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Quantitative Analysis of Oncogenic Kinase Signaling Networks

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Air date: Friday, March 7, 2008, 10:00:00 AM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 20 * This only includes stats from October 2011 and forward.
Category: Proteomics
Runtime: 01:07:53
Description: Aberrations in protein phosphorylation due to kinase (or phosphatase) mutation or overexpression leads to dysregulation of cellular signaling and has been linked to a variety of pathologies, including cancer, autoimmune, and metabolic disorders. Quantification of specific phosphorylation sites regulating signaling pathways involved in these pathological disorders should enable a better understanding of the genesis and progression of the disease state, potentially providing targets for more effective therapeutic intervention. To effectively monitor protein phosphorylation events governing signaling cascades, we have developed a methodology enabling the simultaneous quantification of tyrosine phosphorylation of specific residues on dozens of key proteins in a time-resolved manner. By combining mass spectrometry-based analysis of protein phosphorylation with phenotypic measurements and computational modeling, we are now able to identify sections of the signaling network that correlate strongly with biological response to cell perturbation. This approach should yield novel insights into the regulation of biological decisions on the network scale.

http://proteome.nih.gov
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NLM Title: Quantitative analysis of oncogenic kinase signaling networks [electronic resource] / Forest White.
Author: White, Forest.
National Institutes of Health (U.S.)
Publisher:
Abstract: (CIT): Aberrations in protein phosphorylation due to kinase (or phosphatase) mutation or overexpression leads to dysregulation of cellular signaling and has been linked to a variety of pathologies, including cancer, autoimmune, and metabolic disorders. Quantification of specific phosphorylation sites regulating signaling pathways involved in these pathological disorders should enable a better understanding of the genesis and progression of the disease state, potentially providing targets for more effective therapeutic intervention. To effectively monitor protein phosphorylation events governing signaling cascades, we have developed a methodology enabling the simultaneous quantification of tyrosine phosphorylation of specific residues on dozens of key proteins in a time-resolved manner. By combining mass spectrometry-based analysis of protein phosphorylation with phenotypic measurements and computational modeling, we are now able to identify sections of the signaling network that correlate strongly with biological response to cell perturbation. This approach should yield novel insights into the regulation of biological decisions on the network scale.
Subjects: MAP Kinase Signaling System--physiology
Oncogenic Viruses--pathogenicity
Proteomics--methods
Publication Types: Lectures
Webcasts
Rights: This is a work of the United States Government.
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NLM Classification: QU 375
NLM ID: 101470348
CIT Live ID: 6279
Permanent link: https://videocast.nih.gov/launch.asp?14344