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49
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0030606239
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The transcriptional coactivators p300 and CBP are histone acetyltransferases
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One of the first of numerous papers published since the description of endogenous histone acetyltransferase activity in transcriptional adaptor, co-activator, or components of the transcriptional machinery. Importantly, the authors show that p300/CBP acetylates all of the core histones in nucleosomes. Thus, p300/CBP may regulate gene activity directly via its targeted acetylation.
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Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959 One of the first of numerous papers published since the description of endogenous histone acetyltransferase activity in transcriptional adaptor, co-activator, or components of the transcriptional machinery. Importantly, the authors show that p300/CBP acetylates all of the core histones in nucleosomes. Thus, p300/CBP may regulate gene activity directly via its targeted acetylation.
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Ogryzko, V.V.1
Schiltz, R.L.2
Russanova, V.3
Howard, B.H.4
Nakatani, Y.5
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50
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0029985730
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Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro
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of special interest. This paper uses antibodies to acetylated H4 and acetylated H3 to show that nucleosome cores with the highest affinity for transcription factors contain histones highly acetylated on histone H4. Highly acetylated H3 was shown to play much less of a role in binding. This finding illustrates the specific effects histone acetylation can have upon gene regulation and may be a harbinger of future work examining the role of specific acetyl-isoforms of the core histones and their effects on transcriptional factor binding.
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Vettese-Dadey M, Grant PA, Hebbes TR, Crane-Robinson C, Allis CD, Workman JL. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. of special interest EMBO J. 15:1996;2508-2518 This paper uses antibodies to acetylated H4 and acetylated H3 to show that nucleosome cores with the highest affinity for transcription factors contain histones highly acetylated on histone H4. Highly acetylated H3 was shown to play much less of a role in binding. This finding illustrates the specific effects histone acetylation can have upon gene regulation and may be a harbinger of future work examining the role of specific acetyl-isoforms of the core histones and their effects on transcriptional factor binding.
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EMBO J
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Vettese-Dadey, M.1
Grant, P.A.2
Hebbes, T.R.3
Crane-Robinson, C.4
Allis, C.D.5
Workman, J.L.6
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51
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0030916336
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Whats up and down with histone deacetylation and transcription?
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of special interest
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Pazin MJ, Kadonaga JT. Whats up and down with histone deacetylation and transcription? of special interest Cell. 89:1997;325-328.
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Cell
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Pazin, M.J.1
Kadonaga, J.T.2
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52
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Induction of γ-globin by histone deacetylase inhibitors
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McCaffrey PG, Newsome DA, Fibach E, Yoshida M, Su MSS. Induction of γ-globin by histone deacetylase inhibitors. Blood. 90:1997;2075-2083.
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Newsome, D.A.2
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Su, M.S.S.5
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53
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0021203873
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Activation of a chicken embryonic globin gene in adult erythroid cells by 5-azacytidine and sodium butyrate
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Ginder GD, Whitters MJ, Pohlman JK. Activation of a chicken embryonic globin gene in adult erythroid cells by 5-azacytidine and sodium butyrate. Proc Natl Acad Sci USA. 81:1984;3954-3958.
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Ginder, G.D.1
Whitters, M.J.2
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