HDAC1: Difference between revisions
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{{Short description|Protein-coding gene in the species Homo sapiens}} |
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'''Histone deacetylase 1 (HDAC1 |
'''Histone deacetylase 1''' ('''HDAC1''') is an [[enzyme]] that in humans is encoded by the ''HDAC1'' [[gene]].<ref name="pmid8602529">{{cite journal | vauthors = Taunton J, Hassig CA, Schreiber SL | title = A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p | journal = Science | volume = 272 | issue = 5260 | pages = 408–11 | date = April 1996 | pmid = 8602529 | doi = 10.1126/science.272.5260.408 | bibcode = 1996Sci...272..408T | s2cid = 25717734 }}</ref> |
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== Function == |
== Function == |
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Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of [[eukaryotic]] gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 [[MTA2]], it deacetylates [[p53]] and modulates its effect on cell growth and apoptosis.<ref name="entrez">{{cite web | title = Entrez Gene: HDAC1 histone deacetylase 1| url = |
[[Histone acetylation and deacetylation]], catalyzed by multisubunit complexes, play a key role in the regulation of [[eukaryotic]] gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 [[MTA2]], it deacetylates [[p53]] and modulates its effect on cell growth and apoptosis.<ref name="entrez">{{cite web | title = Entrez Gene: HDAC1 histone deacetylase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3065}}</ref> |
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== Model organisms == |
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{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" | |
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|+ ''Hdac1'' knockout mouse phenotype |
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! Characteristic!! Phenotype |
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| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal |
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| [[Recessive]] lethal study || bgcolor="#C40000"|Abnormal |
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| Fertility || bgcolor="#488ED3"|Normal |
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| Body weight || bgcolor="#488ED3"|Normal |
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| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal |
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| Neurological assessment || bgcolor="#488ED3"|Normal |
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| Grip strength || bgcolor="#488ED3"|Normal |
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| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal |
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| [[Dysmorphology]] || bgcolor="#488ED3"|Normal |
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| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal |
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| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal |
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| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal |
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| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal |
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| [[Radiography]] || bgcolor="#488ED3"|Normal |
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| Body temperature || bgcolor="#488ED3"|Normal |
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| Eye morphology || bgcolor="#488ED3"|Normal |
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| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal |
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| [[Haematology]] || bgcolor="#488ED3"|Normal |
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| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal |
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| [[Micronucleus test]] || bgcolor="#488ED3"|Normal |
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| Heart weight || bgcolor="#488ED3"|Normal |
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| Brain histopathology || bgcolor="#488ED3"|Normal |
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| Eye Histopathology || bgcolor="#488ED3"|Normal |
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| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAAW/salmonella-challenge/ |title=''Salmonella'' infection data for Hdac1 |publisher=Wellcome Trust Sanger Institute}}</ref> |
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| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAAW/citrobacter-challenge/ |title=''Citrobacter'' infection data for Hdac1 |publisher=Wellcome Trust Sanger Institute}}</ref> |
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| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref> |
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[[Model organism]]s have been used in the study of HDAC1 function. A conditional [[knockout mouse]] line, called ''Hdac1<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Hdac1 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4431918 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the [[Wellcome Trust Sanger Institute]].<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = June 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = January 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref> |
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Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty five tests were carried out and two [[phenotypes]] were reported. A reduced number of [[homozygous]] [[mutant]] embryos were identified during gestation, and none survived until [[weaning]]. The remaining tests were carried out on [[heterozygous]] mutant adult mice, and no significant abnormalities were observed in these animals.<ref name="mgp_reference" /> |
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== Interactions == |
== Interactions == |
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HDAC1 has been shown to [[Protein-protein interaction|interact]] with: |
HDAC1 has been shown to [[Protein-protein interaction|interact]] with: |
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* [[Androgen receptor]],<ref name = pmid11994312>{{cite journal | vauthors = Gaughan L, Logan IR, Cook S, Neal DE, Robson CN | title = Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor | journal = |
* [[Androgen receptor]],<ref name = pmid11994312>{{cite journal | vauthors = Gaughan L, Logan IR, Cook S, Neal DE, Robson CN | title = Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor | journal = The Journal of Biological Chemistry | volume = 277 | issue = 29 | pages = 25904–13 | date = July 2002 | pmid = 11994312 | doi = 10.1074/jbc.M203423200 | doi-access = free }}</ref> |
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* [[BCL6]],<ref name = pmid9627120/><ref name = pmid10611298>{{cite journal | vauthors = Deltour S, Guerardel C, Leprince D | title = Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B | journal = |
* [[BCL6]],<ref name = pmid9627120/><ref name = pmid10611298>{{cite journal | vauthors = Deltour S, Guerardel C, Leprince D | title = Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a general mechanism for BTB/POZ transcriptional repressors: the case of HIC-1 and gammaFBP-B | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 26 | pages = 14831–6 | date = December 1999 | pmid = 10611298 | pmc = 24733 | doi = 10.1073/pnas.96.26.14831 | bibcode = 1999PNAS...9614831D | doi-access = free }}</ref> |
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* [[BTG2]],<ref name = "pmid17371797">{{cite journal | vauthors = Farioli-Vecchioli S, Tanori M, Micheli L, Mancuso M, Leonardi L, Saran A, Ciotti MT, Ferretti E, Gulino A, Pazzaglia S, Tirone F | title = Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3 | journal = FASEB |
* [[BTG2]],<ref name = "pmid17371797">{{cite journal | vauthors = Farioli-Vecchioli S, Tanori M, Micheli L, Mancuso M, Leonardi L, Saran A, Ciotti MT, Ferretti E, Gulino A, Pazzaglia S, Tirone F | title = Inhibition of medulloblastoma tumorigenesis by the antiproliferative and pro-differentiative gene PC3 | journal = FASEB Journal | volume = 21 | issue = 9 | pages = 2215–25 | date = July 2007 | pmid = 17371797 | doi = 10.1096/fj.06-7548com | s2cid = 4974360 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Micheli L, D'Andrea G, Leonardi L, Tirone F | title = HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression | journal = Journal of Cellular Physiology | volume = 232 | issue = 7 | pages = 1696–1707 | date = July 2017 | pmid = 27333946 | doi = 10.1002/jcp.25467 | s2cid = 4070837 | url = http://www.inmm.cnr.it/tirone/pdfs/Micheli_et_al-2017-J_Cell_Physiol%20PC3-HDACs.pdf }}</ref> |
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* [[BUB1B]],<ref name = pmid15388328/> |
