Blood 2000, 96:2149–56 PubMed 112 Gómez MI, Lee A, Reddy B, Muir

Blood 2000, 96:2149–56.PubMed 112. Gómez MI, Lee A, Reddy B, Muir A, Soong G, Pitt A, Cheung A,

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Panizzi P, Bock PE: Von Willebrand factor-binding protein is a hysteretic conformational activator of prothrombin. Proc Natl Acad Sci USA 2009, 106:7786–91.PubMed 118. Liang OD, Flock JI, Wadström T: Isolation and characterisation of a vitronectin-binding surface protein from Staphylococcus aureus. Biochim Biophys Acta 1995, 1250:110–6.PubMed Authors’ contributions AJM participated in study design, generation of sequence alignments, sequence analysis, microarray analysis and in manuscript revisions. JAL participated in the study design and coordination, microarray analysis, GS-1101 solubility dmso and drafted the manuscript. All authors read Benzatropine and approved the final manuscript.”
“Background A possible novel additional

strategy used by bacterial pathogens during infection is to interfere with host cellular processes by inducing epigenetic modifications and, consequently, determining a new specific cell transcriptional profile. Bacteria or their components could be a stimulus to change the genetic program of the target cells through epigenetic mechanisms [1, 2]. These mechanisms may operate at gene-specific level and include both chromatin modifications, orchestrated by chromatin-remodeling complexes and histone-modifying enzymes, and DNA methylation, directed by DNA-methyltransferases. Histone acetylation is in general associated to an active state of the chromatin while the effects of histone methylation may be associated with either transcriptional activation or repression, depending on which lysyl residue is modified [3, 4] and whether this residue is mono, di or trimethylated. Among the best studied H3 lysine modifications are di- and trimethylation of H3 on lysine 9 and lysine 27 (H3K9me2 and H3K27me3), associated with closed chromatin, and dimethylation of H3 on lysine 4 (H3K4me2) that marks active chromatin state.

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