Kim J; Georgopoulos K (Jun. de 1999). «Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes». EMBO J. (ENGLAND) 18 (11): 3090-100. ISSN 0261-4189. PMID 10357820. doi:10.1093/emboj/18.11.3090. 
  14. ↑ Koipally, Joseph; Georgopoulos Katia (Aug. de 2002). «A molecular dissection of the repression circuitry of Ikaros». J. Biol. Chem. (United States) 277 (31): 27697-705. ISSN 0021-9258. PMID 12015313. doi:10.1074/jbc.M201694200. 
  15. ↑ Joshi, Bharat; Ko Danette, Ordonez-Ercan Dalia, Chellappan Srikumar P (Dec. de 2003). «A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis». Biochem. Biophys. Res. Commun. (United States) 312 (2): 459-66. ISSN 0006-291X. PMID 14637159. 
  16. ↑ a b Wang, Sheng; Fusaro Gina, Padmanabhan Jaya, Chellappan Srikumar P (Dec. de 2002). «Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression». Oncogene (England) 21 (55): 8388-96. ISSN 0950-9232. PMID 12466959. doi:10.1038/sj.onc.1208634. 
  17. ↑ Vinatzer, U; Taplick J; Seiser C; Fonatsch C; Wieser R (Sep. de 2001). «The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase». Br. J. Haematol. (England) 114 (3): 566-73. ISSN 0007-1048. PMID 11552981. 
  18. ↑ Chakraborty, S; Senyuk V; Sitailo S; Chi Y; Nucifora G (Nov. de 2001). «Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles». J. Biol. Chem. (United States) 276 (48): 44936-43. ISSN 0021-9258. PMID 11568182. doi:10.1074/jbc.M106733200. 
  19. ↑ a b Wilson, Brian J; Bates Gaynor J, Nicol Samantha M, Gregory David J, Perkins Neil D, Fuller-Pace Frances V (Aug. de 2004). «The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner». BMC Mol. Biol. (England) 5: 11. PMID 15298701. doi:10.1186/1471-2199-5-11. 
  20. ↑ Fuks, F; Burgers W A, Godin N, Kasai M, Kouzarides T (May. de 2001). «Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription». EMBO J. (England) 20 (10): 2536-44. ISSN 0261-4189. PMID 11350943. doi:10.1093/emboj/20.10.2536. 
  21. ↑ Wotton, D; Lo R S, Lee S, Massagué J (Apr. de 1999). «A Smad transcriptional corepressor». Cell (UNITED STATES) 97 (1): 29-39. ISSN 0092-8674. PMID 10199400. 
  22. ↑ a b c d Hakimi, Mohamed-Ali; Bochar Daniel A, Chenoweth Josh, Lane William S, Mandel Gail, Shiekhattar Ramin (May. de 2002). «A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes». Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (11): 7420-5. ISSN 0027-8424. PMID 12032298. doi:10.1073/pnas.112008599. 
  23. ↑ Hakimi, Mohamed-Ali; Dong Yuanshu, Lane William S, Speicher David W, Shiekhattar Ramin (Feb. de 2003). «A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes». J. Biol. Chem. (United States) 278 (9): 7234-9. ISSN 0021-9258. PMID 12493763. doi:10.1074/jbc.M208992200. 
  24. ↑ Fischle, Wolfgang; Dequiedt Franck, Hendzel Michael J, Guenther Matthew G, Lazar Mitchell A, Voelter Wolfgang, Verdin Eric (Jan. de 2002). «Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR». Mol. Cell (United States) 9 (1): 45-57. ISSN 1097-2765. PMID 11804585. 
  25. ↑ a b Johnson, Colin A; White Darren A, Lavender Jayne S, O'Neill Laura P, Turner Bryan M (Mar. de 2002). «Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70». J. Biol. Chem. (United States) 277 (11): 9590-7. ISSN 0021-9258. PMID 11777905. doi:10.1074/jbc.M107942200. 
