Home Technique • Gene Engineering in Endocrinology by Corinne M. Silva PhD (auth.), Margaret A. Shupnik PhD (eds.)

Gene Engineering in Endocrinology by Corinne M. Silva PhD (auth.), Margaret A. Shupnik PhD (eds.)

By Corinne M. Silva PhD (auth.), Margaret A. Shupnik PhD (eds.)

Recent advances in genetic engineering and molecular biology have made it attainable to disrupt particular genes so one can make certain and higher comprehend their functionality and scientific value. In Gene Engineering in Endocrinology, Margaret Shupnik and a workforce of prime investigators assessment the latest breakthroughs, emphasizing how stories of common mutations and gene knockouts have illuminated endocrine approaches. utilizing either animal and human version info, those authoritative researchers study extensive the molecular foundation of improvement, progress, and reproductive procedures, the categorical mutations that specify sure genetic syndromes, the hormonal rules of gene expression (which impacts the remedy of infertility and steroid-dependent cancers), and present learn instructions. while attainable, molecular stories are in comparison with obviously taking place human and animal gene mutations to set up the variation among entire removal of, or an altered, gene function.
accomplished and updated, Gene Engineering in Endocrinology deals modern-day experimental and scientific endocrinologists, in addition to reproductive biologists, a richly informative survey of what has already been entire with the genetic engineering of hormone methods and hormone-related genetic syndromes-research that supplies robust new experimental and healing possibilities as this box keeps it quick improvement.

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Alterations in skeletal muscle proteintyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes. J Clin Invest 1997; 100:449–458. Tappia PS, Sharma RP, Sale GJ. Dephosphorylation of autophosphorylated insulin and epidermalgrowth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta. Biochem J 1991; 278:69–74. Hashimoto N, Zhang WR, Goldstein BJ. Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system.

Based on the sequence flanking the tyrosine phosphorylation site in pp120/ HA4, Najjar et al. (117) predicted that the protein would bind to the SH2 domain of SH2-containing phosphotyrosine phosphatases. Subsequently, two other laboratories identified two homologous glycoproteins (SHP substrate-1 [118] and signal-regulatory protein [SIRP] [119]) that were phosphorylated by the insulin receptor and other tyrosine kinases. Furthermore, the phosphorylated proteins did indeed bind to SHP-1 and SHP2, and served as substrates for these two phosphotyrosine phosphatases.

EMBO J 1997; 16:5572–5581. 16. Songyang Z, Shoelson SE, Chaudhuri M, Gish G, Pawson T, Haser WG, King F, Roberts T, Ratnofsky S, Lechleider RJ, Neel BG, Birge RB, Fajardo JE, Chou MM, Hanafusa H. SH2 domains recognize specific phosphopeptide sequences. Cell 1993; 72:767–778. 17. Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, Bustelo XR, Barbacid M, Sabe H, Hanafusa H, Yi T, Ren R, Baltimore D, Ratnosfky S, Feldman RA, Cantley LC. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav.

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