V
Valeria C. Culotta
Researcher at Johns Hopkins University
Publications - 137
Citations - 17325
Valeria C. Culotta is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Superoxide dismutase & Saccharomyces cerevisiae. The author has an hindex of 70, co-authored 134 publications receiving 16223 citations. Previous affiliations of Valeria C. Culotta include Johns Hopkins University School of Medicine & Washington University in St. Louis.
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Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase.
TL;DR: Results indicate that intracellular [Cu]free is limited to less than one free copper ion per cell and suggest that a pool of free copper ions is not used in physiological activation of metalloenzymes.
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Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
Su Ju Lin,Matt Kaeberlein,Alex A. Andalis,Lori A. Sturtz,Pierre-Antoine Defossez,Pierre-Antoine Defossez,Valeria C. Culotta,Gerald R. Fink,Leonard Guarente +8 more
TL;DR: In this paper, a model of calorie restriction in yeast Saccharomyces cerevisiae was established and it was shown that the shunting of carbon metabolism toward the mitochondrial tricarboxylic acid cycle and the concomitant increase in respiration play a central part in this process.
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The Copper Chaperone for Superoxide Dismutase
Valeria C. Culotta,Leo W.J. Klomp,Jeffrey Strain,Ruby Leah B. Casareno,Bernhard Krems,Jonathan D. Gitlin +5 more
TL;DR: It is demonstrated here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copperchaperone for SOD).
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Metallochaperones, an intracellular shuttle service for metal ions.
TL;DR: The most recent advances in the understanding of copper metallochaperones are reviewed and mechanisms that may be relevant to other essential, yet potentially toxic, metal ions are discussed.
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A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage.
TL;DR: It is demonstrated that Cu,Zn-SOD1 in the mitochondria appears important for reactive oxygen physiology and may have critical implications for SOD1 mutations linked to the fatal neurodegenerative disorder, amyotrophic lateral sclerosis.