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Natalie Lassen
Researcher at Anschutz Medical Campus
Publications - 15
Citations - 658
Natalie Lassen is an academic researcher from Anschutz Medical Campus. The author has contributed to research in topics: Oxidative stress & Aldehyde dehydrogenase. The author has an hindex of 8, co-authored 15 publications receiving 604 citations. Previous affiliations of Natalie Lassen include Denver Health Medical Center & University of Colorado Boulder.
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Journal ArticleDOI
Multiple and Additive Functions of ALDH3A1 and ALDH1A1: CATARACT PHENOTYPE AND OCULAR OXIDATIVE DAMAGE IN Aldh3a1(−/−)/Aldh1a1(−/−) KNOCK-OUT MICE
Natalie Lassen,J. Bronwyn Bateman,Tia Estey,Jer R. Kuszak,David W. Nees,Joram Piatigorsky,Gregg Duester,Brian J. Day,Jie Huang,Lisa M. Hines,Vasilis Vasiliou +10 more
TL;DR: The hypothesis that corneal ALDH3A1 and lens ALDH1A1 protect the eye against cataract formation via nonenzymatic and enzymatic (detoxification) functions is supported.
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ALDH3A1: a corneal crystallin with diverse functions.
TL;DR: The multiple roles of ALDH3A1 against oxidative stress in addition to its contributions to the optical properties of the cornea are consistent with the idea that this specialized protein performs diverse biological functions as do the lens crystallins.
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The role of corneal crystallins in the cellular defense mechanisms against oxidative stress
TL;DR: The discussion of the antioxidant defenses of the cornea is extended to include these highly expressed corneal crystallins and address their specific capacities to minimize oxidative damage.
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Antioxidant function of corneal ALDH3A1 in cultured stromal fibroblasts.
Natalie Lassen,Aglaia Pappa,William Black,James V. Jester,Brian J. Day,Elysia Min,Vasilis Vasiliou +6 more
TL;DR: The results suggest that ALDH3A1 may act to protect corneal cells against cellular oxidative damage by metabolizing toxic lipid peroxidation products, maintaining cellular GSH levels and redox balance, and operating as an antioxidant.
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Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2.
TL;DR: Zebrafish ALDH2 is catalytically active and efficiently oxidizes acetaldehyde and propionaldehyde and indicates that zebrafish is a suitable model for studying ethanol metabolism and, therefore, toxicity.