* [[BUB1B]],<ref name = pmid15388328/> |
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* [[BUB1]],<ref name = pmid15388328/> |
* [[BUB1]],<ref name = pmid15388328/> |
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* [[BUB3]],<ref name = pmid15388328/> |
* [[BUB3]],<ref name = pmid15388328/> |
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* [[CBFA2T3]],<ref name = pmid12242670>{{cite journal | vauthors = Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N | title = The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies | journal = Oncogene | volume = 21 | issue = 43 | pages = 6703–12 | date = September 2002 | pmid = 12242670 | doi = 10.1038/sj.onc.1205882 }}</ref><ref name = pmid11533236>{{cite journal | vauthors = Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW | title = ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain | journal = |
* [[CBFA2T3]],<ref name = pmid12242670>{{cite journal | vauthors = Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N | title = The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies | journal = Oncogene | volume = 21 | issue = 43 | pages = 6703–12 | date = September 2002 | pmid = 12242670 | doi = 10.1038/sj.onc.1205882 | s2cid = 19634011 | doi-access = }}</ref><ref name = pmid11533236>{{cite journal | vauthors = Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW | title = ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain | journal = Molecular and Cellular Biology | volume = 21 | issue = 19 | pages = 6470–83 | date = October 2001 | pmid = 11533236 | pmc = 99794 | doi = 10.1128/mcb.21.19.6470-6483.2001 }}</ref> |
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* [[CDC20]],<ref name = pmid15388328>{{cite journal | vauthors = Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW | title = WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase | journal = FEBS |
* [[CDC20]],<ref name = pmid15388328>{{cite journal | vauthors = Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW | title = WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase | journal = FEBS Letters | volume = 575 | issue = 1–3 | pages = 23–9 | date = September 2004 | pmid = 15388328 | doi = 10.1016/j.febslet.2004.07.089 | s2cid = 21762011 | doi-access = free }}</ref> |
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* [[CDH1 (gene)|CDH1]],<ref name = pmid15388328/> |
* [[CDH1 (gene)|CDH1]],<ref name = pmid15388328/> |
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* [[CHD3]],<ref name = pmid9804427/><ref name = pmid11784859/> |
* [[CHD3]],<ref name = pmid9804427/><ref name = pmid11784859/> |
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* [[CHD4]],<ref name = pmid9804427/><ref name = pmid12920132/><ref name = pmid10220385/> |
* [[CHD4]],<ref name = pmid9804427/><ref name = pmid12920132/><ref name = pmid10220385/> |
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* [[COUP-TFII]],<ref name = pmid10704340>{{cite journal | vauthors = Smirnov DA, Hou S, Ricciardi RP | title = Association of histone deacetylase with COUP-TF in tumorigenic Ad12-transformed cells and its potential role in shut-off of MHC class I transcription | journal = Virology | volume = 268 | issue = 2 | pages = 319–28 | date = March 2000 | pmid = 10704340 | doi = 10.1006/viro.1999.0181 }}</ref> |
* [[COUP-TFII]],<ref name = pmid10704340>{{cite journal | vauthors = Smirnov DA, Hou S, Ricciardi RP | title = Association of histone deacetylase with COUP-TF in tumorigenic Ad12-transformed cells and its potential role in shut-off of MHC class I transcription | journal = Virology | volume = 268 | issue = 2 | pages = 319–28 | date = March 2000 | pmid = 10704340 | doi = 10.1006/viro.1999.0181 | doi-access = free }}</ref> |
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* [[CTBP1]],<ref name = pmid10995736/><ref name = pmid11022042>{{cite journal | vauthors = Zhang CL, McKinsey TA, Lu JR, Olson EN | title = Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor | journal = |
* [[CTBP1]],<ref name = pmid10995736/><ref name = pmid11022042>{{cite journal | vauthors = Zhang CL, McKinsey TA, Lu JR, Olson EN | title = Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor | journal = The Journal of Biological Chemistry | volume = 276 | issue = 1 | pages = 35–9 | date = January 2001 | pmid = 11022042 | doi = 10.1074/jbc.M007364200 | doi-access = free }}</ref><ref name = pmid9650586>{{cite journal | vauthors = Sundqvist A, Sollerbrant K, Svensson C | title = The carboxy-terminal region of adenovirus E1A activates transcription through targeting of a C-terminal binding protein-histone deacetylase complex | journal = FEBS Letters | volume = 429 | issue = 2 | pages = 183–8 | date = June 1998 | pmid = 9650586 | doi = 10.1016/s0014-5793(98)00588-2 | s2cid = 20660291 | doi-access = }}</ref> |
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* [[DDX17]],<ref name = pmid15298701/> |
* [[DDX17]],<ref name = pmid15298701/> |
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* [[DDX5]],<ref name = pmid15298701>{{cite journal | vauthors = Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV | title = The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner | journal = BMC |
* [[DDX5]],<ref name = pmid15298701>{{cite journal | vauthors = Wilson BJ, Bates GJ, Nicol SM, Gregory DJ, Perkins ND, Fuller-Pace FV | title = The p68 and p72 DEAD box RNA helicases interact with HDAC1 and repress transcription in a promoter-specific manner | journal = BMC Molecular Biology | volume = 5 | pages = 11 | date = August 2004 | pmid = 15298701 | pmc = 514542 | doi = 10.1186/1471-2199-5-11 | doi-access = free }}</ref> |
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* [[DNMT3A]],<ref name = pmid11350943>{{cite journal | vauthors = Fuks F, Burgers WA, Godin N, Kasai M, Kouzarides T | title = Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription | journal = EMBO |
* [[DNMT3A]],<ref name = pmid11350943>{{cite journal | vauthors = Fuks F, Burgers WA, Godin N, Kasai M, Kouzarides T | title = Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription | journal = The EMBO Journal | volume = 20 | issue = 10 | pages = 2536–44 | date = May 2001 | pmid = 11350943 | pmc = 125250 | doi = 10.1093/emboj/20.10.2536 }}</ref> |
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* [[DNMT3L]],<ref name = pmid12177302>{{cite journal | vauthors = Aapola U, Liiv I, Peterson P | title = Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity | journal = Nucleic Acids |
* [[DNMT3L]],<ref name = pmid12177302>{{cite journal | vauthors = Aapola U, Liiv I, Peterson P | title = Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity | journal = Nucleic Acids Research | volume = 30 | issue = 16 | pages = 3602–8 | date = August 2002 | pmid = 12177302 | pmc = 134241 | doi = 10.1093/nar/gkf474 }}</ref><ref name = pmid12202768>{{cite journal | vauthors = Deplus R, Brenner C, Burgers WA, Putmans P, Kouzarides T, de Launoit Y, Fuks F | title = Dnmt3L is a transcriptional repressor that recruits histone deacetylase | journal = Nucleic Acids Research | volume = 30 | issue = 17 | pages = 3831–8 | date = September 2002 | pmid = 12202768 | pmc = 137431 | doi = 10.1093/nar/gkf509 }}</ref> |
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* [[Death-associated protein 6]],<ref name = pmid10669754>{{cite journal | vauthors = Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD | title = Sequestration and inhibition of Daxx-mediated transcriptional repression by PML | journal = |
* [[Death-associated protein 6]],<ref name = pmid10669754>{{cite journal | vauthors = Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD | title = Sequestration and inhibition of Daxx-mediated transcriptional repression by PML | journal = Molecular and Cellular Biology | volume = 20 | issue = 5 | pages = 1784–96 | date = March 2000 | pmid = 10669754 | pmc = 85360 | doi = 10.1128/mcb.20.5.1784-1796.2000 }}</ref> |
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* [[EED (protein)|EED]],<ref name = pmid10581039/> |
* [[EED (protein)|EED]],<ref name = pmid10581039/> |
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* [[EVI1]],<ref name = pmid11552981>{{cite journal | vauthors = Vinatzer U, Taplick J, Seiser C, Fonatsch C, Wieser R | title = The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase | journal = |
* [[EVI1]],<ref name = pmid11552981>{{cite journal | vauthors = Vinatzer U, Taplick J, Seiser C, Fonatsch C, Wieser R | title = The leukaemia-associated transcription factors EVI-1 and MDS1/EVI1 repress transcription and interact with histone deacetylase | journal = British Journal of Haematology | volume = 114 | issue = 3 | pages = 566–73 | date = September 2001 | pmid = 11552981 | doi = 10.1046/j.1365-2141.2001.02987.x | s2cid = 7643309 | doi-access = }}</ref><ref name = pmid11568182>{{cite journal | vauthors = Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G | title = 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 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 48 | pages = 44936–43 | date = November 2001 | pmid = 11568182 | doi = 10.1074/jbc.M106733200 | doi-access = free }}</ref> |
