What's new for 'JKB_daily1' in PubMed

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Sender's message: Sepsis or genomics or altitude: JKB_daily1

Sent on Wednesday, 2011 Jan 05
Search (sepsis[MeSH Terms] OR septic shock[MeSH Terms] OR altitude[MeSH Terms] OR genomics[MeSH Terms] OR genetics[MeSH Terms] OR retrotransposons[MeSH Terms] OR macrophage[MeSH Terms]) AND ("2009/8/8"[Publication Date] : "3000"[Publication Date]) AND (("Science"[Journal] OR "Nature"[Journal] OR "The New England journal of medicine"[Journal] OR "Lancet"[Journal] OR "Nature genetics"[Journal] OR "Nature medicine"[Journal]) OR (Hume DA[Author] OR Baillie JK[Author] OR Faulkner, Geoffrey J[Author]))
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PubMed Results

Items 1 - 7 of 7

1.	Nature. 2010 Dec 23;468(7327):1124-8. Transcriptional activation of polycomb-repressed genes by ZRF1. Richly H, Rocha-Viegas L, Ribeiro JD, Demajo S, Gundem G, Lopez-Bigas N, Nakagawa T, Rospert S, Ito T, Di Croce L. Centre de Regulació Genòmica (CRG)/UPF, 08003 Barcelona, Spain. Abstract Covalent modification of histones is fundamental in orchestrating chromatin dynamics and transcription. One example of such an epigenetic mark is the mono-ubiquitination of histones, which mainly occurs at histone H2A and H2B. Ubiquitination of histone H2A has been implicated in polycomb-mediated transcriptional silencing. However, the precise role of the ubiquitin mark during silencing is still elusive. Here we show in human cell lines that ZRF1 (zuotin-related factor 1) is specifically recruited to histone H2A when it is ubiquitinated at Lys 119 by means of a novel ubiquitin-interacting domain that is located in the evolutionarily conserved zuotin domain. At the onset of differentiation, ZRF1 specifically displaces polycomb-repressive complex 1 (PRC1) from chromatin and facilitates transcriptional activation. A genome-wide mapping of ZRF1, RING1B and H2A-ubiquitin targets revealed its involvement in the regulation of a large set of polycomb target genes, emphasizing the key role ZRF1 has in cell fate decisions. We provide here a model of the molecular mechanism of switching polycomb-repressed genes to an active state.
	PMID: 21179169 [PubMed - indexed for MEDLINE]
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2.	Nature. 2010 Dec 23;468(7327):S21-2. Technology: A flavour of the future. Frood A.
	PMID: 21179082 [PubMed - indexed for MEDLINE]
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3.	Nature. 2010 Dec 23;468(7327):S20. Epigenetics: Tales of adversity. Ahmed F.
	PMID: 21179081 [PubMed - indexed for MEDLINE]
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4.	Nature. 2010 Dec 23;468(7327):S2-4. Interdisciplinary research: Big science at the table. Laurse n L.
	PMID: 21179080 [PubMed - indexed for MEDLINE]
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5.	Nature. 2010 Dec 23;468(7327):S16-7. History: The changing notion of food. Stafford N.
	PMID: 21179078 [PubMed - indexed for MEDLINE]
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6.	Nature. 2010 Dec 23;468(7327):S1. Nutrigenomics. Grayson M.
	PMID: 21179075 [PubMed - indexed for MEDLINE]
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7.	Nature. 2010 Dec 23;468(7327):1119-23. Epub 2010 Nov 10. Suppression of inflammation by a synthetic histone mimic. Nicodeme E, Jeffrey KL, Schaefer U, Beinke S, Dewell S, Chung CW, Chandwani R, Marazzi I, Wilson P, Coste H, White J, Kirilovsky J, Rice CM, Lora JM, Prinjha RK, Lee K, Tarakhovsky A. Centre de Recherche GSK, 27 Avenue du Québec, 91140 Villebon Sur Yvette, France. Comment in: Nature. 2010 Dec 23;468(7327):1050-1. Abstract Interaction of pathogens with cells of the immune system results in activation of inflammatory gene expression. This response, although vital for immune defence, is frequently deleterious to the host due to the exaggerated production of inflammatory proteins. The scope of inflammatory responses reflects the activation state of signalling proteins upstream of inflammatory genes as well as signal-induced assembly of nuclear chromatin complexes that support mRNA expression. Recognition of post-translationally modified histones by nuclear proteins that initiate mRNA transcription and support mRNA elongation is a critical step in the regulation of gene expression. Here we present a novel pharmacological approach that targets inflammatory gene expression by interfering with the recognition of acetylated histones by the bromodomain and extra terminal domain (BET) family of proteins. We describe a synthetic compound (I-BET) that by 'mimicking' acetylated histones disrupts chromatin complexes responsible for the expression of key inflammatory genes in activated macrophages, and confers protection against lipopolysaccharide-induced endotoxic shock and bacteria-induced sepsis. Our findings suggest that synthetic compounds specifically targeting proteins that recognize post-translationally modified histones can serve as a new generation of immunomodulatory drugs.
	PMID: 21068722 [PubMed - indexed for MEDLINE]
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