L
Linda M. Benson
Researcher at Mayo Clinic
Publications - 95
Citations - 3153
Linda M. Benson is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Mass spectrometry & Capillary electrophoresis. The author has an hindex of 32, co-authored 93 publications receiving 3023 citations. Previous affiliations of Linda M. Benson include Universidade Nova de Lisboa & University of Rochester.
Papers
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Journal ArticleDOI
Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia
Jiri Adamec,Frank Rusnak,Whyte G. Owen,Stephen Naylor,Linda M. Benson,A. Marquis Gacy,Grazia Isaya +6 more
TL;DR: It is proposed that iron-dependent self-assembly of recombinant mYfh1p reflects a physiological role for frataxin in mitochondrial iron sequestration and bioavailability and is essential for mitochondrial iron homeostasis and protection from iron-induced formation of free radicals.
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Recombinant Mycobacterium tuberculosis KatG(S315T) Is a Competent Catalase-Peroxidase with Reduced Activity toward Isoniazid
Nancy L. Wengenack,James R. Uhl,Allison L. St. Amand,Andy J. Tomlinson,Linda M. Benson,Stephen Naylor,Bruce C. Kline,Frank R. Cockerill,Frank Rusnak +8 more
TL;DR: It is demonstrated that KatG(S315T), as expressed in E. coli, is a competent catalase-peroxidase that exhibits a reduced ability to metabolize isoniazid, and high-performance liquid chromatography analysis showed that wild-type KatG was more efficient than KatG
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Preconcentration and microreaction technology on-line with capillary electrophoresis
TL;DR: In this article, the potential merits of analyte concentrator and membrane preconcentration technologies are discussed, and the future developments are discussed for analyte separation by capillary electrophoresis.
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Neelaredoxin, an Iron-binding Protein from the Syphilis Spirochete, Treponema pallidum, Is a Superoxide Reductase
Tijana Jovanović,Carla Ascenso,Karsten R. O. Hazlett,Robert A. Sikkink,Carsten Krebs,Robert D. Litwiller,Linda M. Benson,Isabel Moura,José J. G. Moura,Justin D. Radolf,Boi Hanh Huynh,Stephen Naylor,Frank Rusnak +12 more
TL;DR: This finding, the first description of a T. pallidum iron-binding protein, indicates that the syphilis spirochete copes with oxidative stress via a primitive mechanism, which, thus far, has not been described in pathogenic bacteria.
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The Anticancer Agent Chaetocin Is a Competitive Substrate and Inhibitor of Thioredoxin Reductase
TL;DR: It is reported that chaetocin is a competitive and selective substrate for the oxidative stress mitigation enzyme thioredoxin reductase-1 (TrxR1) with lower K(m) than the TrxR2 native substrate thiOREDoxin (TrX), thereby attenuating reduction of the critical downstream ROS remediation substrate Trx at achieved intracellular concentrations.