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* [[EZH2]],<ref name = pmid10581039/> |
* [[EZH2]],<ref name = pmid10581039/> |
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* [[FKBP3]],<ref name = pmid11532945>{{cite journal | vauthors = Yang WM, Yao YL, Seto E | title = The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1 | journal = EMBO |
* [[FKBP3]],<ref name = pmid11532945>{{cite journal | vauthors = Yang WM, Yao YL, Seto E | title = The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1 | journal = The EMBO Journal | volume = 20 | issue = 17 | pages = 4814–25 | date = September 2001 | pmid = 11532945 | pmc = 125595 | doi = 10.1093/emboj/20.17.4814 }}</ref> |
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* [[GATA1]],<ref name = pmid14668799>{{cite journal | vauthors = Watamoto K, Towatari M, Ozawa Y, Miyata Y, Okamoto M, Abe A, Naoe T, Saito H | title = Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation | journal = Oncogene | volume = 22 | issue = 57 | pages = 9176–84 | date = December 2003 | pmid = 14668799 | doi = 10.1038/sj.onc.1206902 }}</ref> |
* [[GATA1]],<ref name = pmid14668799>{{cite journal | vauthors = Watamoto K, Towatari M, Ozawa Y, Miyata Y, Okamoto M, Abe A, Naoe T, Saito H | title = Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation | journal = Oncogene | volume = 22 | issue = 57 | pages = 9176–84 | date = December 2003 | pmid = 14668799 | doi = 10.1038/sj.onc.1206902 | s2cid = 24491249 | doi-access = }}</ref> |
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* [[HMG20B]],<ref name = pmid12032298/> |
* [[HMG20B]],<ref name = pmid12032298/> |
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* [[HSPA4]],<ref name = pmid11777905/> |
* [[HSPA4]],<ref name = pmid11777905/> |
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* [[HUS1]],<ref name = pmid10846170/> |
* [[HUS1]],<ref name = pmid10846170/> |
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* [[Histone deacetylase 2]],<ref name = pmid9804427>{{cite journal | vauthors = Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL | title = Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex | journal = Nature | volume = 395 | issue = 6705 | pages = 917–21 | date = October 1998 | pmid = 9804427 | doi = 10.1038/27699 }}</ref><ref name = pmid12920132/><ref name = pmid10581039>{{cite journal | vauthors = van der Vlag J, Otte AP | title = Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation | journal = |
* [[Histone deacetylase 2]],<ref name = pmid9804427>{{cite journal | vauthors = Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL | title = Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex | journal = Nature | volume = 395 | issue = 6705 | pages = 917–21 | date = October 1998 | pmid = 9804427 | doi = 10.1038/27699 | bibcode = 1998Natur.395..917T | s2cid = 4355885 }}</ref><ref name = pmid12920132/><ref name = pmid10581039>{{cite journal | vauthors = van der Vlag J, Otte AP | title = Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation | journal = Nature Genetics | volume = 23 | issue = 4 | pages = 474–8 | date = December 1999 | pmid = 10581039 | doi = 10.1038/70602 | s2cid = 6748531 }}</ref><ref name = pmid12032298>{{cite journal | vauthors = Hakimi MA, Bochar DA, Chenoweth J, Lane WS, Mandel G, Shiekhattar R | title = A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 11 | pages = 7420–5 | date = May 2002 | pmid = 12032298 | pmc = 124246 | doi = 10.1073/pnas.112008599 | bibcode = 2002PNAS...99.7420H | doi-access = free }}</ref><ref name = pmid11777905>{{cite journal | vauthors = Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM | title = 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 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 11 | pages = 9590–7 | date = March 2002 | pmid = 11777905 | doi = 10.1074/jbc.M107942200 | doi-access = free}}</ref><ref name = pmid11739383/><ref name = pmid12493763>{{cite journal | vauthors = Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R | title = A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes | journal = The Journal of Biological Chemistry | volume = 278 | issue = 9 | pages = 7234–9 | date = February 2003 | pmid = 12493763 | doi = 10.1074/jbc.M208992200 | doi-access = free}}</ref><ref name = pmid11804585>{{cite journal | vauthors = Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E | title = Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR | journal = Molecular Cell | volume = 9 | issue = 1 | pages = 45–57 | date = January 2002 | pmid = 11804585 | doi = 10.1016/s1097-2765(01)00429-4 | hdl = 11858/00-001M-0000-002C-9FF7-D | hdl-access = free }}</ref><ref name = pmid11466315>{{cite journal | vauthors = Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E | title = Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo | journal = The Journal of Biological Chemistry | volume = 276 | issue = 38 | pages = 35826–35 | date = September 2001 | pmid = 11466315 | doi = 10.1074/jbc.M104935200 | doi-access = free }}</ref><ref name = pmid11564889>{{cite journal | vauthors = Ashburner BP, Westerheide SD, Baldwin AS | title = The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression | journal = Molecular and Cellular Biology | volume = 21 | issue = 20 | pages = 7065–77 | date = October 2001 | pmid = 11564889 | pmc = 99882 | doi = 10.1128/MCB.21.20.7065-7077.2001 }}</ref><ref name = pmid10444591>{{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes & Development | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924 }}</ref><ref name = pmid9520398>{{cite journal | vauthors = Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL | title = A role for histone deacetylase activity in HDAC1-mediated transcriptional repression | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 7 | pages = 3519–24 | date = March 1998 | pmid = 9520398 | pmc = 19868 | doi = 10.1073/pnas.95.7.3519 | bibcode = 1998PNAS...95.3519H | doi-access = free }}</ref><ref name = pmid9150135>{{cite journal | vauthors = Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | date = May 1997 | pmid = 9150135 | doi = 10.1016/s0092-8674(00)80216-0 | doi-access = free }}</ref> |
||
* [[Homeobox protein TGIF1]],<ref name = pmid10995736>{{cite journal | vauthors = Melhuish TA, Wotton D | title = The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF | journal = |
* [[Homeobox protein TGIF1]],<ref name = pmid10995736>{{cite journal | vauthors = Melhuish TA, Wotton D | title = The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF | journal = The Journal of Biological Chemistry | volume = 275 | issue = 50 | pages = 39762–6 | date = December 2000 | pmid = 10995736 | doi = 10.1074/jbc.C000416200 | doi-access = free }}</ref><ref name = pmid11427533>{{cite journal | vauthors = Melhuish TA, Gallo CM, Wotton D | title = TGIF2 interacts with histone deacetylase 1 and represses transcription | journal = The Journal of Biological Chemistry | volume = 276 | issue = 34 | pages = 32109–14 | date = August 2001 | pmid = 11427533 | doi = 10.1074/jbc.M103377200 | doi-access = free }}</ref> |
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* [[Host cell factor C1]],<ref name = pmid12670868>{{cite journal | vauthors = Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W | title = Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 | journal = Genes |
* [[Host cell factor C1]],<ref name = pmid12670868>{{cite journal | vauthors = Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W | title = Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 | journal = Genes & Development | volume = 17 | issue = 7 | pages = 896–911 | date = April 2003 | pmid = 12670868 | pmc = 196026 | doi = 10.1101/gad.252103 }}</ref> |
||
* [[IFRD1]],<ref name = pmid12198164>{{cite journal | vauthors = Vietor I, Vadivelu SK, Wick N, Hoffman R, Cotten M, Seiser C, Fialka I, Wunderlich W, Haase A, Korinkova G, Brosch G, Huber LA | title = TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells | journal = EMBO |
* [[IFRD1]],<ref name = pmid12198164>{{cite journal | vauthors = Vietor I, Vadivelu SK, Wick N, Hoffman R, Cotten M, Seiser C, Fialka I, Wunderlich W, Haase A, Korinkova G, Brosch G, Huber LA | title = TIS7 interacts with the mammalian SIN3 histone deacetylase complex in epithelial cells | journal = The EMBO Journal | volume = 21 | issue = 17 | pages = 4621–31 | date = September 2002 | pmid = 12198164 | pmc = 125408 | doi = 10.1093/emboj/cdf461 }}</ref> |
||
* [[IKZF1]],<ref name = pmid10357820>{{cite journal | vauthors = Koipally J, Renold A, Kim J, Georgopoulos K | title = Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes | journal = EMBO |
