Results 41 to 50 of about 2,318 (179)

Peroxiredoxin 2: An Important Element of the Antioxidant Defense of the Erythrocyte

open access: yesAntioxidants, 2023
Peroxiredoxin 2 (Prdx2) is the third most abundant erythrocyte protein. It was known previously as calpromotin since its binding to the membrane stimulates the calcium-dependent potassium channel.
Izabela Sadowska-Bartosz   +1 more
doaj   +1 more source

Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin, [PDF]

open access: yesBiochemistry, 2005
Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. The reduction of the cysteine sulfinic acid moiety within the active site of the Prx by Srx involves novel sulfur chemistry and the use of ATP and Mg(2+).
Thomas J, Jönsson   +4 more
openaire   +2 more sources

Cysteine Specific Targeting of the Functionally Distinct Peroxiredoxin and Glutaredoxin Proteins by the Investigational Disulfide BNP7787

open access: yesMolecules, 2015
Glutaredoxin (Grx), peroxiredoxin (Prx), and thioredoxin (Trx) are redoxin family proteins that catalyze different types of chemical reactions that impact cell growth and survival through functionally distinct intracellular pathways.
Aulma R. Parker   +10 more
doaj   +1 more source

Molecular and functional characterization of sulfiredoxin homologs from higher plants [PDF]

open access: yesCell Research, 2006
By reducing cysteine-sulfinic acid in oxidized peroxiredoxin, sulfiredoxin (Srx) plays an important role in oxidation stress resistance in yeast and human cells. Here, we report the first molecular and functional characterization of Srx homolog from higher plants.
Xian Peng, Liu   +6 more
openaire   +2 more sources

Piecing Together How Peroxiredoxins Maintain Genomic Stability

open access: yesAntioxidants, 2018
Peroxiredoxins, a highly conserved family of thiol oxidoreductases, play a key role in oxidant detoxification by partnering with the thioredoxin system to protect against oxidative stress.
James D. West   +4 more
doaj   +1 more source

Synergistic effects of methyl 2-cyano-3,11-dioxo-18beta-olean-1,-12-dien-30-oate and erlotinib on erlotinib-resistant non-small cell lung cancer cells

open access: yesJournal of Pharmaceutical Analysis, 2021
Non-small cell lung cancer (NSCLC) is often characterized by an underlying mutation in the epidermal growth factor receptor (EGFR), contributing to aggressive metastatic disease.
Ebony Nottingham   +8 more
doaj   +1 more source

Upregulation of Mitochondrial Redox Sensitive Proteins in LPS-Treated Stefin B-Deficient Macrophages

open access: yesCells, 2019
Stefin B (cystatin B) is an intracellular inhibitor of cysteine cathepsins and mutations in the stefin B gene, resulting in the development of Unverricht−Lundborg disease, which is a form of myoclonic epilepsy. It was suggested that a key mechanism
Mojca Trstenjak Prebanda   +3 more
doaj   +1 more source

Probing the mechanism of the peroxiredoxin decamer interaction with its reductase sulfiredoxin from the single molecule to the solution scale.

open access: yesNanoscale Horizons, 2022
Peroxiredoxins from the Prx1 subfamily (Prx) are highly regulated multifunctional proteins involved in oxidative stress response, redox signaling and cell protection. Prx is a homodimer that associates into a decamer.
A. Beaussart   +7 more
semanticscholar   +1 more source

Sulfiredoxin Promotes Cancer Cell Invasion through Regulation of the miR143-Fascin Axis

open access: yesMolecular and Cellular Biology, 2022
Intracellular antioxidant enzymes are critical for maintenance of redox homeostasis, but whether and how they contribute to the malignancy of cancer cells remains poorly understood.
Hong Jiang   +7 more
semanticscholar   +1 more source

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