  26. ↑ Fischle, W; Dequiedt F, Fillion M, Hendzel M J, Voelter W, Verdin E (Sep. de 2001). «Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo». J. Biol. Chem. (United States) 276 (38): 35826-35. ISSN 0021-9258. PMID 11466315. doi:10.1074/jbc.M104935200. 
  27. ↑ a b Ashburner, B P; Westerheide S D, Baldwin A S (Oct. de 2001). «The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression». Mol. Cell. Biol. (United States) 21 (20): 7065-77. ISSN 0270-7306. PMID 11564889. doi:10.1128/MCB.21.20.7065-7077.2001. 
  28. ↑ a b c d e f g h i Zhang, Y; Ng H H, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (Aug. de 1999). «Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation». Genes Dev. (UNITED STATES) 13 (15): 1924-35. ISSN 0890-9369. PMID 10444591. 
  29. ↑ a b c d Tong, J K; Hassig C A, Schnitzler G R, Kingston R E, Schreiber S L (Oct. de 1998). «Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex». Nature (ENGLAND) 395 (6705): 917-21. ISSN 0028-0836. PMID 9804427. doi:10.1038/27699. 
  30. ↑ a b c Hassig, C A; Tong J K, Fleischer T C, Owa T, Grable P G, Ayer D E, Schreiber S L (Mar. de 1998). «A role for histone deacetylase activity in HDAC1-mediated transcriptional repression». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (7): 3519-24. ISSN 0027-8424. PMID 9520398. 
  31. ↑ a b c Zhang, Y; Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May. de 1997). «Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex». Cell (UNITED STATES) 89 (3): 357-64. ISSN 0092-8674. PMID 9150135. 
  32. ↑ a b c van der Vlag, J; Otte A P (Dec. de 1999). «Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation». Nat. Genet. (UNITED STATES) 23 (4): 474-8. ISSN 1061-4036. PMID 10581039. doi:10.1038/70602. 
  33. ↑ Ding, Zhihu; Gillespie Laura L, Paterno Gary D (Jan. de 2003). «Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain». Mol. Cell. Biol. (United States) 23 (1): 250-8. ISSN 0270-7306. PMID 12482978. 
  34. ↑ a b Zhang, Ying; Dufau Maria L (Jun. de 2003). «Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes». J. Steroid Biochem. Mol. Biol. (England) 85 (2-5): 401-14. ISSN 0960-0760. PMID 12943729. 
  35. ↑ a b Fleischer, Tracey C; Yun Ui Jeong, Ayer Donald E (May. de 2003). «Identification and characterization of three new components of the mSin3A corepressor complex». Mol. Cell. Biol. (United States) 23 (10): 3456-67. ISSN 0270-7306. PMID 12724404. 
  36. ↑ Yang, Liu; Mei Qi, Zielinska-Kwiatkowska Anna, Matsui Yoshito, Blackburn Michael L, Benedetti Daniel, Krumm Anton A, Taborsky Gerald J, Chansky Howard A (Feb. de 2003). «An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B». Biochem. J. (England) 369 (Pt 3): 651-7. ISSN 0264-6021. PMID 12398767. doi:10.1042/BJ20020854. 
  37. ↑ a b c Grozinger, C M; Hassig C A, Schreiber S L (Apr. de 1999). «Three proteins define a class of human histone deacetylases related to yeast Hda1p». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (9): 4868-73. ISSN 0027-8424. PMID 10220385. 
  38. ↑ Zhang, Jinsong; Kalkum Markus, Chait Brian T, Roeder Robert G (Mar. de 2002). «The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2». Mol. Cell (United States) 9 (3): 611-23. ISSN 1097-2765. PMID 11931768. 
  39. ↑ a b c d You, A; Tong J K, Grozinger C M, Schreiber S L (Feb. de 2001). «CoREST is an integral component of the CoREST- human histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (4): 1454-8. ISSN 0027-8424. PMID 11171972. doi:10.1073/pnas.98.4.1454. 
