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- Publications
- Influence
Chromatin Modifications and Their Function
- T. Kouzarides
- Biology, Medicine
- Cell
- 23 February 2007
The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each… Expand
Regulation of chromatin by histone modifications
- Andrew J. Bannister, T. Kouzarides
- Biology, Medicine
- Cell Research
- 15 February 2011
Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key… Expand
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
- Andrew J. Bannister, P. Zegerman, +4 authors T. Kouzarides
- Biology, Medicine
- Nature
- 1 March 2001
Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1 is necessary for both targeting and transcriptional repression. In the… Expand
Analysis of the protein-coding content of the sequence of human cytomegalovirus strain AD169.
- M. Chee, A. Bankier, +7 authors J. A. Martignetti
- Biology, Medicine
- Current topics in microbiology and immunology
- 1990
Large-scale sequence analysis of the AD169 strain of human cytomegalovirus (HCMV) began in this laboratory in 1984 when very little was known about the sequence or location of genetic information in… Expand
Active genes are tri-methylated at K4 of histone H3
- H. Santos-Rosa, R. Schneider, +6 authors T. Kouzarides
- Biology, Medicine
- Nature
- 26 September 2002
Lysine methylation of histones in vivo occurs in three states: mono-, di- and tri-methyl. Histone H3 has been found to be di-methylated at lysine 4 (K4) in active euchromatic regions but not in… Expand
Cancer Epigenetics: From Mechanism to Therapy
- M. Dawson, T. Kouzarides
- Biology, Medicine
- Cell
- 6 July 2012
The epigenetic regulation of DNA-templated processes has been intensely studied over the last 15 years. DNA methylation, histone modification, nucleosome remodeling, and RNA-mediated targeting… Expand
Retinoblastoma protein recruits histone deacetylase to repress transcription
- A. Brehm, E. Miska, D. Mccance, J. L. Reid, Andrew J. Bannister, T. Kouzarides
- Biology, Medicine
- Nature
- 5 February 1998
The retinoblastoma protein (Rb) silences specific genes that are active in the S phase of the cell cycle and which are regulated by E2F transcription factors. Rb binds to the activation domain of E2F… Expand
The CBP co-activator is a histone acetyltransferase
- Andrew J. Bannister, T. Kouzarides
- Biology, Medicine
- Nature
- 19 December 1996
THE CBP protein acts as a transcriptional adaptor for many different transcription factors by directly contacting DNA-bound activators1–7. One mechanism by which CBP is thought to stimulate… Expand
DNA methyltransferase Dnmt1 associates with histone deacetylase activity
- F. Fuks, W. Burgers, A. Brehm, L. Hughes-Davies, T. Kouzarides
- Biology, Medicine
- Nature Genetics
- 2000
The DNA methyltransferase Dnmt1 is responsible for cytosine methylation in mammals and has a role in gene silencing. DNA methylation represses genes partly by recruitment of the methyl-CpG-binding… Expand
The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase.
- F. Fuks, P. Hurd, Rachel Deplus, T. Kouzarides
- Biology, Medicine
- Nucleic acids research
- 1 May 2003
The DNA methyltransferases, Dnmts, are the enzymes responsible for methylating DNA in mammals, which leads to gene silencing. Repression by DNA methylation is mediated partly by recruitment of the… Expand