dc.contributor.author | Kuzmichev, A. | en |
dc.contributor.author | Margueron, R. | en |
dc.contributor.author | Vaquero, A. | en |
dc.contributor.author | Preissner, T. S. | en |
dc.contributor.author | Scher, M. | en |
dc.contributor.author | Kirmizis, Antonis | en |
dc.contributor.author | Ouyang, X. | en |
dc.contributor.author | Brockdorff, N. | en |
dc.contributor.author | Abate-Shen, C. | en |
dc.contributor.author | Farnham, P. | en |
dc.contributor.author | Reinberg, D. | en |
dc.creator | Kuzmichev, A. | en |
dc.creator | Margueron, R. | en |
dc.creator | Vaquero, A. | en |
dc.creator | Preissner, T. S. | en |
dc.creator | Scher, M. | en |
dc.creator | Kirmizis, Antonis | en |
dc.creator | Ouyang, X. | en |
dc.creator | Brockdorff, N. | en |
dc.creator | Abate-Shen, C. | en |
dc.creator | Farnham, P. | en |
dc.creator | Reinberg, D. | en |
dc.date.accessioned | 2019-11-04T12:52:16Z | |
dc.date.available | 2019-11-04T12:52:16Z | |
dc.date.issued | 2005 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/53216 | |
dc.description.abstract | Changes in the substrate specificities of factors that irreversibly modify the histone components of chromatin are expected to have a profound effect on gene expression through epigenetics. Ezh2 is a histone-lysine methyltransferase with activity dependent on its association with other components of the Polycomb Repressive Complexes 2 and 3 (PRC2/3). Ezh2 levels are increasingly elevated during prostate cancer progression. Other PRC2/3 components also are elevated in cancer cells. Overexpression of Ezh2 in tissue culture promotes formation of a previously undescribed PRC complex, PRC4, that contains the NAD +-dependent histone deacetylase SirT1 and isoform 2 of the PRC component Eed. Eed2 is expressed in cancer and undifferentiated embryonic stem (ES) cells but is undetectable in normal and differentiated ES cells. The distinct PRCs exhibit differential histone substrate specificities. These findings suggest that formation of a transformation-specific PRC complex may have a major role in resetting patterns of gene expression by regulating chromatin structure. | en |
dc.source | Proceedings of the National Academy of Sciences of the United States of America | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-13844315463&doi=10.1073%2fpnas.0409875102&partnerID=40&md5=298567df4b6b433a13ff62414af787f2 | |
dc.subject | article | en |
dc.subject | Male | en |
dc.subject | human | en |
dc.subject | Humans | en |
dc.subject | controlled study | en |
dc.subject | cancer growth | en |
dc.subject | priority journal | en |
dc.subject | protein analysis | en |
dc.subject | protein expression | en |
dc.subject | Gene Expression Regulation | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | cancer cell | en |
dc.subject | human cell | en |
dc.subject | gene expression | en |
dc.subject | Animals | en |
dc.subject | Mice | en |
dc.subject | animal cell | en |
dc.subject | animal tissue | en |
dc.subject | mouse | en |
dc.subject | gene overexpression | en |
dc.subject | Transcription Factors | en |
dc.subject | DNA-Binding Proteins | en |
dc.subject | cell differentiation | en |
dc.subject | enzyme activity | en |
dc.subject | Prostate cancer | en |
dc.subject | Prostatic Neoplasms | en |
dc.subject | regulatory mechanism | en |
dc.subject | epigenetics | en |
dc.subject | Gene Expression Profiling | en |
dc.subject | Animalia | en |
dc.subject | Proteins | en |
dc.subject | repressor protein | en |
dc.subject | Repressor Proteins | en |
dc.subject | Protein Isoforms | en |
dc.subject | RNA Interference | en |
dc.subject | chromatin structure | en |
dc.subject | Multigene Family | en |
dc.subject | Histones | en |
dc.subject | tissue culture | en |
dc.subject | Hela Cells | en |
dc.subject | embryonic ectoderm development protein | en |
dc.subject | histone lysine methyltransferase | en |
dc.subject | Macromolecular Substances | en |
dc.subject | Methylation | en |
dc.subject | Oligonucleotide Array Sequence Analysis | en |
dc.subject | enzyme specificity | en |
dc.subject | Ezh2 | en |
dc.subject | histone | en |
dc.subject | histone deacetylase | en |
dc.subject | Histone H1 | en |
dc.subject | isoenzyme | en |
dc.subject | nicotinamide adenine dinucleotide | en |
dc.subject | polycomb repressive complex 2 | en |
dc.subject | polycomb repressive complex 3 | en |
dc.subject | polycomb repressive complex 4 | en |
dc.subject | protein Eed2 | en |
dc.subject | protein EZH2 | en |
dc.subject | protein sirt1 | en |
dc.subject | Sirtuins | en |
dc.subject | Substrate Specificity | en |
dc.title | Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1073/pnas.0409875102 | |
dc.description.volume | 102 | |
dc.description.startingpage | 1859 | |
dc.description.endingpage | 1864 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Βιολογικών Επιστημών / Department of Biological Sciences | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :317</p> | en |
dc.source.abbreviation | Proc.Natl.Acad.Sci.U.S.A. | en |
dc.contributor.orcid | Kirmizis, Antonis [0000-0002-3748-8711] | |
dc.gnosis.orcid | 0000-0002-3748-8711 | |