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Titlebook: Hormone Signaling; Vincent Goffin,Paul A. Kelly Book 2002 Springer Science+Business Media New York 2002 EGF receptor.G protein-coupled rec

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書目名稱Hormone Signaling
編輯Vincent Goffin,Paul A. Kelly
視頻videohttp://file.papertrans.cn/429/428317/428317.mp4
叢書名稱Endocrine Updates
圖書封面Titlebook: Hormone Signaling;  Vincent Goffin,Paul A. Kelly Book 2002 Springer Science+Business Media New York 2002 EGF receptor.G protein-coupled rec
描述Multicellular organisms require a means of intracellular communication to organize and develop the complex body plan that occurs during embryogenesis and then for cell and organ systems to access and respond to an ever changing environmental milieu. Mediators of this constant exchange of information are growth factors, neurotransmmitters, peptide and protein hormones which bind to cell surface receptors and transduce their signals from the extracellular space to the intracellular compartment. Via multiple signaling pathways, receptors of this general class affect growth, development and differentiation. Smaller hydrophobic signaling molecules, such as steroids and non-steroid hormones, vitamins and metabolic mediators interact with a large family of nuclear receptors. These receptors function as transcription factors affecting gene expression, to regulate the multiple aspects of animal and human physiology, including development, reproduction and homeostasis..The aim of this book is to cover various aspects of intracellular signaling involving hormone receptors.
出版日期Book 2002
關(guān)鍵詞EGF receptor; G protein-coupled receptors; TSH receptors; cytokine receptors; erythropoietin; estrogen ac
版次1
doihttps://doi.org/10.1007/978-1-4757-3600-7
isbn_softcover978-1-4419-4948-6
isbn_ebook978-1-4757-3600-7Series ISSN 1566-0729
issn_series 1566-0729
copyrightSpringer Science+Business Media New York 2002
The information of publication is updating

書目名稱Hormone Signaling影響因子(影響力)




書目名稱Hormone Signaling影響因子(影響力)學(xué)科排名




書目名稱Hormone Signaling網(wǎng)絡(luò)公開度




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978-1-4419-4948-6Springer Science+Business Media New York 2002
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William Bourguet,Pierre Germain,Hinrich Gronemeyer
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Control of Signaling by Tyrosine Phosphatasesades [1]. However, the importance of PTPs has not been fully appreciated until recently. The addition or removal of a phosphoryl moiety from tyrosine residue(s) in a protein can generate novel recognition motifs that regulate protein-protein interactions, control protein stability, and most importan
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Spatio-Temporal Parameters: The Case of the MAP Kinase Pathwayd MKK activates in turn the serine/threonine kinase MAP kinase or MAPK on the threonine and tyrosine residues of the consensus motif TXY (where T is threonine, X is glutamic acid, glycine or proline, and Y is tyrosine) [4]. Finally, activated MAPK phosphorylates diverse substrates including nuclear
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