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acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
acetyl-L-methionine-NHMe + thioredoxin disulfide + H2O
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
-
FMsr is specific for the S-isomer
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
FMsr is specific for the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
the membrane-associated isozyme reduces both R- and S-stereoisomer of methionine sulfoxide in proteins
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
-
enzyme reduces L-methionine (S)-sulfoxide of the protein substrate
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, there exist MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
highest activity by enzyme MsrA, low activity by enzyme MsrA1
-
-
?
additional information
?
-
enzyme catalyzes two reductase steps. In the presence of thioredoxin, the overall rate-limiting step is associated with the thioredoxin-recycling process, and MsrA accumulates under Cys51 sulfenic acid state. Formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin
-
-
?
additional information
?
-
-
enzyme catalyzes two reductase steps. In the presence of thioredoxin, the overall rate-limiting step is associated with the thioredoxin-recycling process, and MsrA accumulates under Cys51 sulfenic acid state. Formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin
-
-
?
additional information
?
-
MsrA oxidation mechanism follows three consecutive, pH dependent steps, corresponding to the oxidation of tyrosine, tryptophan and histidine amino acid residues
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
physiological role
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
?
additional information
?
-
-
MsrA is specific for the S-form of the substrate
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
?
additional information
?
-
-
substrate specificity of enzyme forms with S-form of free and protein-bound methionine sulfoxide, overview
-
-
?
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation
-
-
?
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates
-
-
?
additional information
?
-
-
the reduction step is rate-determining
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
additional information
?
-
-
physiological role
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
?
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Grimaud, R.; Ezraty, B.; Mitchell, J.K.; Lafitte, D.; Briand, C.; Derrick, P.J.; Barras, F.
Repair of oxidized proteins: identification of a new methionine sulfoxide reductase
J. Biol. Chem.
276
48915-48920
2001
Escherichia coli
brenda
Brot, N.; Weissbach, L.; Werth, J.; Weissbach, H.
Enzymatic reduction of protein-bound methionine sulfoxide
Proc. Natl. Acad. Sci. USA
78
2155-2158
1981
Escherichia coli, Escherichia coli Z19
brenda
Wizemann, T.M.; Moskovitz, J.; Pearce, B.J.; Cundell, D.; Arvidson, C.G.; So, M.; Weissbach, H.; Brot, N.; Masure, H.R.
Peptide methionine-sulfoxide reductase contributes to the maintenance of adhesions in three major pathogens
Proc. Natl. Acad. Sci. USA
93
7985-7990
1996
Streptococcus pneumoniae, Escherichia coli, Neisseria gonorrhoeae, Neisseria gonorrhoeae MS11A, Streptococcus pneumoniae R6x
brenda
Moskovitz, J.; Poston, J.M.; Berlett, B.S.; Nosworthy, N.J.; Szczepanowski, R.; Stadtman, E.R.
Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
J. Biol. Chem.
275
14167-14172
2000
Saccharomyces cerevisiae, Escherichia coli
brenda
St.John, G.; Brot, N.; Ruan, J.; Erdjument-Bromage, H.; Tempst, P.; Weissbach, H.; Nathan, C.
Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
Proc. Natl. Acad. Sci. USA
98
9901-9906
2001
Escherichia coli, Mycobacterium tuberculosis
brenda
Weissbach, H.; Etienne, F.; Hoshi, T.; Heinemann, S.H.; Lowther, W.T.; Matthews, B.; St John, G.; Nathan, C.; Brot, N.
Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function
Arch. Biochem. Biophys.
397
172-178
2002
Streptococcus pneumoniae, Escherichia coli
brenda
Spector, D.; Etienne, F.; Brot, N.; Weissbach, H.
New membrane-associated and soluble peptide methionine sulfoxide reductases in Escherichia coli
Biochem. Biophys. Res. Commun.
302
284-289
2003
Escherichia coli
brenda
Etienne, F.; Resnick, L.; Sagher, D.; Brot, N.; Weissbach, H.
Reduction of Sulindac to its active metabolite, sulindac sulfide: assay and role of the methionine sulfoxide reductase system
Biochem. Biophys. Res. Commun.
312
1005-1010
2003
Bos taurus, Escherichia coli
brenda
Weissbach, H.; Resnick, L.; Brot, N.
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Biochim. Biophys. Acta
1703
203-212
2005
Bos taurus, Dickeya chrysanthemi, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Neisseria gonorrhoeae, Neisseria meningitidis, Saccharomyces cerevisiae, Streptococcus gordonii, Streptococcus pneumoniae
brenda
Moskovitz, J.
Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
Biochim. Biophys. Acta
1703
213-219
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Staphylococcus aureus, Mus musculus, Sus scrofa
brenda
Ezraty, B.; Aussel, L.; Barras, F.
Methionine sulfoxide reductases in prokaryotes
Biochim. Biophys. Acta
1703
221-229
2005
Aggregatibacter actinomycetemcomitans, Bacillus subtilis, Dickeya chrysanthemi, Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Mycoplasma genitalium, Neisseria gonorrhoeae, Neisseria meningitidis, no activity in Aquifex aeolicus, no activity in Thermotoga maritima, Sinorhizobium meliloti, Staphylococcus aureus, Vibrio cholerae serotype O1
brenda
Boschi-Muller, S.; Olry, A.; Antoine, M.; Branlant, G.
The enzymology and biochemistry of methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
231-238
2005
Bacillus subtilis, Escherichia coli, Neisseria meningitidis, Xanthomonas campestris
brenda
Kauffmann, B.; Aubry, A.; Favier, F.
The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions
Biochim. Biophys. Acta
1703
249-260
2005
Bacillus subtilis, Bos taurus (P54149), Deinococcus radiodurans, Escherichia coli (P0A744), Mycobacterium tuberculosis (P9WJM5), Mycobacterium tuberculosis H37Rv (P9WJM5), Neisseria gonorrhoeae (P14930), Neisseria meningitidis, Solanum lycopersicum
brenda
Petropoulos, I.; Friguet, B.
Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
261-266
2005
Saccharomyces cerevisiae, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
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Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli
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