T. Kouzarides

Publications247
h-index116
Citations70,445
Highly Influential Citations3,770
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Chromatin Modifications and Their Function
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Regulation of chromatin by histone modifications
TLDR
The known histone modifications are described, where they are found genomically and discussed and some of their functional consequences are discussed, concentrating mostly on transcription where the majority of characterisation has taken place.
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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
TLDR
A stepwise model for the formation of a transcriptionally silent heterochromatin is provided: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain, which may also explain the stable inheritance of theheterochromatic state.
View on Nature
Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169.
TLDR
This chapter is being written in March 1989 when the sequence is complete except for some remaining polishing of certain areas which is still going on (manuscript in preparation).
View on PubMed
Active genes are tri-methylated at K4 of histone H3
TLDR
It is shown that the Saccharomyces cerevisiae Set1 protein can catalyse di- and tri-methylation of K4 and stimulate the activity of many genes, establishing the concept of methyl status as a determinant for gene activity and extending considerably the complexity of histone modifications.
View on Nature
Retinoblastoma protein recruits histone deacetylase to repress transcription
TLDR
It is shown that Rb associates with a histone deacetylase, HDAC1, through the Rb ‘pocket’ domain, and that active transcriptional repression by Rb may involve the modification of chromatin structure.
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Cancer Epigenetics: From Mechanism to Therapy
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The CBP co-activator is a histone acetyltransferase
TLDR
It is shown that CBP has intrinsic HAT activity, and Targeting CBP-associated H AT activity to specific promoters may be a mechanism by which E1A acts as a transcriptional activator.
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Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia
TLDR
It is shown that a novel small molecule inhibitor of the BET family, GSK1210151A (I-BET151), has profound efficacy against human and murine MLL-fusion leukaemic cell lines, through the induction of early cell cycle arrest and apoptosis, establishing the displacement of BET proteins from chromatin as a promising epigenetic therapy for these aggressive leukaemias.
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New Nomenclature for Chromatin-Modifying Enzymes
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