Results 21 to 30 of about 91,937 (143)
Loss of methionine sulfoxide reductases increases resistance to oxidative stress [PDF]
Rodney L Levine +2 more
exaly +2 more sources
Functions and evolution of selenoprotein methionine sulfoxide reductases. [PDF]
Methionine sulfoxide reductases (Msrs) are thiol-dependent enzymes which catalyze conversion of methionine sulfoxide to methionine. Three Msr families, MsrA, MsrB, and fRMsr, are known.
Lee BC, Dikiy A, Kim HY, Gladyshev VN.
europepmc +2 more sources
Compartmentalization and regulation of mitochondrial function by methionine sulfoxide reductases in yeast. [PDF]
Elevated levels of reactive oxygen species can damage proteins. Sulfur-containing amino acid residues, cysteine and methionine, are particularly susceptible to such damage.
Kaya A +7 more
europepmc +2 more sources
The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression
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 +14 more
wiley +1 more source
Methionine Redox Homeostasis in Protein Quality Control
Bacteria live in different environments and are subject to a wide variety of fluctuating conditions. During evolution, they acquired sophisticated systems dedicated to maintaining protein structure and function, especially during oxidative stress.
Laurent Aussel, Benjamin Ezraty
doaj +1 more source
Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase
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 +9 more
doaj +1 more source
Methionine residues are particularly sensitive to oxidation by reactive oxygen or chlorine species (ROS/RCS), leading to the appearance of methionine sulfoxide in proteins.
Alexandra Vergnes +9 more
doaj +1 more source
Methionine sulfoxide reductases are key enzymes in the cellular oxidative defense system. Reactive oxygen species oxidize methionine residues to methionine sulfoxide, and the methionine sulfoxide reductases catalyze their reduction back to methionine. We
Venkata R. Sabbasani (1930561) +3 more
core +1 more source
Sacrificial Methionine Residues Protect Active-Site Histidines From Oxidation. [PDF]
Methionine residues near the active site of human ribonuclease 1 act as sacrificial antioxidants, protecting catalytic histidines from oxidation by reactive oxygen species (ROS). Chemoselective capping with an oxaziridine and total chemical synthesis with a sulfur‐free norleucine isostere each render the enzyme more susceptible to oxidative ...
Wralstad EC +6 more
europepmc +2 more sources
Redox controls RecA protein activity via reversible oxidation of its methionine residues
Reactive oxygen species (ROS) cause damage to DNA and proteins. Here, we report that the RecA recombinase is itself oxidized by ROS. Genetic and biochemical analyses revealed that oxidation of RecA altered its DNA repair and DNA recombination activities.
Camille Henry +10 more
doaj +1 more source

