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Keap1-Nrf2 Pathway Regulates ALDH and Contributes to Radioresistance in Breast Cancer Stem Cells

open access: yesCells, 2021
Tumor recurrence after radiotherapy due to the presence of breast cancer stem cells (BCSCs) is a clinical challenge, and the mechanism remains unclear.
Dinisha Kamble   +3 more
doaj   +1 more source

Highly Polymorphic Materials and Dissolution Behaviour: The Peculiar Case of Rifaximin

open access: yesPharmaceutics, 2022
Rifaximin is a locally acting antibiotic practically insoluble in water. It presents several crystal phases characterized by different degrees of hydration. The aim of this work is to investigate the dissolution behaviour of rifaximin α, β, and amorphous
Annalisa Bianchera   +4 more
doaj   +1 more source

Redox Proteomics [PDF]

open access: yesAntioxidants & Redox Signaling, 2012
Proteins are major targets of reactive oxygen and nitrogen species (ROS/RNS) and numerous post-translational, reversible or irreversible modifications have been characterized, which may lead to a change in the structure and/or function of the oxidized protein.
D. A. Butterfield, I. Dalle-Donne
openaire   +2 more sources

Redox controls UPR to control redox [PDF]

open access: yesJournal of Cell Science, 2014
In many physiological contexts, intracellular reduction–oxidation (redox) conditions and the unfolded protein response (UPR) are important for the control of cell life and death decisions. UPR is triggered by the disruption of endoplasmic reticulum (ER) homeostasis, also known as ER stress. Depending on the duration and severity of the disruption, this
Eletto D   +3 more
openaire   +3 more sources

miR-140-5p Attenuates Hypoxia-Induced Breast Cancer Progression by Targeting Nrf2/HO-1 Axis in a Keap1-Independent Mechanism

open access: yesCells, 2021
Hypoxia and oxidative stress significantly contribute to breast cancer (BC) progression. Although hypoxia-inducible factor 1α (Hif-1α) is considered a key effector of the cellular response to hypoxia, nuclear factor erythroid 2–related factor 2 (Nrf2), a
Megharani Mahajan, Sandhya Sitasawad
doaj   +1 more source

The Redox Proteome [PDF]

open access: yesJournal of Biological Chemistry, 2013
The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control
Go, Young-Mi, Jones, Dean P.
openaire   +2 more sources

Understanding Cysteine Chemistry Using Conventional and Serial X-ray Protein Crystallography

open access: yesCrystals, 2022
Proteins that use cysteine residues for catalysis or regulation are widely distributed and intensively studied, with many biomedically important examples.
Nathan Smith, Mark A. Wilson
doaj   +1 more source

The C-terminal region of the oxidoreductase MIA40 stabilizes its cytosolic precursor during mitochondrial import

open access: yesBMC Biology, 2020
Background The mitochondrial intermembrane space (IMS) is home to proteins fulfilling numerous essential cellular processes, particularly in metabolism and mitochondrial function.
Lena Maria Murschall   +7 more
doaj   +1 more source

Cross-linking between cysteine and lysine, tryptophan or tyrosine in peptides and proteins treated with hypochlorous acid and other reactive halogens

open access: yesRedox Biochemistry and Chemistry, 2023
Cysteine residues are the most favored targets for oxidation by hypochlorous acid and other reactive halogen species. The end-products of cysteine oxidation are usually considered to be reversibly formed disulfides and the more highly oxidized sulfinic ...
Nicholas J. Magon   +3 more
doaj   +1 more source

The Redox Code [PDF]

open access: yesAntioxidants & Redox Signaling, 2015
Significance: The redox code is a set of principles that defines the positioning of the nicotinamide adenine dinucleotide (NAD, NADP) and thiol/disulfide and other redox systems as well as the thiol redox proteome in space and time in biological systems.
Jones, Dean P., Sies, Helmut
openaire   +2 more sources

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