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Titlebook: Receptor Tyrosine Kinases: Structure, Functions and Role in Human Disease; Deric L. Wheeler,Yosef Yarden Book 2015 Springer Science+Busine

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书目名称Receptor Tyrosine Kinases: Structure, Functions and Role in Human Disease
编辑Deric L. Wheeler,Yosef Yarden
视频video
概述Leading scientists and researcher providing cutting-edge data.A comprehensive resource that summarizes what we know about receptor tyrosine kinases.An incredible resource to researchers and clinicians
图书封面Titlebook: Receptor Tyrosine Kinases: Structure, Functions and Role in Human Disease;  Deric L. Wheeler,Yosef Yarden Book 2015 Springer Science+Busine
描述.Receptor Tyrosine Kinase: Structure, Functions and Role in Human Disease., for the first time, systematically covers the shared structural and functional features of the RTK family. Receptor Tyrosine Kinases (RTKs) play critical roles in embryogenesis, normal physiology and several diseases. And over the last decade they have become the .Number 1. targets of cancer drugs. To be able to conduct fundamental research or to attempt to develop pharmacological agents able to enhance or intercept them, it is essential first to understand the evolutionary origin of the 58 RTKs and their roles in invertebrates and in humans, as well as downstream signaling pathways. The assembly of chapters is written by experts and underscores commonalities between and among the RTKs. It is an ideal companion volume to .The Receptor Tyrosine Kinase: Families and Subfamilies., which proceeds, family by family through all of the specific subfamilies of RTKs, along with their unique landmarks..
出版日期Book 2015
关键词Kinase; Proteins; Receptors; Signaling pathways; Tyrosines
版次1
doihttps://doi.org/10.1007/978-1-4939-2053-2
isbn_softcover978-1-4939-4119-3
isbn_ebook978-1-4939-2053-2
copyrightSpringer Science+Business Media New York 2015
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Receptor Tyrosine Kinase Signal Transduction and the Molecular Basis of Signalling Specificity,rations in cancer and metabolic diseases. Since the cloning of the first RTK (the EGF receptor) 30 years ago, considerable progress has been made in the structural biology of both the extracellular domains and the tyrosine kinase domains of many members of the RTK superfamily. These studies have fir
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Computational and Modeling Aspects of RTK Networks, to the cytoplasm and nucleus of target cells. Here we focus on one subgroup of receptor tyrosine kinases, whose prototype is the epidermal growth factor receptor (EGFR). Due to ligand-induced homo- and heterodimerization by EGFR (also called ERBB1) and other family members, extracellular signals ar
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Endocytosis and Endosomal Sorting of Receptor Tyrosine Kinases,g of internalized RTKs to lysosomes for degradation. Rapid internalization and efficient sorting of an activated RTK to lysosomes lead to a dramatic reduction in the cellular level of an RTK protein, a phenomenon called ligand-induced RTK downregulation. Endocytic trafficking is the major regulator
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