Anbieter: Ria Christie Collections, Uxbridge, Vereinigtes Königreich
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In den WarenkorbZustand: New. In.
Sprache: Englisch
Verlag: Springer Berlin Heidelberg, 2012
ISBN 10: 3642804837 ISBN 13: 9783642804830
Anbieter: Revaluation Books, Exeter, Vereinigtes Königreich
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In den WarenkorbPaperback. Zustand: Brand New. reprint edition. 377 pages. 9.00x6.10x0.90 inches. In Stock.
Taschenbuch. Zustand: Neu. Protein Modules in Signal Transduction | Anthony J. Pawson | Taschenbuch | Current Topics in Microbiology and Immunology | ix | Englisch | 2011 | Springer | EAN 9783642804830 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.
Sprache: Englisch
Verlag: Springer Berlin Heidelberg, 2011
ISBN 10: 3642804837 ISBN 13: 9783642804830
Anbieter: AHA-BUCH GmbH, Einbeck, Deutschland
Taschenbuch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - The behavior of eukaryotic cells, particularly those of multicel lular organisms, depends on the transmission of signals from one cell to another. Such extracellular signals can take the form of hormones, antigens, cells surface molecules, or components of the extracellular matrix and exert their effects by binding to specific receptors, usually exposed on the surface of the target cell. These transmembrane receptors possess a cytoplasmic domain that al lows communication with intracellular signaling pathways, pro viding access to the regulation of gene expression, cytoskeletal architecture, cell metabolism, survival, and the cell cycle. Defining the process through which a signal emanating from an individual receptor can influence so many aspects of cellular function is of central importance for our understanding of signal transduction. Many polypeptide factors that regulate cellular growth and differentiation bind to receptors with cytoplasmic tyrosine kinase domains. Recent evidence has indicated that intracellular sig naling from receptor tyrosine kinases proceeds through a series of modular protein-protein interactions, typified by the interaction of autophosphorylated growth factor receptors with the Src ho mology 2 (SH2) domains of cytoplasmic target proteins. Thus, a crucial role of tyrosine phosphorylation is to promote the for mation of protein complexes through the creation of specific SH2 domain-binding sites, thereby regulating the activation of bio chemical pathways within the cell.