* [[IKZF1]],<ref name = pmid10357820>{{cite journal | vauthors = Koipally J, Renold A, Kim J, Georgopoulos K | title = Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes | journal = The EMBO Journal | volume = 18 | issue = 11 | pages = 3090–100 | date = June 1999 | pmid = 10357820 | pmc = 1171390 | doi = 10.1093/emboj/18.11.3090 }}</ref><ref name = pmid12015313>{{cite journal | vauthors = Koipally J, Georgopoulos K | title = A molecular dissection of the repression circuitry of Ikaros | journal = The Journal of Biological Chemistry | volume = 277 | issue = 31 | pages = 27697–705 | date = August 2002 | pmid = 12015313 | doi = 10.1074/jbc.M201694200 | doi-access = free }}</ref> |
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* [[ING1]],<ref name = pmid11784859/><ref name = pmid12015309>{{cite journal | vauthors = Vieyra D, Loewith R, Scott M, Bonnefin P, Boisvert FM, Cheema P, Pastyryeva S, Meijer M, Johnston RN, Bazett-Jones DP, McMahon S, Cole MD, Young D, Riabowol K | title = Human ING1 proteins differentially regulate histone acetylation | journal = |
* [[ING1]],<ref name = pmid11784859/><ref name = pmid12015309>{{cite journal | vauthors = Vieyra D, Loewith R, Scott M, Bonnefin P, Boisvert FM, Cheema P, Pastyryeva S, Meijer M, Johnston RN, Bazett-Jones DP, McMahon S, Cole MD, Young D, Riabowol K | title = Human ING1 proteins differentially regulate histone acetylation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 33 | pages = 29832–9 | date = August 2002 | pmid = 12015309 | doi = 10.1074/jbc.M200197200 | doi-access = free }}</ref> |
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* [[MBD3]],<ref name = pmid10444591/><ref name = pmid12354758>{{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase | journal = |
* [[MBD3]],<ref name = pmid10444591/><ref name = pmid12354758>{{cite journal | vauthors = Sakai H, Urano T, Ookata K, Kim MH, Hirai Y, Saito M, Nojima Y, Ishikawa F | title = MBD3 and HDAC1, two components of the NuRD complex, are localized at Aurora-A-positive centrosomes in M phase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 50 | pages = 48714–23 | date = December 2002 | pmid = 12354758 | doi = 10.1074/jbc.M208461200 | doi-access = free }}</ref><ref name = pmid12124384>{{cite journal | vauthors = Saito M, Ishikawa F | title = The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35434–9 | date = September 2002 | pmid = 12124384 | doi = 10.1074/jbc.M203455200 | doi-access = free }}</ref> |
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* [[MIER1]],<ref name = pmid12482978>{{cite journal | vauthors = Ding Z, Gillespie LL, Paterno GD | title = Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain | journal = |
* [[MIER1]],<ref name = pmid12482978>{{cite journal | vauthors = Ding Z, Gillespie LL, Paterno GD | title = Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain | journal = Molecular and Cellular Biology | volume = 23 | issue = 1 | pages = 250–8 | date = January 2003 | pmid = 12482978 | pmc = 140656 | doi = 10.1128/mcb.23.1.250-258.2003 }}</ref> |
||
* [[MLL (gene)|MLL]],<ref name = pmid12829790>{{cite journal | vauthors = Xia ZB, Anderson M, Diaz MO, Zeleznik-Le NJ | title = MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein | journal = |
* [[MLL (gene)|MLL]],<ref name = pmid12829790>{{cite journal | vauthors = Xia ZB, Anderson M, Diaz MO, Zeleznik-Le NJ | title = MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 14 | pages = 8342–7 | date = July 2003 | pmid = 12829790 | pmc = 166231 | doi = 10.1073/pnas.1436338100 | bibcode = 2003PNAS..100.8342X | doi-access = free }}</ref> |
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* [[MTA1]],<ref name = pmid12920132>{{cite journal | vauthors = Yao YL, Yang WM | title = The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity | journal = |
* [[MTA1]],<ref name = pmid12920132>{{cite journal | vauthors = Yao YL, Yang WM | title = The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity | journal = The Journal of Biological Chemistry | volume = 278 | issue = 43 | pages = 42560–8 | date = October 2003 | pmid = 12920132 | doi = 10.1074/jbc.M302955200 | doi-access = free }}</ref><ref name = pmid11146623>{{cite journal | vauthors = Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R | title = Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor | journal = Nature Cell Biology | volume = 3 | issue = 1 | pages = 30–7 | date = January 2001 | pmid = 11146623 | doi = 10.1038/35050532 | s2cid = 23477845 }}</ref> |
||
* [[MTA2]],<ref name = pmid12920132/><ref name = pmid10444591/><ref name = pmid11171972/><ref name = pmid12374985/> |
* [[MTA2]],<ref name = pmid12920132/><ref name = pmid10444591/><ref name = pmid11171972/><ref name = pmid12374985/> |
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* [[Mad1]],<ref name = pmid15388328/> |
* [[Mad1]],<ref name = pmid15388328/> |
||
* [[Mdm2]],<ref name = pmid12426395>{{cite journal | vauthors = Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP | title = MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation | journal = EMBO |
* [[Mdm2]],<ref name = pmid12426395>{{cite journal | vauthors = Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP | title = MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation | journal = The EMBO Journal | volume = 21 | issue = 22 | pages = 6236–45 | date = November 2002 | pmid = 12426395 | pmc = 137207 | doi = 10.1093/emboj/cdf616 }}</ref> |
||
* [[Methyl-CpG-binding domain protein 2]],<ref name = pmid10444591/><ref name = pmid10471499/><ref name = pmid12183469>{{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3 | journal = |
* [[Methyl-CpG-binding domain protein 2]],<ref name = pmid10444591/><ref name = pmid10471499/><ref name = pmid12183469>{{cite journal | vauthors = Brackertz M, Boeke J, Zhang R, Renkawitz R | title = Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40958–66 | date = October 2002 | pmid = 12183469 | doi = 10.1074/jbc.M207467200 | doi-access = free }}</ref> |
||
* [[Mothers against decapentaplegic homolog 2]],<ref name = pmid10199400>{{cite journal | vauthors = Wotton D, Lo RS, Lee S, Massagué J | title = A Smad transcriptional corepressor | journal = Cell | volume = 97 | issue = 1 | pages = 29–39 | date = April 1999 | pmid = 10199400 | doi = |
* [[Mothers against decapentaplegic homolog 2]],<ref name = pmid10199400>{{cite journal | vauthors = Wotton D, Lo RS, Lee S, Massagué J | title = A Smad transcriptional corepressor | journal = Cell | volume = 97 | issue = 1 | pages = 29–39 | date = April 1999 | pmid = 10199400 | doi = 10.1016/s0092-8674(00)80712-6 | s2cid = 6907878 | doi-access = free }}</ref> |
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* [[MyoD]],<ref name = pmid11684023>{{cite journal | vauthors = Polesskaya A, Rudnicki MA | title = A MyoD-dependent differentiation checkpoint: ensuring genome integrity | journal = |
* [[MyoD]],<ref name = pmid11684023>{{cite journal | vauthors = Polesskaya A, Rudnicki MA | title = A MyoD-dependent differentiation checkpoint: ensuring genome integrity | journal = Developmental Cell | volume = 3 | issue = 6 | pages = 757–8 | date = December 2002 | pmid = 12479798 | doi = 10.1016/s1534-5807(02)00372-6 | doi-access = free }}</ref><ref name = pmid11285237>{{cite journal | vauthors = Mal A, Sturniolo M, Schiltz RL, Ghosh MK, Harter ML | title = A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program | journal = The EMBO Journal | volume = 20 | issue = 7 | pages = 1739–53 | date = April 2001 | pmid = 11285237 | pmc = 145490 | doi = 10.1093/emboj/20.7.1739 }}</ref> |
||
* [[NFKB1]],<ref name = pmid11931769/> |
* [[NFKB1]],<ref name = pmid11931769/> |
||
* [[Nuclear receptor co-repressor 2]],<ref name = pmid11739383>{{cite journal | vauthors = Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D | title = Isolation and characterization of a novel class II histone deacetylase, HDAC10 | journal = |
* [[Nuclear receptor co-repressor 2]],<ref name = pmid11739383>{{cite journal | vauthors = Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D | title = Isolation and characterization of a novel class II histone deacetylase, HDAC10 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 8 | pages = 6656–66 | date = February 2002 | pmid = 11739383 | doi = 10.1074/jbc.M108055200 | doi-access = free }}</ref><ref name = pmid11013263>{{cite journal | vauthors = Underhill C, Qutob MS, Yee SP, Torchia J | title = A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 51 | pages = 40463–70 | date = December 2000 | pmid = 11013263 | doi = 10.1074/jbc.M007864200 | doi-access = free }}</ref> |
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* [[P21]],<ref>{{cite journal |last1=Zupkovitz |first1=Gordin |last2=Lagger |first2=Sabine |last3=Martin |first3=David |last4=Steiner |first4=Marianne |last5=Hagelkruys |first5=Astrid |last6=Seiser |first6=Christian |last7=Schöfer |first7=Christian |last8=Pusch |first8=Oliver |title=Histone deacetylase 1 expression is inversely correlated with age in the short-lived fish Nothobranchius furzeri |journal=Histochemistry and Cell Biology |date=28 June 2018 |volume=150 |issue=3 |pages=255–269 |doi=10.1007/s00418-018-1687-4|pmc=6096771 |pmid=29951776}}</ref> |
