P
P. John Hart
Researcher at University of Texas Health Science Center at San Antonio
Publications - 114
Citations - 7310
P. John Hart is an academic researcher from University of Texas Health Science Center at San Antonio. The author has contributed to research in topics: SOD1 & Superoxide dismutase. The author has an hindex of 44, co-authored 113 publications receiving 6681 citations. Previous affiliations of P. John Hart include St. Mary's University & Veterans Health Administration.
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Journal ArticleDOI
Misfolded CuZnSOD and amyotrophic lateral sclerosis.
TL;DR: Some of the properties of both wild-type and mutant CuZnSOD proteins are reviewed, suggests how these properties may be relevant to these two hypotheses, and proposes that these two hypothesis are not necessarily mutually exclusive.
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Amyloid-like Filaments and Water-filled Nanotubes Formed by SOD1 Mutant Proteins Linked to Familial ALS
Jennifer Stine Elam,Alexander B. Taylor,Richard W. Strange,Svetlana V. Antonyuk,Peter A. Doucette,Jorge A. Rodriguez,S. Samar Hasnain,Lawrence J. Hayward,Joan Selverstone Valentine,Todd O. Yeates,P. John Hart +10 more
TL;DR: It is shown that metal-deficient, pathogenic S OD1 mutant proteins crystallize in three different crystal forms, all of which reveal higher-order assemblies of aligned β-sheets, which could be a toxic property common to mutants of SOD1 linked to FALS.
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Sequence-specific recognition and cooperative dimerization of N-terminal aromatic peptides in aqueous solution by a synthetic host.
TL;DR: The peptide sequence selectivity and positively cooperative dimerization reported here are, to the best of the authors' knowledge, unprecedented for synthetic hosts in aqueous solution.
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Molecular recognition of insulin by a synthetic receptor.
Jordan M. Chinai,Alexander B. Taylor,Lisa M. Ryno,Nicholas D. Hargreaves,Christopher A. Morris,P. John Hart,Adam R. Urbach +6 more
TL;DR: Findings suggest that site-selective recognition is based on the properties inherent to a protein terminus, including the unique chemical epitope presented by the terminal residue and the greater freedom of the terminus to unfold, like the end of a ball of string, to accommodate binding.
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Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease.
TL;DR: The majority of pedigrees in which patients exhibit reproducibly short disease durations are associated with mutations that show a high inherent propensity to induce aggregation of SOD1, and this shows that all ALS-associated mutations in S OD1 increase the inherent aggregation propensity of the protein.