  40. ↑ a b c Zhang, Ying; Dufau Maria L (Sep. de 2002). «Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex». J. Biol. Chem. (United States) 277 (36): 33431-8. ISSN 0021-9258. PMID 12091390. doi:10.1074/jbc.M204417200. 
  41. ↑ a b c Yasui, Dag; Miyano Masaru, Cai Shutao, Varga-Weisz Patrick, Kohwi-Shigematsu Terumi (Oct. de 2002). «SATB1 targets chromatin remodelling to regulate genes over long distances». Nature (England) 419 (6907): 641-5. ISSN 0028-0836. PMID 12374985. doi:10.1038/nature01084. 
  42. ↑ Huang, E Y; Zhang J, Miska E A, Guenther M G, Kouzarides T, Lazar M A (Jan. de 2000). «Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway». Genes Dev. (UNITED STATES) 14 (1): 45-54. ISSN 0890-9369. PMID 10640275. 
  43. ↑ a b c d Kuzmichev, A; Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb. de 2002). «Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)». Mol. Cell. Biol. (United States) 22 (3): 835-48. ISSN 0270-7306. PMID 11784859. 
  44. ↑ Li, H; Leo C, Zhu J, Wu X, O'Neil J, Park E J, Chen J D (Mar. de 2000). «Sequestration and inhibition of Daxx-mediated transcriptional repression by PML». Mol. Cell. Biol. (UNITED STATES) 20 (5): 1784-96. ISSN 0270-7306. PMID 10669754. 
  45. ↑ Gaughan, Luke; Logan Ian R, Cook Susan, Neal David E, Robson Craig N (Jul. de 2002). «Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor». J. Biol. Chem. (United States) 277 (29): 25904-13. ISSN 0021-9258. PMID 11994312. doi:10.1074/jbc.M203423200. 
  46. ↑ Vietor, Ilja; Vadivelu Santhosh K, Wick Nikolaus, Hoffman Robert, Cotten Matt, Seiser Christian, Fialka Irene, Wunderlich Winfried, Haase Astrid, Korinkova Gabriela, Brosch Gerald, Huber Lukas A (Sep. de 2002). «TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells». EMBO J. (England) 21 (17): 4621-31. ISSN 0261-4189. PMID 12198164. 
  47. ↑ Xia, Zhen-Biao; Anderson Melanie, Diaz Manuel O, Zeleznik-Le Nancy J (Jul. de 2003). «MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein». Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (14): 8342-7. ISSN 0027-8424. PMID 12829790. doi:10.1073/pnas.1436338100. 
  48. ↑ Vieyra, Diego; Loewith Robbie, Scott Michelle, Bonnefin Paul, Boisvert Francois-Michel, Cheema Parneet, Pastyryeva Svitlana, Meijer Maria, Johnston Randal N, Bazett-Jones David P, McMahon Steven, Cole Michael D, Young Dallan, Riabowol Karl (Aug. de 2002). «Human ING1 proteins differentially regulate histone acetylation». J. Biol. Chem. (United States) 277 (33): 29832-9. ISSN 0021-9258. PMID 12015309. doi:10.1074/jbc.M200197200. 
  49. ↑ a b Puri, P L; Iezzi S, Stiegler P, Chen T T, Schiltz R L, Muscat G E, Giordano A, Kedes L, Wang J Y, Sartorelli V (Oct. de 2001). «Class I histone deacetylases sequentially interact with MyoD and pRb during skeletal myogenesis». Mol. Cell (United States) 8 (4): 885-97. ISSN 1097-2765. PMID 12479798. 
  50. ↑ Mal, A; Sturniolo M, Schiltz R L, Ghosh M K, Harter M L (Apr. de 2001). «A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program». EMBO J. (England) 20 (7): 1739-53. ISSN 0261-4189. PMID 11285237. doi:10.1093/emboj/20.7.1739. 
  51. ↑ Watamoto, Kouichi; Towatari Masayuki, Ozawa Yukiyasu, Miyata Yasuhiko, Okamoto Mitsunori, Abe Akihiro, Naoe Tomoki, Saito Hidehiko (Dec. de 2003). «Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation». Oncogene (England) 22 (57): 9176-84. ISSN 0950-9232. PMID 14668799. doi:10.1038/sj.onc.1206902. 
  52. ↑ Shi, Y; Downes M, Xie W, Kao H Y, Ordentlich P, Tsai C C, Hon M, Evans R M (May. de 2001). «Sharp, an inducible cofactor that integrates nuclear receptor repression and activation». Genes Dev. (United States) 15 (9): 1140-51. ISSN 0890-9369. PMID 11331609. doi:10.1101/gad.871201. 
  53. ↑ Khan, M M; Nomura T, Kim H, Kaul S C, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi P P, Ishii S (Jun. de 2001). «Role of PML and PML-RARalpha in Mad-mediated transcriptional repression». Mol. Cell (United States) 7 (6): 1233-43. ISSN 1097-2765. PMID 11430826. 
  54. ↑ Wu, W S; Vallian S, Seto E, Yang W M, Edmondson D, Roth S, Chang K S (Apr. de 2001). «The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases». Mol. Cell. Biol. (United States) 21 (7): 2259-68. ISSN 0270-7306. PMID 11259576. doi:10.1128/MCB.21.7.2259-2268.2001. 
  55. ↑ a b Melhuish, T A; Wotton D (Dec. de 2000). «The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF». J. Biol. Chem. (UNITED STATES) 275 (50): 39762-6. ISSN 0021-9258. PMID 10995736. doi:10.1074/jbc.C000416200. 
  56. ↑ Melhuish, T A; Gallo C M, Wotton D (Aug. de 2001). «TGIF2 interacts with histone deacetylase 1 and represses transcription». J. Biol. Chem. (United States) 276 (34): 32109-14. ISSN 0021-9258. PMID 11427533. doi:10.1074/jbc.M103377200. 
  57. ↑ a b c Ferreira, R; Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (Sep. de 1998). «The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (18): 10493-8. ISSN 0027-8424. PMID 9724731. 
  58. ↑ Bouzahzah, B; Fu M, Iavarone A, Factor V M, Thorgeirsson S S, Pestell R G (Aug. de 2000). «Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo». Cancer Res. (UNITED STATES) 60 (16): 4531-7. ISSN 0008-5472. PMID 10969803. 
  59. ↑ a b Lai, A; Lee J M, Yang W M, DeCaprio J A, Kaelin W G, Seto E, Branton P E (Oct. de 1999). «RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins». Mol. Cell. Biol. (UNITED STATES) 19 (10): 6632-41. ISSN 0270-7306. PMID 10490602. 
  60. ↑ a b c Ng, H H; Zhang Y, Hendrich B, Johnson C A, Turner B M, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (Sep. de 1999). «MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex». Nat. Genet. (UNITED STATES) 23 (1): 58-61. ISSN 1061-4036. PMID 10471484. doi:10.1038/12659. 
  61. ↑ Anderson, Lisa A; Perkins Neil D (Aug. de 2002). «The large subunit of replication factor C interacts with the histone deacetylase, HDAC1». J. Biol. Chem. (United States) 277 (33): 29550-4. ISSN 0021-9258. PMID 12045192. doi:10.1074/jbc.M200513200. 
  62. ↑ Dick, F A; Sailhamer E, Dyson N J (May. de 2000). «Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins». Mol. Cell. Biol. (UNITED STATES) 20 (10): 3715-27. ISSN 0270-7306. PMID 10779361. 
  63. ↑ Fuks, F; Burgers W A, Brehm A, Hughes-Davies L, Kouzarides T (Jan. de 2000). «DNA methyltransferase Dnmt1 associates with histone deacetylase activity». Nat. Genet. (UNITED STATES) 24 (1): 88-91. ISSN 1061-4036. PMID 10615135. doi:10.1038/71750. 
  64. ↑ Luo, R X; Postigo A A, Dean D C (Feb. de 1998). «Rb interacts with histone deacetylase to repress transcription». Cell (UNITED STATES) 92 (4): 463-73. ISSN 0092-8674. PMID 9491888. 