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* [[PCNA]],<ref name = pmid11929879>{{cite journal | vauthors = Milutinovic S, Zhuang Q, Szyf M | title = Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification | journal = J. Biol. Chem. | volume = 277 | issue = 23 | pages = 20974–8 | date = June 2002 | pmid = 11929879 | doi = 10.1074/jbc.M202504200 }}</ref> |
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* [[ |
* [[PCNA]],<ref name = pmid11929879>{{cite journal | vauthors = Milutinovic S, Zhuang Q, Szyf M | title = Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20974–8 | date = June 2002 | pmid = 11929879 | doi = 10.1074/jbc.M202504200 | doi-access = free }}</ref> |
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* [[ |
* [[PHF21A]],<ref name = pmid12032298/><ref name = pmid15325272>{{cite journal | vauthors = Iwase S, Januma A, Miyamoto K, Shono N, Honda A, Yanagisawa J, Baba T | title = Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression | journal = Biochemical and Biophysical Research Communications | volume = 322 | issue = 2 | pages = 601–8 | date = September 2004 | pmid = 15325272 | doi = 10.1016/j.bbrc.2004.07.163 }}</ref> |
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* [[ |
* [[Prohibitin]],<ref name = pmid14637159>{{cite journal | vauthors = Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP | title = A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis | journal = Biochemical and Biophysical Research Communications | volume = 312 | issue = 2 | pages = 459–66 | date = December 2003 | pmid = 14637159 | doi = 10.1016/j.bbrc.2003.10.148 }}</ref><ref name = pmid12466959>{{cite journal | vauthors = Wang S, Fusaro G, Padmanabhan J, Chellappan SP | title = Prohibitin co-localizes with Rb in the nucleus and recruits N-CoR and HDAC1 for transcriptional repression | journal = Oncogene | volume = 21 | issue = 55 | pages = 8388–96 | date = December 2002 | pmid = 12466959 | doi = 10.1038/sj.onc.1205944 | s2cid = 22880111 | doi-access = }}</ref> |
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* [[Promyelocytic leukemia protein]],<ref name = pmid11430826>{{cite journal | vauthors = Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S | title = Role of PML and PML-RARalpha in Mad-mediated transcriptional repression | journal = Molecular Cell | volume = 7 | issue = 6 | pages = 1233–43 | date = June 2001 | pmid = 11430826 | doi = 10.1016/s1097-2765(01)00257-x | doi-access = free }}</ref><ref name = pmid11259576>{{cite journal | vauthors = Wu WS, Vallian S, Seto E, Yang WM, Edmondson D, Roth S, Chang KS | title = The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases | journal = Molecular and Cellular Biology | volume = 21 | issue = 7 | pages = 2259–68 | date = April 2001 | pmid = 11259576 | pmc = 86860 | doi = 10.1128/MCB.21.7.2259-2268.2001 }}</ref> |
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* [[RAD9A]],<ref name = pmid10846170>{{cite journal | vauthors = Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D | title = HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins | journal = J. Biol. Chem. | volume = 275 | issue = 36 | pages = 27909–16 | date = September 2000 | pmid = 10846170 | doi = 10.1074/jbc.M000168200 }}</ref> |
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* [[RBBP4]],<ref name = pmid12920132/><ref name = pmid10220385/><ref name = pmid10444591/><ref name = pmid9520398/><ref name = pmid9150135/><ref name = pmid11171972/><ref name = pmid10471499/><ref name = pmid12943729/><ref name = pmid12091390/><ref name = pmid11470869>{{cite journal | vauthors = Nicolas E, Ait-Si-Ali S, Trouche D | title = The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein | journal = Nucleic Acids |
* [[RAD9A]],<ref name = pmid10846170>{{cite journal | vauthors = Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D | title = HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins | journal = The Journal of Biological Chemistry | volume = 275 | issue = 36 | pages = 27909–16 | date = September 2000 | pmid = 10846170 | doi = 10.1074/jbc.M000168200 | doi-access = free }}</ref> |
||
* [[RBBP4]],<ref name = pmid12920132/><ref name = pmid10220385/><ref name = pmid10444591/><ref name = pmid9520398/><ref name = pmid9150135/><ref name = pmid11171972/><ref name = pmid10471499/><ref name = pmid12943729/><ref name = pmid12091390/><ref name = pmid11470869>{{cite journal | vauthors = Nicolas E, Ait-Si-Ali S, Trouche D | title = The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein | journal = Nucleic Acids Research | volume = 29 | issue = 15 | pages = 3131–6 | date = August 2001 | pmid = 11470869 | pmc = 55834 | doi = 10.1093/nar/29.15.3131 }}</ref><ref name = pmid9150133>{{cite journal | vauthors = Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE | title = Histone deacetylase activity is required for full transcriptional repression by mSin3A | journal = Cell | volume = 89 | issue = 3 | pages = 341–7 | date = May 1997 | pmid = 9150133 | doi = 10.1016/s0092-8674(00)80214-7 | s2cid = 14233219 | doi-access = free }}</ref> |
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* [[RBBP7]],<ref name = pmid12920132/><ref name = pmid10444591/><ref name = pmid9150135/><ref name = pmid10471499>{{cite journal | vauthors = Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A | title = MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex | journal = |
* [[RBBP7]],<ref name = pmid12920132/><ref name = pmid10444591/><ref name = pmid9150135/><ref name = pmid10471499>{{cite journal | vauthors = Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A | title = MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex | journal = Nature Genetics | volume = 23 | issue = 1 | pages = 58–61 | date = September 1999 | pmid = 10471499 | doi = 10.1038/12659 | hdl = 1842/684 | s2cid = 6147725 | hdl-access = free }}</ref> |
||
* [[RCOR1]],<ref name = pmid12032298/><ref name = pmid11171972/> |
* [[RCOR1]],<ref name = pmid12032298/><ref name = pmid11171972/> |
||
* [[RELA]],<ref name = pmid11564889/><ref name = pmid11931769>{{cite journal | vauthors = Zhong H, May MJ, Jimi E, Ghosh S | title = The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1 | journal = |
* [[RELA]],<ref name = pmid11564889/><ref name = pmid11931769>{{cite journal | vauthors = Zhong H, May MJ, Jimi E, Ghosh S | title = The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1 | journal = Molecular Cell | volume = 9 | issue = 3 | pages = 625–36 | date = March 2002 | pmid = 11931769 | doi = 10.1016/s1097-2765(02)00477-x | doi-access = free }}</ref><ref name = pmid12419806>{{cite journal | vauthors = Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M | title = Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 4 | pages = 2758–66 | date = January 2003 | pmid = 12419806 | doi = 10.1074/jbc.M209572200 | doi-access = free }}</ref> |
||
* [[RFC1]],<ref name = pmid12045192>{{cite journal | vauthors = Anderson LA, Perkins ND | title = The large subunit of replication factor C interacts with the histone deacetylase, HDAC1 | journal = |
* [[RFC1]],<ref name = pmid12045192>{{cite journal | vauthors = Anderson LA, Perkins ND | title = The large subunit of replication factor C interacts with the histone deacetylase, HDAC1 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 33 | pages = 29550–4 | date = August 2002 | pmid = 12045192 | doi = 10.1074/jbc.M200513200 | doi-access = free }}</ref> |
||
* [[Retinoblastoma protein]],<ref name = pmid11684023/><ref name = pmid12466959/><ref name = pmid9724731/><ref name = pmid10490602/><ref name = pmid10779361>{{cite journal | vauthors = Dick FA, Sailhamer E, Dyson NJ | title = Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins | journal = |
* [[Retinoblastoma protein]],<ref name = pmid11684023/><ref name = pmid12466959/><ref name = pmid9724731/><ref name = pmid10490602/><ref name = pmid10779361>{{cite journal | vauthors = Dick FA, Sailhamer E, Dyson NJ | title = Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins | journal = Molecular and Cellular Biology | volume = 20 | issue = 10 | pages = 3715–27 | date = May 2000 | pmid = 10779361 | pmc = 85672 | doi = 10.1128/mcb.20.10.3715-3727.2000 }}</ref><ref name = pmid10615135>{{cite journal | vauthors = Fuks F, Burgers WA, Brehm A, Hughes-Davies L, Kouzarides T | title = DNA methyltransferase Dnmt1 associates with histone deacetylase activity | journal = Nature Genetics | volume = 24 | issue = 1 | pages = 88–91 | date = January 2000 | pmid = 10615135 | doi = 10.1038/71750 | s2cid = 20428600 }}</ref><ref name = pmid9491888>{{cite journal | vauthors = Luo RX, Postigo AA, Dean DC | title = Rb interacts with histone deacetylase to repress transcription | journal = Cell | volume = 92 | issue = 4 | pages = 463–73 | date = February 1998 | pmid = 9491888 | doi = 10.1016/s0092-8674(00)80940-x | s2cid = 18857544 | doi-access = free }}</ref> |
