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Paul J. Hurd

Researcher at Queen Mary University of London

Publications -  28
Citations -  3250

Paul J. Hurd is an academic researcher from Queen Mary University of London. The author has contributed to research in topics: DNA methylation & Epigenetics. The author has an hindex of 17, co-authored 27 publications receiving 3008 citations. Previous affiliations of Paul J. Hurd include University of Sheffield & Cairo University.

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The Methyl-CpG-binding Protein MeCP2 Links DNA Methylation to Histone Methylation

TL;DR: It is shown that MeCP2 associates with histone methyltransferase activity in vivo and that this activity is directed against Lys9 of histone H3, and this activity coincides with an increase in H3 Lys9methylation.
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The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase

TL;DR: The data show a direct connection between the enzymes responsible for DNA methylation and histone methylation, and substantiate the notion of a self-reinforcing repressive chromatin state through the interplay between these two global epigenetic modifications.
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Zebularine: A Novel DNA Methylation Inhibitor that Forms a Covalent Complex with DNA Methyltransferases

TL;DR: The interaction between the C5 MTase from Haemophilus haemolyticus and an oligodeoxynucleotide duplex containing 2-H pyrimidinone provides a molecular explanation for the mechanism of action of the anti-cancer drug zebularine.
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Advantages of next-generation sequencing versus the microarray in epigenetic research

TL;DR: It is inevitable that massively-parallel sequencing platforms will supercede the microarray for many applications, however, there are niches for microarrays to fill and interestingly the authors may very well witness a symbiotic relationship between microarray and high-throughput sequencing in the future.
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Dynamic distribution of the replacement histone variant H3.3 in the mouse oocyte and preimplantation embryos.

TL;DR: It is detected H3.3 in the nuclei of mouse embryos in all of the stages analysed, from the zygote to the blastocyst stage, suggesting that the epigenetic mechanisms in the early embryo not only involve changes in histone modifications but may also include histone replacement.