The Antioxidant Enzyme Methionine Sulfoxide Reductase A (MsrA) Interacts with Jab1/CSN5 and Regulates Its Function [PDF]
Antioxidants, 2020 Methionine sulfoxide (MetO) is an oxidative posttranslational modification that primarily occurs under oxidative stress conditions, leading to alteration of protein structure and function.
Beichen Jiang +5 more
doaj +2 more sources
Novel Mechanism for Scavenging of Hypochlorite Involving a Periplasmic Methionine-Rich Peptide and Methionine Sulfoxide Reductase [PDF]
mBio, 2015 Reactive chlorine species (RCS) defense mechanisms are important for bacterial fitness in diverse environments. In addition to the anthropogenic use of RCS in the form of bleach, these compounds are also produced naturally through photochemical reactions
Ryan A. Melnyk +9 more
doaj +2 more sources
Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling
Antioxidants, 2018 Oxidation of methionine (Met) leads to the formation of two S- and R-diastereoisomers of Met sulfoxide (MetO) that are reduced back to Met by methionine sulfoxide reductases (MSRs), A and B, respectively.
Pascal Rey, Lionel Tarrago
doaj +3 more sources
Methionine biosynthetic genes and methionine sulfoxide reductase A are required for Rhizoctonia solani AG1‐IA to cause sheath blight disease in rice [PDF]
Microbial BiotechnologyRhizoctonia solani is a polyphagous necrotrophic fungal pathogen that causes sheath blight disease in rice. It deploys effector molecules as well as carbohydrate‐active enzymes and enhances the production of reactive oxygen species for killing host ...
Joyati Das +4 more
doaj +2 more sources
Role of ClpX and MsrA/B in the Oxidative and Cell Wall Stress Response in Bacillus anthracis Sterne
MicrobiologyOpenClpX functions as a component of the ClpXP protease, a conserved intracellular protease that regulates protein turnover, stress responses, and virulence in multiple bacterial species.
Aeron B. Pennington +5 more
doaj +2 more sources
Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii. [PDF]
PLoS ONE, 2015 Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution.
Eun Hye Lee +6 more
doaj +2 more sources
Monitoring of Methionine Sulfoxide Content and Methionine Sulfoxide Reductase Activity. [PDF]
Methods Mol Biol, 2018 The sulfur-containing amino acid methionine (Met) plays critical roles in protein synthesis, methylation, and sulfur metabolism. Both in its free form and in the form of an amino acid residue, it can be oxidized to the R and S diastereomers of methionine sulfoxide (MetO).
Tarrago L +3 more
europepmc +4 more sources
A study into the cobalamin-dependent methionine synthase reactivation mechanism in corynebacterium glutamicum [PDF]
, 2009 PhDMethionine is one of the seven essential amino-acids for humans and is also used in feed supplements, predominantly for poultry and felines. Thus there is commercial interest in producing this nutrient. The final step in the biological synthesis of
Burton-Smith, Raymond Nathaniel
core +4 more sources
Plant methionine sulfoxide reductase A and B multigenic families
Photosynthesis Research, 2006 International audienceMethionine oxidation to methionine sulfoxide (MetSo), which results in modification of activity and conformation for many proteins, is reversed by an enzyme present in most organisms and termed as methionine sulfoxide reductase (MSR)
Tarrago, Lionel +3 more
core +5 more sources
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 +14 more
wiley +1 more source