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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Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice.
TL;DR: The findings provide a biochemical basis for a pathological hallmark of this disease; namely, incorrect disulfide cross-linking of the immature, misfolded mutant proteins leads to insoluble aggregates.
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Polymer-caged lipsomes: a pH-responsive delivery system with high stability.
TL;DR: These modified liposomes possess surface-active carboxylate groups that can be cross-linked with telechelic 2,2‘-(ethylenedioxy)bis(ethylamine) linkers, resulting in polymer-caged liposome (PCLs) that are highly stable and have tunable pH-sensitive responses.
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Cu(I) Recognition Via Cation-Pi and Methionine Interactions in Cusf.
Yi Xue,Anna V Davis,Gurusamy Balakrishnan,Jay Stasser,Benjamin M. Staehlin,Pamela J. Focia,Thomas G. Spiro,James E. Penner-Hahn,Thomas V. O'Halloran +8 more
TL;DR: It is shown that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan, affording mechanisms for control of adventitious metal redox and substitution chemistry.
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Zinc Availability Regulates Exit from Meiosis in Maturing Mammalian Oocytes
TL;DR: Major changes in the zinc physiology of the mammalian oocyte as it matures and initiates embryonic development are described and implicate the zinc bolus acquired during meiotic maturation as an important part of the maternal legacy to the embryo.
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DNA-bend modulation in a repressor-to-activator switching mechanism.
TL;DR: It is shown that MerR bends DNA towards itself in a manner similar to the bacterial catabolite-activator protein CAP, namely at two loci demarked by DNase I sensitivity, and that the activator conformation, Hg–MerR, relaxes these bends.