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Matthew Hirschey

Associate Professor of Medicine
Medicine, Endocrinology, Metabolism, and Nutrition
104775, Room 50-201, Durham, NC 27701
300 N. Duke Street, 50-201, Durham, NC 27701

Featured Works


SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production.

Journal article Cell Metab · December 1, 2010 Featured Publication The mitochondrial sirtuin SIRT3 regulates metabolic homeostasis during fasting and calorie restriction. We identified mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 (HMGCS2) as an acetylated protein and a possible target of SIRT3 in a proteomics s ... Full text Link to item Cite

Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation.

Journal article Cell Metab · December 1, 2010 Featured Publication A major cause of aging and numerous diseases is thought to be cumulative oxidative stress, resulting from the production of reactive oxygen species (ROS) during respiration. Calorie restriction (CR), the most robust intervention to extend life span and ame ... Full text Link to item Cite

SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation.

Journal article Nature · March 4, 2010 Featured Publication Sirtuins are NAD(+)-dependent protein deacetylases. They mediate adaptive responses to a variety of stresses, including calorie restriction and metabolic stress. Sirtuin 3 (SIRT3) is localized in the mitochondrial matrix, where it regulates the acetylation ... Full text Link to item Cite

Acetylation of mitochondrial proteins.

Journal article Methods Enzymol · 2009 Featured Publication Sirtuins (SIRT1-SIRT7) are a family of NAD(+)-dependent protein deacetylases that regulate cell survival, metabolism, and longevity. SIRT3 is localized to the mitochondria where it deacetylates several key metabolic enzymes: acetylcoenzyme A synthetase, gl ... Full text Link to item Cite