TY - BOOK ID - 8580344 TI - Protein tyrosine phosphatase control of metabolism PY - 2013 SN - 1461478545 1489997989 1461478553 PB - New York : Springer, DB - UniCat KW - Biochemistry. KW - Endocrinology. KW - Life sciences. KW - Medicine. KW - Protein-tyrosine kinase. KW - Protein-tyrosine phosphatase -- Metabolism -- Regulation. KW - Protein-tyrosine phosphatase KW - Biological Science Disciplines KW - Nutritional and Metabolic Diseases KW - Metabolic Phenomena KW - Protein Kinases KW - Phosphoric Monoester Hydrolases KW - Natural Science Disciplines KW - Phosphotransferases (Alcohol Group Acceptor) KW - Esterases KW - Phenomena and Processes KW - Diseases KW - Disciplines and Occupations KW - Hydrolases KW - Phosphotransferases KW - Enzymes KW - Transferases KW - Enzymes and Coenzymes KW - Chemicals and Drugs KW - Metabolic Diseases KW - Protein-Tyrosine Kinases KW - Metabolism KW - Protein Tyrosine Phosphatases KW - Physiology KW - Chemistry KW - Physical Sciences & Mathematics KW - Biochemistry KW - Regulation KW - Physiological effect. KW - Regulation. KW - Control of metabolism KW - Metabolic control KW - Metabolic regulation KW - Regulation of metabolism KW - Phosphotyrosine phosphatase KW - PTPase KW - Tyrosine phosphatase KW - Tyrosine phosphoprotein phosphatase KW - Tyrosyl phosphoprotein phosphatase KW - Proteins. KW - Life Sciences. KW - Protein Science. KW - Biochemistry, general. KW - Biomedicine general. KW - Biological control systems KW - Phosphoprotein phosphatases KW - Clinical sciences KW - Medical profession KW - Human biology KW - Life sciences KW - Medical sciences KW - Pathology KW - Physicians KW - Internal medicine KW - Hormones KW - Biological chemistry KW - Chemical composition of organisms KW - Organisms KW - Physiological chemistry KW - Biology KW - Composition KW - Proteins . KW - Endocrinology . KW - Biomedicine, general. KW - Health Workforce KW - Proteids KW - Biomolecules KW - Polypeptides KW - Proteomics UR - https://www.unicat.be/uniCat?func=search&query=sysid:8580344 AB - Tyrosine phosphorylation is a rapid and reversible protein modification catalyzed by the yin and yang activities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs).  A multitude of PTPs have been implicated in human disease, with a growing number of PTPs now known to play major roles in prevalent metabolic diseases including obesity and type 2 diabetes.  Recent studies into PTP function in the context of metabolism highlight the importance of understanding the specific substrates and binding partners of these enzymes, the regulation of PTP activity, and the cell/tissue specificity of PTP functions.  This volume contains chapters which highlight many aspects of PTP function in the context of metabolism. ER -