Results 41 to 50 of about 180,383 (183)

Structure-functional Characterization of Mammalian Redox Proteins: Methionine sulfoxide reductase B1 (MsrB1), Glutaredoxin domain (Grx) of TGR, and Thioredoxin (Trx) [PDF]

open access: yes, 2013
This thesis was written at the Department of Biotechnology of Norwegian University of Science and Technology (NTNU) and made as a completion of the three-year PhD program.
Dobrovolska, Olena
core   +1 more source

Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior

open access: yesAntioxidants, 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   +4 more
doaj   +1 more source

Protein Repair and Degradation during Aging

open access: yesThe 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

Characterization of the Methionine Sulfoxide Reductases of Schistosoma mansoni [PDF]

open access: yesJournal of Parasitology, 2009
Schistosomiasis, also known as Bilharzia, is an infectious disease caused by several species of Schistosoma. Twenty million individuals suffer severe symptoms and 200,000 people die annually from the disease. The host responds to the presence of S. mansoni by producing reactive oxygen species that cause oxidative stress.
Tolulope T, Oke   +2 more
openaire   +2 more sources

The role of methionine sulfoxide reductase in redox signaling. [PDF]

open access: yesJ Biol Chem, 2012
This letter concerns the article published recently by Lim et al. (1). The mechanism of methionine sulfoxide reductases begins with formation of a sulfenic acid on the catalytic Cys. Most of the methionine sulfoxide reductases (Msr) then form only one intradisulfide bond via the attack of a recycling Cys.
Branlant G.
europepmc   +4 more sources

Myristoylated methionine sulfoxide reductase A is a late endosomal protein. [PDF]

open access: yesJ Biol Chem, 2018
Methionine residues in proteins provide antioxidant defense by reacting with oxidizing species, which oxidize methionine to methionine sulfoxide. Reduction of the sulfoxide back to methionine is catalyzed by methionine sulfoxide reductases, essential for protection against oxidative stress. The nonmyristoylated form of methionine sulfoxide reductase A (
Lim JM, Lim JC, Kim G, Levine RL.
europepmc   +4 more sources

Methionine Sulfoxide Reductases Contribute to Anaerobic Fermentative Metabolism in Bacillus cereus

open access: yesAntioxidants, 2021
Reversible oxidation of methionine to methionine sulfoxide (Met(O)) is a common posttranslational modification occurring on proteins in all organisms under oxic conditions.
Catherine Duport   +4 more
doaj   +1 more source

Stereospecific oxidation of calmodulin by methionine sulfoxide reductase A. [PDF]

open access: yesFree Radic Biol Med, 2013
Methionine sulfoxide reductase A has long been known to reduce S-methionine sulfoxide, both as a free amino acid and within proteins. Recently the enzyme was shown to be bidirectional, capable of oxidizing free methionine and methionine in proteins to S-methionine sulfoxide.
Lim JC, Kim G, Levine RL.
europepmc   +4 more sources

Defective protein repair under methionine sulfoxide A deletion drives autophagy and ARE-dependent gene transcription

open access: yesRedox Biology, 2018
Objective: Reduction of oxidized methionines is emerging as a major protein repair pathway. The lack of methionine sulfoxide reductase A (MsrA) exacerbates cardiovascular disease phenotypes driven by increased oxidative stress.
Steven M. Pennington   +7 more
doaj   +1 more source

Functions and evolution of selenoprotein methionine sulfoxide reductases

open access: yesBiochimica et Biophysica Acta (BBA) - General Subjects, 2009
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. MsrA and MsrB are responsible for the reduction of methionine-S-sulfoxide and methionine-R-sulfoxide residues in proteins, respectively, whereas fRMsr reduces free ...
Cheon Lee, Byung   +3 more
openaire   +3 more sources

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