||
* [[Retinoblastoma-like protein 1]],<ref name = pmid9724731/><ref name = pmid10490602>{{cite journal | vauthors = Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE | title = RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins | journal = |
* [[Retinoblastoma-like protein 1]],<ref name = pmid9724731/><ref name = pmid10490602>{{cite journal | vauthors = Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE | title = RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins | journal = Molecular and Cellular Biology | volume = 19 | issue = 10 | pages = 6632–41 | date = October 1999 | pmid = 10490602 | pmc = 84642 | doi = 10.1128/mcb.19.10.6632 }}</ref> |
||
* [[Retinoblastoma-like protein 2]],<ref name = pmid9724731>{{cite journal | vauthors = Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D | title = The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase | journal = |
* [[Retinoblastoma-like protein 2]],<ref name = pmid9724731>{{cite journal | vauthors = Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D | title = The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 18 | pages = 10493–8 | date = September 1998 | pmid = 9724731 | pmc = 27922 | doi = 10.1073/pnas.95.18.10493 | bibcode = 1998PNAS...9510493F | doi-access = free }}</ref><ref name = pmid10969803>{{cite journal | vauthors = Bouzahzah B, Fu M, Iavarone A, Factor VM, Thorgeirsson SS, Pestell RG | title = Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo | journal = Cancer Research | volume = 60 | issue = 16 | pages = 4531–7 | date = August 2000 | pmid = 10969803 }}</ref> |
||
* [[SAP30]],<ref name = pmid11784859/><ref name = pmid10444591/><ref name = pmid12788099>{{cite journal | vauthors = Huang NE, Lin CH, Lin YS, Yu WC | title = Modulation of YY1 activity by SAP30 | journal = |
* [[SAP30]],<ref name = pmid11784859/><ref name = pmid10444591/><ref name = pmid12788099>{{cite journal | vauthors = Huang NE, Lin CH, Lin YS, Yu WC | title = Modulation of YY1 activity by SAP30 | journal = Biochemical and Biophysical Research Communications | volume = 306 | issue = 1 | pages = 267–75 | date = June 2003 | pmid = 12788099 | doi = 10.1016/S0006-291X(03)00966-5 }}</ref><ref name = pmid9651585>{{cite journal | vauthors = Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D | title = SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex | journal = Molecular Cell | volume = 1 | issue = 7 | pages = 1021–31 | date = June 1998 | pmid = 9651585 | doi = 10.1016/s1097-2765(00)80102-1 | doi-access = free }}</ref><ref name = pmid15235594>{{cite journal | vauthors = Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I | title = HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations | journal = Nature Structural & Molecular Biology | volume = 11 | issue = 8 | pages = 738–46 | date = August 2004 | pmid = 15235594 | doi = 10.1038/nsmb798 | s2cid = 44324333 }}</ref><ref name = pmid11390640>{{cite journal | vauthors = Yochum GS, Ayer DE | title = Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex | journal = Molecular and Cellular Biology | volume = 21 | issue = 13 | pages = 4110–8 | date = July 2001 | pmid = 11390640 | pmc = 87072 | doi = 10.1128/MCB.21.13.4110-4118.2001 }}</ref> |
||
* [[SATB1]],<ref name = pmid12374985/> |
* [[SATB1]],<ref name = pmid12374985/> |
||
* [[SIN3A]],<ref name = pmid9804427/><ref name = pmid11784859>{{cite journal | vauthors = Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D | title = Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1) | journal = |
* [[SIN3A]],<ref name = pmid9804427/><ref name = pmid11784859>{{cite journal | vauthors = Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D | title = Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1) | journal = Molecular and Cellular Biology | volume = 22 | issue = 3 | pages = 835–48 | date = February 2002 | pmid = 11784859 | pmc = 133546 | doi = 10.1128/mcb.22.3.835-848.2002 }}</ref><ref name = pmid12920132/><ref name = pmid10220385>{{cite journal | vauthors = Grozinger CM, Hassig CA, Schreiber SL | title = Three proteins define a class of human histone deacetylases related to yeast Hda1p | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 9 | pages = 4868–73 | date = April 1999 | pmid = 10220385 | pmc = 21783 | doi = 10.1073/pnas.96.9.4868 | bibcode = 1999PNAS...96.4868G | doi-access = free }}</ref><ref name = pmid10444591/><ref name = pmid9520398/><ref name = pmid11171972>{{cite journal | vauthors = You A, Tong JK, Grozinger CM, Schreiber SL | title = CoREST is an integral component of the CoREST- human histone deacetylase complex | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 4 | pages = 1454–8 | date = February 2001 | pmid = 11171972 | pmc = 29278 | doi = 10.1073/pnas.98.4.1454 | bibcode = 2001PNAS...98.1454Y | doi-access = free }}</ref><ref name = pmid12374985>{{cite journal | vauthors = Yasui D, Miyano M, Cai S, Varga-Weisz P, Kohwi-Shigematsu T | title = SATB1 targets chromatin remodelling to regulate genes over long distances | journal = Nature | volume = 419 | issue = 6907 | pages = 641–5 | date = October 2002 | pmid = 12374985 | doi = 10.1038/nature01084 | bibcode = 2002Natur.419..641Y | s2cid = 25822700 | url = https://digital.library.unt.edu/ark:/67531/metadc733622/ }}</ref><ref name = pmid12943729>{{cite journal | vauthors = Zhang Y, Dufau ML | title = Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 85 | issue = 2–5 | pages = 401–14 | date = June 2003 | pmid = 12943729 | doi = 10.1016/s0960-0760(03)00230-9 | s2cid = 28512341 | url = https://zenodo.org/record/1260176 }}</ref><ref name = pmid12091390>{{cite journal | vauthors = Zhang Y, Dufau ML | title = Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex | journal = The Journal of Biological Chemistry | volume = 277 | issue = 36 | pages = 33431–8 | date = September 2002 | pmid = 12091390 | doi = 10.1074/jbc.M204417200 | doi-access = free }}</ref><ref name = pmid12724404>{{cite journal | vauthors = Fleischer TC, Yun UJ, Ayer DE | title = Identification and characterization of three new components of the mSin3A corepressor complex | journal = Molecular and Cellular Biology | volume = 23 | issue = 10 | pages = 3456–67 | date = May 2003 | pmid = 12724404 | pmc = 164750 | doi = 10.1128/mcb.23.10.3456-3467.2003 }}</ref><ref name = pmid12398767>{{cite journal | vauthors = Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA | title = An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B | journal = The Biochemical Journal | volume = 369 | issue = Pt 3 | pages = 651–7 | date = February 2003 | pmid = 12398767 | pmc = 1223118 | doi = 10.1042/BJ20020854 }}</ref><ref name = pmid11931768>{{cite journal | vauthors = Zhang J, Kalkum M, Chait BT, Roeder RG | title = The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2 | journal = Molecular Cell | volume = 9 | issue = 3 | pages = 611–23 | date = March 2002 | pmid = 11931768 | doi = 10.1016/s1097-2765(02)00468-9 | doi-access = free }}</ref><ref name = pmid10640275>{{cite journal | vauthors = Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA | title = Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway | journal = Genes & Development | volume = 14 | issue = 1 | pages = 45–54 | date = January 2000 | doi = 10.1101/gad.14.1.45 | pmid = 10640275 | pmc = 316335 }}</ref> |
||
* [[SIN3B]],<ref name = pmid10444591/><ref name = pmid10357820/> |
* [[SIN3B]],<ref name = pmid10444591/><ref name = pmid10357820/> |
||
* [[SPEN]],<ref name = pmid11331609>{{cite journal | vauthors = Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM | title = Sharp, an inducible cofactor that integrates nuclear receptor repression and activation | journal = Genes |
* [[SPEN]],<ref name = pmid11331609>{{cite journal | vauthors = Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM | title = Sharp, an inducible cofactor that integrates nuclear receptor repression and activation | journal = Genes & Development | volume = 15 | issue = 9 | pages = 1140–51 | date = May 2001 | pmid = 11331609 | pmc = 312688 | doi = 10.1101/gad.871201 }}</ref> |
||
* [[SUDS3]],<ref name = pmid12724404/><ref name = pmid11909966>{{cite journal | vauthors = Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA | title = Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex | journal = |
* [[SUDS3]],<ref name = pmid12724404/><ref name = pmid11909966>{{cite journal | vauthors = Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA | title = Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex | journal = Molecular and Cellular Biology | volume = 22 | issue = 8 | pages = 2743–50 | date = April 2002 | pmid = 11909966 | pmc = 133736 | doi = 10.1128/mcb.22.8.2743-2750.2002 }}</ref> |
||
* [[SUV39H1]],<ref name = pmid11788710>{{cite journal | vauthors = Vaute O, Nicolas E, Vandel L, Trouche D | title = Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases | journal = Nucleic Acids |
* [[SUV39H1]],<ref name = pmid11788710>{{cite journal | vauthors = Vaute O, Nicolas E, Vandel L, Trouche D | title = Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases | journal = Nucleic Acids Research | volume = 30 | issue = 2 | pages = 475–81 | date = January 2002 | pmid = 11788710 | pmc = 99834 | doi = 10.1093/nar/30.2.475 }}</ref> |
||
* [[Sp1 transcription factor]],<ref name = pmid12091390/><ref name = pmid12847090>{{cite journal | vauthors = Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M | title = Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter | journal = |
* [[Sp1 transcription factor]],<ref name = pmid12091390/><ref name = pmid12847090>{{cite journal | vauthors = Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M | title = Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter | journal = The Journal of Biological Chemistry | volume = 278 | issue = 38 | pages = 36496–504 | date = September 2003 | pmid = 12847090 | doi = 10.1074/jbc.M306694200 | doi-access = free }}</ref><ref name = pmid11896613>{{cite journal | vauthors = Singh J, Murata K, Itahana Y, Desprez PY | title = Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex | journal = Oncogene | volume = 21 | issue = 12 | pages = 1812–22 | date = March 2002 | pmid = 11896613 | doi = 10.1038/sj.onc.1205252 | s2cid = 30129174 | doi-access = }}</ref><ref name = pmid12176973>{{cite journal | vauthors = Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR | title = The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 39 | pages = 35783–6 | date = September 2002 | pmid = 12176973 | doi = 10.1074/jbc.C200378200 | doi-access = free }}</ref> |
||
* [[TOP2A]],<ref name = pmid11062478/><ref name = pmid11136718/> |
* [[TOP2A]],<ref name = pmid11062478/><ref name = pmid11136718/> |
||
* [[TOP2B]],<ref name = pmid11062478>{{cite journal | vauthors = Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E | title = Histone deacetylase interacts directly with DNA topoisomerase II | journal = |
* [[TOP2B]],<ref name = pmid11062478>{{cite journal | vauthors = Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E | title = Histone deacetylase interacts directly with DNA topoisomerase II | journal = Nature Genetics | volume = 26 | issue = 3 | pages = 349–53 | date = November 2000 | pmid = 11062478 | doi = 10.1038/81671 | s2cid = 19301396 }}</ref><ref name = pmid11136718>{{cite journal | vauthors = Johnson CA, Padget K, Austin CA, Turner BM | title = Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis | journal = The Journal of Biological Chemistry | volume = 276 | issue = 7 | pages = 4539–42 | date = February 2001 | pmid = 11136718 | doi = 10.1074/jbc.C000824200 | doi-access = free }}</ref> and |
||
* [[Zinc finger and BTB domain-containing protein 16]].<ref name = pmid9627120>{{cite journal | vauthors = David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A | title = Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein | journal = Oncogene | volume = 16 | issue = 19 | pages = 2549–56 | date = May 1998 | pmid = 9627120 | doi = 10.1038/sj.onc.1202043 }}</ref><ref name = pmid15467736>{{cite journal | vauthors = Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A | title = HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF | journal = Oncogene | volume = 23 | issue = 54 | pages = 8777–84 | date = November 2004 | pmid = 15467736 | doi = 10.1038/sj.onc.1208128 }}</ref><ref name = pmid9765306>{{cite journal | vauthors = Wong CW, Privalsky ML | title = Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6 | journal = |
* [[Zinc finger and BTB domain-containing protein 16]].<ref name = pmid9627120>{{cite journal | vauthors = David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A | title = Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein | journal = Oncogene | volume = 16 | issue = 19 | pages = 2549–56 | date = May 1998 | pmid = 9627120 | doi = 10.1038/sj.onc.1202043 | s2cid = 655636 | doi-access = }}</ref><ref name = pmid15467736>{{cite journal | vauthors = Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A | title = HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF | journal = Oncogene | volume = 23 | issue = 54 | pages = 8777–84 | date = November 2004 | pmid = 15467736 | doi = 10.1038/sj.onc.1208128 | s2cid = 26092755 | doi-access = }}</ref><ref name = pmid9765306>{{cite journal | vauthors = Wong CW, Privalsky ML | title = Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 42 | pages = 27695–702 | date = October 1998 | pmid = 9765306 | doi = 10.1074/jbc.273.42.27695 | doi-access = free }}</ref> |
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{{Div col end}} |
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== References == |
== References == |
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{{reflist| |
{{reflist|33em}} |
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== Further reading == |
== Further reading == |
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{{refbegin |
{{refbegin|33em}} |
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*{{cite journal | vauthors = Wolffe AP | title = Histone deacetylase: a regulator of transcription | journal = Science | volume = 272 | issue = 5260 | pages = 371–2 | |
* {{cite journal | vauthors = Wolffe AP | title = Histone deacetylase: a regulator of transcription | journal = Science | volume = 272 | issue = 5260 | pages = 371–2 | date = April 1996 | pmid = 8602525 | doi = 10.1126/science.272.5260.371 | bibcode = 1996Sci...272..371W | s2cid = 27257723 | url = https://zenodo.org/record/1231070 }} |
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*{{cite journal | vauthors = Ahringer J | title = NuRD and SIN3 histone deacetylase complexes in development | journal = Trends |
* {{cite journal | vauthors = Ahringer J | title = NuRD and SIN3 histone deacetylase complexes in development | journal = Trends in Genetics | volume = 16 | issue = 8 | pages = 351–6 | date = August 2000 | pmid = 10904264 | doi = 10.1016/S0168-9525(00)02066-7 }} |
||
*{{cite journal | vauthors = Verdin E, Dequiedt F, Kasler HG | title = Class II histone deacetylases: versatile regulators | journal = Trends |
* {{cite journal | vauthors = Verdin E, Dequiedt F, Kasler HG | title = Class II histone deacetylases: versatile regulators | journal = Trends in Genetics | volume = 19 | issue = 5 | pages = 286–93 | date = May 2003 | pmid = 12711221 | doi = 10.1016/S0168-9525(03)00073-8 | hdl = 2268/80861 | hdl-access = free }} |
||
*{{cite journal | vauthors = Zhang Y, Dufau ML | title = Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes | journal = |
* {{cite journal | vauthors = Zhang Y, Dufau ML | title = Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 85 | issue = 2–5 | pages = 401–14 | date = June 2003 | pmid = 12943729 | doi = 10.1016/S0960-0760(03)00230-9 | s2cid = 28512341 | url = https://zenodo.org/record/1260176 }} |
||
*{{cite journal | vauthors = Stevens M, De Clercq E, Balzarini J | title = The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention | journal = |
* {{cite journal | vauthors = Stevens M, De Clercq E, Balzarini J | title = The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention | journal = Medicinal Research Reviews | volume = 26 | issue = 5 | pages = 595–625 | date = September 2006 | pmid = 16838299 | doi = 10.1002/med.20081 | pmc = 7168390 }} |
||
*{{cite journal | vauthors = Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R | title = E2F-5, a new E2F family member that interacts with p130 in vivo | journal = |
* {{cite journal | vauthors = Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R | title = E2F-5, a new E2F family member that interacts with p130 in vivo | journal = Molecular and Cellular Biology | volume = 15 | issue = 6 | pages = 3082–9 | date = June 1995 | pmid = 7760804 | pmc = 230539 | doi = 10.1128/mcb.15.6.3082 }} |
||
*{{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | |
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }} |
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*{{cite journal | vauthors = Margolis DM, Somasundaran M, Green MR | title = Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production | journal = |
* {{cite journal | vauthors = Margolis DM, Somasundaran M, Green MR | title = Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production | journal = Journal of Virology | volume = 68 | issue = 2 | pages = 905–10 | date = February 1994 | doi = 10.1128/JVI.68.2.905-910.1994 | pmid = 8289393 | pmc = 236527 }} |
||
*{{cite journal | vauthors = Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y | title = Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae | journal = |
* {{cite journal | vauthors = Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y | title = Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae | journal = Cytogenetics and Cell Genetics | volume = 73 | issue = 1–2 | pages = 130–3 | year = 1996 | pmid = 8646880 | doi = 10.1159/000134323 }} |
