Pawson, T.

Modular protein-protein interactions provide a general mechanism to organize dynamic cellular systems [electronic resource] / Tony Pawson. - London : Henry Stewart Talks, 2010. - 1 online resource (1 streaming video file (51 min.) : color, sound). - Protein phosphorylation, 2056-452X Signal transduction via protein tyrosine kinase receptors : structures, function, regulation, mechanisms and role in disease, 2056-452X . - Henry Stewart talks. Biomedical & life sciences collection. Protein phosphorylation. Henry Stewart talks. Biomedical & life sciences collection. Signal transduction via protein tyrosine kinase receptors : structures, function, regulation, mechanisms and role in disease. .

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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1115 Henry Stewart Talks


Cellular signal transduction.
Phosphorylation.
Proteins.
Receptor Protein-Tyrosine Kinases.
Signal Transduction.
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