Modular protein-protein interactions provide a general mechanism to organize dynamic cellular systems [electronic resource] / Tony Pawson.

By: Pawson, T [spk]Material type: FilmFilmSeries: Henry Stewart talksBiomedical & life sciences collection. Protein phosphorylation: ; Henry Stewart talksBiomedical & life sciences collection. Signal transduction via protein tyrosine kinase receptors : structures, function, regulation, mechanisms and role in disease: Publisher: London : Henry Stewart Talks, 2010Description: 1 online resource (1 streaming video file (51 min.) : color, sound)Subject(s): Cellular signal transduction | Phosphorylation | Proteins | Receptor Protein-Tyrosine Kinases | Signal TransductionOnline resources: Click here to access online | Series (Signal Transduction) | Series (Protein Phosphorylation)
Contents:
Contents: Mechanisms through which protein interactions modules, such as the SH2 domain, mediate the activation of specific signaling pathways by normal and oncogenic tyrosine kinases -- The biological functions and biochemical properties of interaction domains including their roles in controlling protein localization, in recognition of post-translational modifications, in forming multi-protein complexes, and in regulating enzymatic function -- The versatility of interaction domains, their potential utility in the evolution of new signaling pathways, and their exploitation by pathogenic proteins to rewire cellular behavior
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Animated audio-visual presentation with synchronized narration.

Title from title frames.

Updated version of a talk first published 2007.

Contents: Mechanisms through which protein interactions modules, such as the SH2 domain, mediate the activation of specific signaling pathways by normal and oncogenic tyrosine kinases -- The biological functions and biochemical properties of interaction domains including their roles in controlling protein localization, in recognition of post-translational modifications, in forming multi-protein complexes, and in regulating enzymatic function -- The versatility of interaction domains, their potential utility in the evolution of new signaling pathways, and their exploitation by pathogenic proteins to rewire cellular behavior

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