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*{{cite journal | vauthors = Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE | title = Histone deacetylase activity is required for full transcriptional repression by mSin3A | journal = Cell | volume = 89 | issue = 3 | pages = 341–7 | |
* {{cite journal | vauthors = Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE | title = Histone deacetylase activity is required for full transcriptional repression by mSin3A | journal = Cell | volume = 89 | issue = 3 | pages = 341–7 | date = May 1997 | pmid = 9150133 | doi = 10.1016/S0092-8674(00)80214-7 | s2cid = 14233219 | doi-access = free }} |
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*{{cite journal | vauthors = Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN | title = Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression | journal = Cell | volume = 89 | issue = 3 | pages = 349–56 | |
* {{cite journal | vauthors = Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN | title = Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression | journal = Cell | volume = 89 | issue = 3 | pages = 349–56 | date = May 1997 | pmid = 9150134 | doi = 10.1016/S0092-8674(00)80215-9 | s2cid = 13490886 | doi-access = free }} |
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*{{cite journal | vauthors = Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | |
* {{cite journal | vauthors = Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | date = May 1997 | pmid = 9150135 | doi = 10.1016/S0092-8674(00)80216-0 | doi-access = free }} |
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*{{cite journal | vauthors = Romerio F, Gabriel MN, Margolis DM | title = Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF | journal = |
* {{cite journal | vauthors = Romerio F, Gabriel MN, Margolis DM | title = Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF | journal = Journal of Virology | volume = 71 | issue = 12 | pages = 9375–82 | date = December 1997 | doi = 10.1128/JVI.71.12.9375-9382.1997 | pmid = 9371597 | pmc = 230241 }} |
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*{{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | |
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }} |
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*{{cite journal | vauthors = Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T | title = Retinoblastoma protein recruits histone deacetylase to repress transcription | journal = Nature | volume = 391 | issue = 6667 | pages = 597–601 | |
* {{cite journal | vauthors = Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T | title = Retinoblastoma protein recruits histone deacetylase to repress transcription | journal = Nature | volume = 391 | issue = 6667 | pages = 597–601 | date = February 1998 | pmid = 9468139 | doi = 10.1038/35404 | bibcode = 1998Natur.391..597B | s2cid = 4326464 }} |
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*{{cite journal | vauthors = Magnaghi-Jaulin L, Groisman R, Naguibneva I, Robin P, Lorain S, Le Villain JP, Troalen F, Trouche D, Harel-Bellan A | title = Retinoblastoma protein represses transcription by recruiting a histone deacetylase | journal = Nature | volume = 391 | issue = 6667 | pages = 601–5 | |
* {{cite journal | vauthors = Magnaghi-Jaulin L, Groisman R, Naguibneva I, Robin P, Lorain S, Le Villain JP, Troalen F, Trouche D, Harel-Bellan A | title = Retinoblastoma protein represses transcription by recruiting a histone deacetylase | journal = Nature | volume = 391 | issue = 6667 | pages = 601–5 | date = February 1998 | pmid = 9468140 | doi = 10.1038/35410 | bibcode = 1998Natur.391..601M | s2cid = 4315457 }} |
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*{{cite journal | vauthors = Lin RJ, Nagy L, Inoue S, Shao W, Miller WH, Evans RM | title = Role of the histone deacetylase complex in acute promyelocytic leukaemia | journal = Nature | volume = 391 | issue = 6669 | pages = 811–4 | |
* {{cite journal | vauthors = Lin RJ, Nagy L, Inoue S, Shao W, Miller WH, Evans RM | title = Role of the histone deacetylase complex in acute promyelocytic leukaemia | journal = Nature | volume = 391 | issue = 6669 | pages = 811–4 | date = February 1998 | pmid = 9486654 | doi = 10.1038/35895 | bibcode = 1998Natur.391..811L | s2cid = 4383951 | doi-access = free }} |
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*{{cite journal | vauthors = Luo RX, Postigo AA, Dean DC | title = Rb interacts with histone deacetylase to repress transcription | journal = Cell | volume = 92 | issue = 4 | pages = 463–73 | |
* {{cite journal | vauthors = Luo RX, Postigo AA, Dean DC | title = Rb interacts with histone deacetylase to repress transcription | journal = Cell | volume = 92 | issue = 4 | pages = 463–73 | date = February 1998 | pmid = 9491888 | doi = 10.1016/S0092-8674(00)80940-X | s2cid = 18857544 | doi-access = free }} |
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Latest revision as of 01:27, 4 January 2024
Histone deacetylase 1 (HDAC1) is an enzyme that in humans is encoded by the HDAC1 gene.[5]
Function
[edit]Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2 MTA2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.[6]
Interactions
[edit]HDAC1 has been shown to interact with:
- Androgen receptor,[7]
- BCL6,[8][9]
- BTG2,[10][11]
- BUB1B,[12]
- BUB1,[12]
- BUB3,[12]
- CBFA2T3,[13][14]
- CDC20,[12]
- CDH1,[12]
- CHD3,[15][16]
- CHD4,[15][17][18]
- COUP-TFII,[19]
- CTBP1,[20][21][22]
- DDX17,[23]
- DDX5,[23]
- DNMT3A,[24]
- DNMT3L,[25][26]
- Death-associated protein 6,[27]
- EED,[28]
- EVI1,[29][30]
- EZH2,[28]
- FKBP3,[31]
- GATA1,[32]
- HMG20B,[33]
- HSPA4,[34]
- HUS1,[35]
- Histone deacetylase 2,[15][17][28][33][34][36][37][38][39][40][41][42][43]
- Homeobox protein TGIF1,[20][44]
- Host cell factor C1,[45]
- IFRD1,[46]
- IKZF1,[47][48]
- ING1,[16][49]
- MBD3,[41][50][51]
- MIER1,[52]
- MLL,[53]
- MTA1,[17][54]
- MTA2,[17][41][55][56]
- Mad1,[12]
- Mdm2,[57]
- Methyl-CpG-binding domain protein 2,[41][58][59]
- Mothers against decapentaplegic homolog 2,[60]
- MyoD,[61][62]
- NFKB1,[63]
- Nuclear receptor co-repressor 2,[36][64]
- P21,[65]
- PCNA,[66]
- PHF21A,[33][67]
- Prohibitin,[68][69]
- Promyelocytic leukemia protein,[70][71]
- RAD9A,[35]
- RBBP4,[17][18][41][42][43][55][58][72][73][74][75]
- RBBP7,[17][41][43][58]
- RCOR1,[33][55]
- RELA,[40][63][76]
- RFC1,[77]
- Retinoblastoma protein,[61][69][78][79][80][81][82]
- Retinoblastoma-like protein 1,[78][79]
- Retinoblastoma-like protein 2,[78][83]
- SAP30,[16][41][84][85][86][87]
- SATB1,[56]
- SIN3A,[15][16][17][18][41][42][55][56][72][73][88][89][90][91]
- SIN3B,[41][47]
- SPEN,[92]
- SUDS3,[88][93]
- SUV39H1,[94]
- Sp1 transcription factor,[73][95][96][97]
- TOP2A,[98][99]
- TOP2B,[98][99] and
- Zinc finger and BTB domain-containing protein 16.[8][100][101]
See also
[edit]References
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Further reading
[edit]- Wolffe AP (April 1996). "Histone deacetylase: a regulator of transcription". Science. 272 (5260): 371–2. Bibcode:1996Sci...272..371W. doi:10.1126/science.272.5260.371. PMID 8602525. S2CID 27257723.
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- Verdin E, Dequiedt F, Kasler HG (May 2003). "Class II histone deacetylases: versatile regulators". Trends in Genetics. 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. hdl:2268/80861. PMID 12711221.
- Zhang Y, Dufau ML (June 2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 401–14. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729. S2CID 28512341.
- Stevens M, De Clercq E, Balzarini J (September 2006). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention". Medicinal Research Reviews. 26 (5): 595–625. doi:10.1002/med.20081. PMC 7168390. PMID 16838299.
- Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (June 1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Molecular and Cellular Biology. 15 (6): 3082–9. doi:10.1128/mcb.15.6.3082. PMC 230539. PMID 7760804.
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- Margolis DM, Somasundaran M, Green MR (February 1994). "Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production". Journal of Virology. 68 (2): 905–10. doi:10.1128/JVI.68.2.905-910.1994. PMC 236527. PMID 8289393.
- Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y (1996). "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae". Cytogenetics and Cell Genetics. 73 (1–2): 130–3. doi:10.1159/000134323. PMID 8646880.
- Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
- Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134. S2CID 13490886.
- Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
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- Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T (February 1998). "Retinoblastoma protein recruits histone deacetylase to repress transcription". Nature. 391 (6667): 597–601. Bibcode:1998Natur.391..597B. doi:10.1038/35404. PMID 9468139. S2CID 4326464.
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External links
[edit]- HDAC1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
