G
Garth Powis
Researcher at Discovery Institute
Publications - 195
Citations - 12010
Garth Powis is an academic researcher from Discovery Institute. The author has contributed to research in topics: Thioredoxin & Thioredoxin reductase. The author has an hindex of 57, co-authored 194 publications receiving 11475 citations. Previous affiliations of Garth Powis include University of Texas Health Science Center at Houston & Mayo Clinic.
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Journal ArticleDOI
The phosphatidylinositol-3-kinase inhibitor PX-866 overcomes resistance to the epidermal growth factor receptor inhibitor gefitinib in A-549 human non–small cell lung cancer xenografts
Nathan T. Ihle,Gillian Paine-Murrieta,Margareta Berggren,Amanda F. Baker,Wendy R. Tate,Peter Wipf,Robert T. Abraham,D. Lynn Kirkpatrick,Garth Powis +8 more
TL;DR: PX-866, a PI3-K inhibitor with selectivity for p110α, potentiates the antitumor activity of gefitinib against even large A-549 NSCL xenografts giving complete tumor growth control in the early stages of treatment.
Journal ArticleDOI
Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteins.
Garth Powis,P. L. Appel +1 more
TL;DR: Metabolism was more closely related to single-electron reduction potential than to structural features or lipid solubility of the quinones studied, and metabolism under aerobic conditions showed an increased V max and an unchanged K m, compared to metabolism under anaerobic conditions.
Journal ArticleDOI
The predicted amino acid sequence of human thioredoxin is identical to that of the autocrine growth factor human adult T-cell derived factor (ADF): Thioredoxin mRNA is elevated in some human tumors
TL;DR: The cDNA sequences of thioredoxin obtained by PCR cloning from human colon cancer cells, human lymphoblastoid cells, and human liver have been found to be identical with the cDNA sequence reported for the autocrine growth factor, human adult T-cell leukemia derived factor (ADF).
Journal ArticleDOI
Mechanisms of inhibition of the thioredoxin growth factor system by antitumor 2-imidazolyl disulfides
D. Lynn Kirkpatrick,Miles Kuperus,Marla Dowdeswell,Noelle Potier,Lynda J. Donald,Mark Kunkel,Margareta Berggren,Miguel Angulo,Garth Powis +8 more
TL;DR: The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of h Trx by the disulfide that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the Disulfides.
Book ChapterDOI
Redox signaling and the control of cell growth and death.
TL;DR: The chapter details the redox targets—ribonucleotide reductase, receptor proteins, and the transcription factors: OxyR, NF-KB/Rel, AP-1—and protein folding and degradation.