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Redox proteomics tools for study of redox lesions in proteins

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David Sheehan University College Cork, Ireland

When 29 Sep, 2009 from
03:00 pm to 04:00 pm
Where Auditorium
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ITQB Seminar

 

Title: Redox proteomics tools for study of redox lesions in proteins

Speaker: David Sheehan

Affiliation: Senior Lecturer and Associate Professor, Dept Biochemistry,
University College Cork (1989-DATE)

Host: Mass Spectrometry Laboratory


Short CV David Sheehan:

BSc in Biochemistry, University College Cork (1980)
PhD in Biochemistry, Trinity College Dublin (1985)
Biotechnology industry 1985-1989
Lecturer, Senior Lecturer and Associate Professor, Dept Biochemistry,
University College Cork (1989-DATE)

Research: Enzymology of glutathione transferases; Protein biomarkers in
environmental toxicology; redox proteomics; oxidative stress in
hypertensive kidney.

Author of >80 peer-reviewed paper and numerous other publications
including 4 books.

Physical Biochemistry: Principles and Applications. D. Sheehan (Wileys,
second edition) and Two Dimensional Electrophoresis Protocols. D.
Sheehan and R. Tyther eds. (Springer), were both published in May 2009

 

Abstract:

Adaptation to aerobic metabolism was a fundamental step in biological
evolution making possible development of multicellular organisms and
changing the Earth's environment from reducing to oxidizing. This step
necessitated biology coming to terms with oxygen, its reduction
derivatives, the reactive oxygen species (ROS), and related reactive
nitrogen species (RNS) which was achieved partly by evolution of
antioxidant defences and partly by incorporating ROS into biological
signalling. When ROS levels exceed antioxidant capacity, a state of
oxidative stress ensues which is a common feature of many important
pathologies. Since proteins absorb around 70% of ROS, redox proteomics
focuses on detecting redox lesions in proteins to gain insight to both
oxidative stress and redox signaling. This presentation describes a
toolkit of approaches to a) identify proteins that are redox targets,
and b) select for sub-proteomes enriched in redox proteins targets.

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