S
Sheila M. Healy
Researcher at University of Arizona
Publications - 9
Citations - 695
Sheila M. Healy is an academic researcher from University of Arizona. The author has contributed to research in topics: Arsenite & Arsenate. The author has an hindex of 7, co-authored 9 publications receiving 680 citations.
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Journal ArticleDOI
Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily.
Robert A. Zakharyan,Adriana Sampayo-Reyes,Sheila M. Healy,George Tsaprailis,Philip G. Board,Daniel C. Liebler,H V Aposhian +6 more
TL;DR: It is proposed that MMA(V) reductase and hGSTO 1-1 are identical proteins, which is 100% identical, over 92% of sequence that was analyzed, with the recently discovered human glutathione-S-transferase Omega class hG STO1-1.
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DMPS-arsenic challenge test. II. Modulation of arsenic species, including monomethylarsonous acid (MMAIII), excreted in human urine.
H. Vasken Aposhian,Baoshan Zheng,Mary M. Aposhian,X. Chris Le,Mariano E. Cebrián,William R. Cullen,Robert A. Zakharyan,Mingsheng Ma,Richard C. Dart,Zhai Cheng,Zhai Cheng,Paul Andrewes,Luke Yip,Gerald F. O'Malley,R M Maiorino,Wayne A. Van Voorhies,Sheila M. Healy,Allison Titcomb +17 more
TL;DR: The experimental results support the hypothesis that DMPS competes with endogenous ligands for MMA(III), forming a DMPS-MMA complex that is readily excreted in the urine and points out the need for studying the biochemical toxicology of MMA( III).
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Enzymatic Methylation of Arsenic Compounds: V. Arsenite Methyltransferase Activity in Tissues of Mice
TL;DR: The specific activity of this critical enzyme for arsenite biotransformation was determined by incubating liver, testis, kidney, or lung cytosol of male B6C3F1 mice with sodium arsenite and S-[methyl-3H]adenosyl-L-methionine and measuring the formation of [methyl- 3H]monomethylarsonate.
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Monomethylarsonic acid reductase and monomethylarsonous acid in hamster tissue.
TL;DR: The first-time identification of MMA( III) and DMA(III) in liver after arsenate exposure indicates that the significance of arsenic species in mammalian tissue needs to be re-examined and re-evaluated with respect to their role in the toxicity and carcinogenicity of inorganic arsenic.
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Enzymatic methylation of arsenic compounds: IV. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig.
TL;DR: The guinea pig, like the marmoset and tamarin monkeys and unlike most other animals studied thus far, appears to be deficient as far as the enzyme activities that methylate inorganic arsenite.