Includes bibliographical references and indexes.
|Statement||edited by Steven G. Clarke, Fuyuhiko Tamanoi.|
|Series||The enzymes -- v. 24|
|Contributions||Clarke, Steven G., Tamanoi, Fuyuhiko.|
|LC Classifications||QP606.M48 P76 2006|
|The Physical Object|
|Pagination||xii, 570 p. :|
|Number of Pages||570|
|LC Control Number||2006285718|
1. Copeland RA, Solomon ME, Richon VR. Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov ;– 2. Bannister AJ, et al. Regulation of chromatin by histone modiﬁcations. Cell Res ; – 3. Richon VM, et al. Chemogenetic analysis of human protein methyltransferases. Chem Biol Drug Des. DNA methyltransferases are important enzymes in a broad range of organisms. Dysfunction of DNA methyltransferases in humans leads to many severe diseases, including cancer. This book focuses on the biochemical properties of these enzymes, describing their structures and mechanisms in bacteria, humans and other species, including plants, and also explains the biological processes of reading of. Protein methyltransferases (PMTs) are implicated in various cancers and numerous other diseases, and the discovery of selective small‐molecule inhibitors of PMTs has become a very active research area. This chapter highlight the progress made in the discovery of PMT inhibitors in the last 15 : H. Ümit Kaniskan, Jian Jin. Inhibitors of Protein Methyltransferases and Demethylases H. Ümit Kaniskan,* Michael L. Martini, and Jian Jin* Departments of Pharmacological Sciences and Oncological Sciences, Icahn School of Medicine at Mount Sinai, New York, New York , United States ABSTRACT: Post-translational modiﬁcations of histones by protein methyltransferases.
yltransferases (both protein arginine and lysine methyltransferases) and the relatedness of their catalytic domains. We identiﬁed 51 protein lysine methyltransferase proteins based on similarity to the canonical Drosophila Su(var), enhancer of zeste (E(z)), and trithorax (trx) domain. Disruptor of telomeric silencinglike, a known protein. Protein Methyltransferase. Protein methyltransferases are essential for epigenetic regulation of gene expression through methylation of histones and non-histone proteins such as transcription factors, and have been implicated to play key roles in human diseases including cancer. From: Epigenetic Technological Applications, Related terms. N-alpha methyltransferases transfer a methyl group from SAM to the N-terminal nitrogen on protein targets. The N-terminal methionine is first cleaved by another enzyme and the X-Proline-Lysine consensus sequence is recognized by the all known substrates, the X amino acid is Alanine, Serine, or reaction yields a methylated protein and SAH. the enzymes volume 24 protein methyltransferases By Nora Roberts FILE ID 1f48b9 Freemium Media Library amazoncommx tienda kindle very good used hard cover email to.
This book reviews the chemical, regulatory, and physiological mechanisms of protein arginine and lysine methyltransferases, as well as nucleic acid methylations and methylating enzymes. Protein and nucleic acid methylation play key and diverse roles in cellular signalling and . DNMT3 is a family of DNA methyltransferases that could methylate hemimethylated and unmethylated CpG at the same rate. The architecture of DNMT3 enzymes is similar to that of DNMT1, with a regulatory region attached to a catalytic domain. There are four known members of . DNA methylation is an important modification of DNA that plays a role in genome management and in regulating gene expression during development. Methylation is carried out by DNA methyltransferases which catalyse the transfer of a methyl group to bases within the DNA helix. Plants have at least three classes of cytosine methyltransferase which differ in protein structure and function. REVIEW ARTICLE Critical roles of protein methyltransferases and demethylases in the regulation of embryonic stem cell fate Theodore Vougiouklakis a, Yusuke Nakamura,b, and Vassiliki Salouraa aSection of Hematology/Oncology, Department of Medicine, The University of Chicago, S. Maryland Ave, MC Chicago, IL , USA; bDepartment of Surgery, The University of Chicago, S. .