T
Thomas V. O'Halloran
Researcher at Northwestern University
Publications - 217
Citations - 24119
Thomas V. O'Halloran is an academic researcher from Northwestern University. The author has contributed to research in topics: Zinc & Superoxide dismutase. The author has an hindex of 76, co-authored 207 publications receiving 22523 citations. Previous affiliations of Thomas V. O'Halloran include University of Birmingham & Michigan State University.
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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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Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis
TL;DR: The mechanism of zinc sensors that control metal uptake or export in Escherichia coli are determined and their response against the thermodynamically defined free zinc concentration suggests an extraordinary intracellular zinc-binding capacity.
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Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors
TL;DR: The essential transition metal ions are avidly accumulated by cells, yet they have two faces: They are put to use as required cofactors, but they also can catalyze cytotoxic reactions.
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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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Metal ion chaperone function of the soluble Cu(I) receptor Atx1.
Robert A. Pufahl,C. P. Singer,Katrina Peariso,Su Ju Lin,Paul J. Schmidt,Christoph J. Fahrni,V. Cizewski Culotta,James E. Penner-Hahn,Thomas V. O'Halloran +8 more
TL;DR: The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.