  65. ↑ Nicolas, E; Ait-Si-Ali S, Trouche D (Aug. de 2001). «The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein». Nucleic Acids Res. (England) 29 (15): 3131-6. PMID 11470869. 
  66. ↑ Hassig, C A; Fleischer T C, Billin A N, Schreiber S L, Ayer D E (May. de 1997). «Histone deacetylase activity is required for full transcriptional repression by mSin3A». Cell (UNITED STATES) 89 (3): 341-7. ISSN 0092-8674. PMID 9150133. 
  67. ↑ Iwase, Shigeki; Januma Aya, Miyamoto Kiyoko, Shono Naomi, Honda Arata, Yanagisawa Junn, Baba Tadashi (Sep. de 2004). «Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression». Biochem. Biophys. Res. Commun. (United States) 322 (2): 601-8. ISSN 0006-291X. PMID 15325272. doi:10.1016/j.bbrc.2004.07.163. 
  68. ↑ Kiernan, Rosemary; Brès Vanessa, Ng Raymond W M, Coudart Marie-Pierre, El Messaoudi Selma, Sardet Claude, Jin Dong-Yan, Emiliani Stephane, Benkirane Monsef (Jan. de 2003). «Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65». J. Biol. Chem. (United States) 278 (4): 2758-66. ISSN 0021-9258. PMID 12419806. doi:10.1074/jbc.M209572200. 
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  71. ↑ Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. de 2002). «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. (England) 30 (2): 475-81. PMID 11788710. 
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  77. ↑ Alland, Leila; David Gregory, Shen-Li Hong, Potes Jason, Muhle Rebecca, Lee Hye-Chun, Hou Harry, Chen Ken, DePinho Ronald A (Apr. de 2002). «Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex». Mol. Cell. Biol. (United States) 22 (8): 2743-50. ISSN 0270-7306. PMID 11909966. 
  78. ↑ Huang, Nu En; Lin Ching Hui, Lin Young Sun, Yu Winston C Y (Jun. de 2003). «Modulation of YY1 activity by SAP30». Biochem. Biophys. Res. Commun. (United States) 306 (1): 267-75. ISSN 0006-291X. PMID 12788099. 
  79. ↑ Zhang, Y; Sun Z W, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (Jun. de 1998). «SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex». Mol. Cell (UNITED STATES) 1 (7): 1021-31. ISSN 1097-2765. PMID 9651585. 
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  82. ↑ Di Padova, Monica; Bruno Tiziana, De Nicola Francesca, Iezzi Simona, D'Angelo Carmen, Gallo Rita, Nicosia Daniela, Corbi Nicoletta, Biroccio Annamaria, Floridi Aristide, Passananti Claudio, Fanciulli Maurizio (Sep. de 2003). «Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter». J. Biol. Chem. (United States) 278 (38): 36496-504. ISSN 0021-9258. PMID 12847090. doi:10.1074/jbc.M306694200. 
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  84. ↑ Sun, Jian-Min; Chen Hou Yu, Moniwa Mariko, Litchfield David W, Seto Edward, Davie James R (Sep. de 2002). «The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2». J. Biol. Chem. (United States) 277 (39): 35783-6. ISSN 0021-9258. PMID 12176973. doi:10.1074/jbc.C200378200. 
  85. ↑ Milutinovic, Snezana; Zhuang Qianli, Szyf Moshe (Jun. de 2002). «Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification». J. Biol. Chem. (United States) 277 (23): 20974-8. ISSN 0021-9258. PMID 11929879. doi:10.1074/jbc.M202504200. 
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  94. ↑ Smirnov, D A; Hou S, Ricciardi R P (Mar. de 2000). «Association of histone deacetylase with COUP-TF in tumorigenic Ad12-transformed cells and its potential role in shut-off of MHC class I transcription». Virology (UNITED STATES) 268 (2): 319-28. ISSN 0042-6822. PMID 10704340. doi:10.1006/viro.1999.0181. 

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