Results 21 to 30 of about 7,593 (119)

The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression

Hepatology, EarlyView., 2022
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro, Rut Espinosa‐Sotelo, Eva Crosas‐Molist, Macarena Herranz‐Itúrbide, Daniel Caballero‐Díaz, Ania Alay, Xavier Solé, Emilio Ramos, Teresa Serrano, María L. Martínez‐Chantar, Ulla G. Knaus, José M. Cuezva, Antonio Zorzano, Esther Bertran, Isabel Fabregat   +14 more
wiley   +1 more source

Methionine sulfoxide reductases are essential for virulence of Salmonella typhimurium. [PDF]

PLoS ONE, 2011
Production of reactive oxygen species represents a fundamental innate defense against microbes in a diversity of host organisms. Oxidative stress, amongst others, converts peptidyl and free methionine to a mixture of methionine-S- (Met-S-SO) and ...
Luisa A Denkel, Sarah A Horst, Syed Fazle Rouf, Vera Kitowski, Oliver M Böhm, Mikael Rhen, Timo Jäger, Franz-Christoph Bange   +7 more
doaj   +1 more source

Research Progress on Methionine Sulfoxide Reductase and Its Regulation on the Adversity Stress of Fruit and Vegetable

Shipin gongye ke-ji, 2022
Methionine sulfoxide reductase (Msr) is a kind of antioxidant enzyme that can scavenge free radicals and repair oxidized proteins by reducing methionine sulfoxide to active methionine.
Xiaodong FU, Xiuming ZHAO, Jiong LIU, Xinhua ZHANG, Fujun LI, Xiao'an LI   +5 more
doaj   +1 more source

L-Methionine Protects against Oxidative Stress and Mitochondrial Dysfunction in an In Vitro Model of Parkinson’s Disease

Antioxidants, 2021
Methionine is an aliphatic, sulfur-containing, essential amino acid that has been demonstrated to have crucial roles in metabolism, innate immunity, and activation of endogenous antioxidant enzymes, including methionine sulfoxide reductase A/B and the ...
Mariano Catanesi, Laura Brandolini, Michele d’Angelo, Elisabetta Benedetti, Maria Grazia Tupone, Margherita Alfonsetti, Enrico Cabri, Daniela Iaconis, Maddalena Fratelli, Annamaria Cimini, Vanessa Castelli, Marcello Allegretti   +11 more
doaj   +1 more source

Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase

Antioxidants, 2020
In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO.
Lionel Tarrago, Sandrine Grosse, David Lemaire, Laetitia Faure, Mathilde Tribout, Marina I. Siponen, Mila Kojadinovic-Sirinelli, David Pignol, Pascal Arnoux, Monique Sabaty   +9 more
doaj   +1 more source

The Campylobacter concisus BisA protein plays a dual role: oxide-dependent anaerobic respiration and periplasmic methionine sulfoxide repair

mBio, 2023
Campylobacter concisus, an emerging pathogen found throughout the human oral-gastrointestinal tract, is able to grow under microaerobic or anaerobic conditions; in the latter case, N- or S-oxides could be used as terminal electron acceptors (TEAs ...
Stéphane L. Benoit, Robert J. Maier
doaj   +1 more source

Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior

Antioxidants, 2018
Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown.
Méry Marimoutou, Danielle A. Springer, Chengyu Liu, Geumsoo Kim, Rodney L. Levine   +4 more
doaj   +1 more source

Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide. [PDF]

PLoS Pathogens, 2017
Vibrio cholerae is a diarrheal pathogen that induces accumulation of lipid droplets in enterocytes, leading to lethal infection of the model host Drosophila melanogaster. Through untargeted lipidomics, we provide evidence that this process is the product
Audrey S Vanhove, Saiyu Hang, Vidhya Vijayakumar, Adam Cn Wong, John M Asara, Paula I Watnick   +5 more
doaj   +1 more source

Protein Repair and Degradation during Aging

The Scientific World Journal, 2002
Cellular aging is characterized by a build-up of oxidatively modified proteins. The steady-state level of oxidized proteins depends on the balance between the rate of protein oxidative damage and the rates of protein degradation and repair.
Bertrand Friguet
doaj   +1 more source

Selenium and the Methionine Sulfoxide Reductase System

Molecules, 2009
Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines.
Jackob Moskovitz, Derek B. Oien
doaj   +1 more source