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

Henry Stewart Biomedical & Life Sciences Collection Available online

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Format:
Video
Author/Creator:
Pawson, T., speaker, author.
Series:
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.
Protein phosphorylation, 2056-452X
Signal transduction via protein tyrosine kinase receptors : structures, function, regulation, mechanisms and role in disease, 2056-452X
Language:
English
Subjects (All):
Cellular signal transduction.
Phosphorylation.
Proteins.
Receptor Protein-Tyrosine Kinases.
Signal Transduction.
Medical Subjects:
Phosphorylation.
Proteins.
Receptor Protein-Tyrosine Kinases.
Signal Transduction.
Genre:
Video recordings.
Physical Description:
1 online resource (1 streaming video file (51 min.)) : color, sound.
polychrome
Place of Publication:
London : Henry Stewart Talks, 2010.
System Details:
Mode of access: World Wide Web.
video file
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
Notes:
Animated audio-visual presentation with synchronized narration.
Revised version of a talk first published 2007.
Title from title frames.
Publisher Number:
1115 Henry Stewart Talks
Access Restriction:
Restricted for use by site license.

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