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