{"product_id":"reversible-protein-acetylation-isbn-9780470862612","title":"Reversible Protein Acetylation","description":"A comprehensive review of recent work on chromatin and non-histone proteins, this book arises from the interactions of a multidisciplinary group of scientists involved in the study of acetylation. This area of research opens up new and exciting possibilities for drug design, and so the final chapters in the book examine some of the potential applications in the treatment of various diseases.  Chair's Introduction (E. Verdin).  \u003cp\u003eBeyond the double helix: writing and reading the histone code (Y. Wang, et al.).\u003c\/p\u003e \u003cp\u003eThe indexing potential of histone lysine methylation (G. Schotta, et al.)\u003c\/p\u003e \u003cp\u003eA model for step-wise assembly of heterochromatin in yeast (D. Moazed, et al.).\u003c\/p\u003e \u003cp\u003eH2B Ubiquitylation and deubiquitylation in gene activation (A. Wyce, et al.).\u003c\/p\u003e \u003cp\u003eStructural and chemical basis of histone acetylation (R. Marmorstein).\u003c\/p\u003e \u003cp\u003ePhosphorylation and acetylation of histone H3 at inducible genes: two controversies revisted (L. Mahadevan, et al.).\u003c\/p\u003e \u003cp\u003eHDAC7 regulates apoptosis in developing thymocytes (E. Verdin, et al.).\u003c\/p\u003e \u003cp\u003eDual roles of histone deacetylases in the control of cardiac growth (T. McKinsey and E. Olson).\u003c\/p\u003e \u003cp\u003eChromatin modifications as clues to the regulation of antigen receptor assembly (D. Ciccone and M. Oettinger).\u003c\/p\u003e \u003cp\u003eGeneral discussion I Histone modifications in X inactivation.\u003c\/p\u003e \u003cp\u003eThe HDAC complex and cytoskeleton (J. Kovacs, et al.).\u003c\/p\u003e \u003cp\u003eTat acetylation: a regulatory switch between early and late phases in HIV transcription elongation (M. Ott, et al.).\u003c\/p\u003e \u003cp\u003eDynamics of the p53 acetylation pathway (W. Gu, et al.).\u003c\/p\u003e \u003cp\u003eRegulation of the NF-kB action by reversible acetylation (W. Greene and L. Chen).\u003c\/p\u003e \u003cp\u003eGeneral discussion II p300 and DNA repair.\u003c\/p\u003e \u003cp\u003eReversal of gene silencing as a therapeutic target for cancer - roles for DNA methylation and interdigitation with chromatin (S. Baylin).\u003c\/p\u003e \u003cp\u003eTranscription regulation by histone deacetylases (S. Wang, et al.).\u003c\/p\u003e \u003cp\u003eMolecular and cellular basis for the anti-proliferative effects of the HDAC inhibitor LAQ824 (P. Atadja, et al.).\u003c\/p\u003e \u003cp\u003eHistone deacetylase inhibitors: development as cancer therapy (P. Marks, et al.).\u003c\/p\u003e \u003cp\u003eGeneral discussion III PML-RAR hypermethylation in leukemia.\u003c\/p\u003e \u003cp\u003eIndex of Contributors.\u003c\/p\u003e \u003cp\u003eSubject Index.\u003c\/p\u003e  The \u003cstrong\u003eNovartis Foundation\u003c\/strong\u003e is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.   The reversible acetylation of lysine residues on histone proteins has emerged as a major factor in the regulation of transcription in eukaryotes. All core histone proteins are acetylated and unique functional chromosomal domains are characterized by specific patterns of acetylation within their histone proteins. Functional correlations have been established between the level of acetylation of individual genes and their transcriptional activity. These complex signals are currently being elucidated in the context of the ‘histone code hypothesis’. This model posits that distinct acetylation patterns in histones, along with other post-translational modifications, serve as specific signals recognized by the nuclear transcriptional machinery.  \u003cp\u003eHistone acetylation is under the control of competing histone acetyltransferases (HATs) and histone deacetylases (HDACs). Both enzyme families contain many members: at least 18 distinct human HDACs have been identified. As well as regulating transcription, these proteins play critical roles in cell cycle control and differentiation. Acetylation is not restricted to histone proteins; a growing number of important biological functions appear to be regulated via acetylation. These include DNA binding (p53), nuclear–cytoplasmic shuttling (NF-kB) and coactivator recruitment (HIV Tat protein).\u003c\/p\u003e \u003cp\u003eThis novel research opens up new and exciting possibilities for drug design. Inhibitors have been developed that specifically target either HDACs or HATs. HDAC inhibitors exhibit selective toxicity towards tumour cells and are being developed as potential anticancer drugs. This book describes current knowledge of acetylation and features extensive discussions amongst the world’s experts in this field, with an emphasis on major unanswered questions.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989959459045,"sku":"NP9780470862612","price":211.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9780470862612.jpg?v=1761786034","url":"https:\/\/k12savings.com\/products\/reversible-protein-acetylation-isbn-9780470862612","provider":"K12savings","version":"1.0","type":"link"}