Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 218,261,198 papers from all fields of science
Search
Sign In
Create Free Account
peptide-methionine (R)-S-oxide reductase activity
Known as:
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming] activity
, methionine S-oxide reductase (R-form oxidizing) activity
, protein-methionine-R-oxide reductase activity
Expand
Catalysis of the reaction: peptide-L-methionine + H(2)O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
1 relation
Broader (1)
methionine sulfoxide reductase activity
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2008
Review
2008
Selenoproteins and maternal nutrition.
A. Pappas
,
E. Zoidis
,
Peter F Surai
,
G. Zervas
Comparative Biochemistry and Physiology Part B…
2008
Corpus ID: 23700665
Highly Cited
2008
Highly Cited
2008
Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU.
Poney Chiang
,
L. Sampaleanu
,
+4 authors
Lori L. Burrows
Microbiology
2008
Corpus ID: 21845374
Type IV pili are retractable protein fibres used by many bacterial pathogens for adherence, twitching motility, biofilm…
Expand
Highly Cited
2006
Highly Cited
2006
Group B Streptococcal Pilus Proteins Contribute to Adherence to and Invasion of Brain Microvascular Endothelial Cells
Heather C. Maisey
,
M. Hensler
,
V. Nizet
,
K. Doran
Journal of Bacteriology
2006
Corpus ID: 34764630
ABSTRACT Surface filamentous structures known as pili have been discovered recently in the gram-positive streptococcal pathogens…
Expand
Review
2005
Review
2005
Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases.
J. Moskovitz
Biochimica et Biophysica Acta
2005
Corpus ID: 25154029
Highly Cited
2005
Highly Cited
2005
The Arabidopsis Plastidic Methionine Sulfoxide Reductase B Proteins. Sequence and Activity Characteristics, Comparison of the Expression with Plastidic Methionine Sulfoxide Reductase A, and Induction…
Christina Vieira Dos Santos
,
S. Cuiné
,
N. Rouhier
,
P. Rey
Plant Physiology
2005
Corpus ID: 32825737
Two types of methionine (Met) sulfoxide reductases (Msr) catalyze the reduction of Met sulfoxide (MetSO) back to Met. MsrA, well…
Expand
Highly Cited
2002
Highly Cited
2002
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
W. Lowther
,
H. Weissbach
,
Frantzy Etienne
,
N. Brot
,
Brian W. Matthews
Nature Structural Biology
2002
Corpus ID: 37006950
Methionine sulfoxide reductases (Msr) protect against oxidative damage that can contribute to cell death. The tandem Msr domains…
Expand
Highly Cited
2002
Highly Cited
2002
Reaction Mechanism, Evolutionary Analysis, and Role of Zinc in Drosophila Methionine-R-sulfoxide Reductase*
Abhilash Kumar
,
A. Koc
,
R. Cerny
,
V. Gladyshev
Journal of Biological Chemistry
2002
Corpus ID: 16629828
Methionine residues in proteins are susceptible to oxidation, and the resulting methionine sulfoxides can be reduced back to…
Expand
Highly Cited
2002
Highly Cited
2002
Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity.
J. Moskovitz
,
V. Singh
,
J. Requena
,
B. Wilkinson
,
R. Jayaswal
,
E. Stadtman
Biochemical and Biophysical Research…
2002
Corpus ID: 22026979
Many organisms have been shown to possess a methionine sulfoxide reductase (MsrA), exhibiting high specificity for reduction the…
Expand
Highly Cited
1999
Highly Cited
1999
Diastereoselective reduction of protein‐bound methionine sulfoxide by methionine sulfoxide reductase
V. Sharov
,
D. Ferrington
,
T. Squier
,
C. Schöneich
FEBS Letters
1999
Corpus ID: 34771043
Highly Cited
1992
Highly Cited
1992
Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
Marc Bally
,
A. Filloux
,
M. Akrim
,
Genevieve Ball
,
A. Lazdunski
,
J. Tommassen
Molecular Microbiology
1992
Corpus ID: 7311011
The xcp genes are required for the secretion of most extracellular proteins by Pseudomonas aeruginosa. The products of these…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE