Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
Open accessAbstract
The Escherichia coli peptide methionine sulfoxide reductase gene (msrA) encodes a single-subunit polypeptide of 212 amino acid residues (M. A. Rahman, H. Nelson, H. Weissbach, and N. Brot, J. Biol. Chem. 267:15549-15551, 1992). RNA blot analysis showed that the gene is transcribed into an mRNA of about 850 nucleotides. The promoter region was characterized, and the transcription initiation site was identified by primer extension. The synthesis of the MsrA protein increased about threefold in a growth-phase-dependent fashion. In an attempt to define the in vivo role of msrA, a chromosomal disruption was constructed. This mutant was more sensitive to oxidative stress, suggesting that oxidation of methionine in proteins plays an important role in oxidative damage.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Methionine sulfoxide reductase knockout bacteria are sensitized to the cell killing effects of hydrogen peroxide.
“Significantly, methionine sulfoxide reductase knockout bacteria are sensitized to the cell killing effects of hydrogen peroxide [33,34].”
From Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase (2021) · cites this paper as [33]
The Abstract reports that an E. coli msrA chromosomal-disruption mutant was more sensitive to oxidative stress. The passages in our copy do not specify hydrogen peroxide or show that the increased sensitivity was measured as cell killing, so those details are not supported. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572 · see citing works
REPAIR OF OXIDATIVE DAMAGE TO DNA: Enzymology and Biology
Demple, B., & Harrison, L. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.004411 · Cited by 1,495 · see citing works
New method for generating deletions and gene replacements in Escherichia coli
Hamilton, C. M., Aldea, M., Washburn, B. K., Babitzke, P., & Kushner, S. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.9.4617-4622.1989 · Cited by 678 · see citing works
Self-citationEnzymatic reduction of protein-bound methionine sulfoxide.
Brot, N., Weissbach, L., Werth, J. L., & Weissbach, H. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2155 · Cited by 359 · see citing works
Self-citationCarp, H., Miller, F. W., Hoidal, J. R., & Janoff, A. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.2041 · Cited by 343 · see citing works
Cochrane, C. G., Spragg, R. G., & Revak, S. D. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110823 · Cited by 338 · see citing works
GENETIC BASIS OF STARVATION SURVIVAL IN NONDIFFERENTIATING BACTERIA
Matin, A., Auger, E. A., Blum, P., & Schultz, J. E. (1989) · Annual Review of Microbiology · doi:10.1146/annurev.mi.43.100189.001453 · Cited by 333 · see citing works
Selective oxidation of cysteine and methionine in normal and senile cataractous lenses.
Garner, M. H., & Spector, A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1274 · Cited by 301 · see citing works
Starvation proteins in Escherichia coli: kinetics of synthesis and role in starvation survival
Groat, R. G., Schultz, J. E., Zychlinsky, E., Bockman, A. T., & Matin, A. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.2.486-493.1986 · Cited by 264 · see citing works
Catalases HPI and HPII in Escherichia coli are induced independently
Loewen, P. C., Switala, J., & Triggs‐Raine, B. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90782-9 · Cited by 257 · see citing works
Oxidative changes in human lens proteins during senile nuclear cataract formation
Truscott, R. J. W., & Augusteyn, R. C. (1977) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(77)90212-4 · Cited by 254 · see citing works
Nucleotide sequence ofkatF ofEscherichia colisuggestsKatF protein is a novel σ transcription factor
Mulvey, M. R., & Loewen, P. C. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.23.9979 · Cited by 253 · see citing works
Willetts, N. S., & Mount, D. W. (1969) · Journal of Bacteriology · doi:10.1128/jb.100.2.923-934.1969 · Cited by 165 · see citing works
Aldea, M., Garrido, T., Hernández-Chico, C., Vicente, M., & Kushner, S. R. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08573.x · Cited by 164 · see citing works
Self-citationAn E. coli promoter induced by the cessation of growth
Connell, N. D., Han, Z., Moreno, F., & Kolter, R. (1987) · Molecular Microbiology · doi:10.1111/j.1365-2958.1987.tb00512.x · Cited by 134 · see citing works
Wong, P. S., & Travis, J. W. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)90113-8 · Cited by 129 · see citing works
Inactivation of plasminogen activator inhibitor by oxidants
Lawrence, D. A., & Loskutoff, D. J. (1986) · Biochemistry · doi:10.1021/bi00369a001 · Cited by 123 · see citing works
Biosynthesis of Bacterial Glycogen
Paule, M. R., & Preiss, J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62053-8 · Cited by 119 · see citing works
Okita, T. W., Rodriguez, R. L., & Preiss, J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69082-4 · Cited by 100 · see citing works
Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.
Abrams, W. R., Weinbaum, G., Weissbach, L., Weissbach, H., & Brot, N. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7483 · Cited by 97 · see citing works
Self-citationAmount and chain length of polyphosphates in Escherichia coli depend on cell growth conditions
Rao, N. N., Roberts, M. F., & Torriani, A. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.1.242-247.1985 · Cited by 81 · see citing works
Rahman, M. A., Nelson, H. R., Weissbach, H., & Brot, N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49570-7 · Cited by 75 · see citing works
Self-citationDassa, E., Cahu, M., Desjoyaux-Cherel, B., & Boquet, P. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34481-8 · Cited by 73 · see citing works
Growth phase and ompR regulation of transcription of microcin B17 genes
Hernández-Chico, C., Millán, J. L. S., Kolter, R., & Moreno, F. (1986) · Journal of Bacteriology · doi:10.1128/jb.167.3.1058-1065.1986 · Cited by 65 · see citing works
Tobler, P. H., Tschopp, F. A., Dambacher, M. A., Born, W., & Fischer, J. A. (1983) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-57-4-749 · Cited by 51 · see citing works
appR gene product activates transcription of microcin C7 plasmid genes
Díaz-Guerra, L., Moreno, F., & Millán, J. L. S. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2906-2908.1989 · Cited by 47 · see citing works
Biosynthesis of bacterial glycogen
Preiss, J., Lammel, C. J., & Greenberg, E. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90329-5 · Cited by 35 · see citing works
Oxidation of alpha 1-protease inhibitor: role of lipid peroxidation products
Mohsenin, V., & Gee, J. L. (1989) · Journal of Applied Physiology · doi:10.1152/jappl.1989.66.5.2211 · Cited by 27 · see citing works
Fliss, H., Vasanthakumar, G., Schiffmann, E., Weissbach, H., & Brot, N. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91584-4 · Cited by 19 · see citing works
Self-citationMethionine Sulfoxide: Chemistry and Biochemistry
Brot, N., & Weissbach, H. (2006) · Wiley eBooks · doi:10.1002/0470034386.ch17 · Cited by 14 · see citing works
Self-citationRahman, M. A., Brot, N., & Weissbach, H. (1992) · PubMed · Cited by 11 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563 · see citing works
Storz, G., & Imlayt, J. A. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80033-2 · Cited by 1,077 · see citing works
Stadtman, E. R. (2006) · Free Radical Research · doi:10.1080/10715760600918142 · Cited by 1,056 · see citing works
Oxidative stress, protein damage and repair in bacteria
Ezraty, B., Gennaris, A., Barras, F., & Collet, J. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.26 · Cited by 1,042 · see citing works
Reactive Oxygen-Mediated Protein Oxidation in Aging and Disease
Stadtman, E. R., & Berlett, B. S. (1998) · Drug Metabolism Reviews · doi:10.3109/03602539808996310 · Cited by 892 · see citing works
The pharmacology of the antioxidant lipoic acid
Biewenga, G. P., Haenen, G. R. M. M., & Bast, A. (1997) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(96)00474-0 · Cited by 844 · see citing works
Seaver, L. C., & Imlay, J. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7173-7181.2001 · Cited by 797 · see citing works
Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
Moskovitz, J., Barnoy, S., Williams, W. M., Requena, J. R., Berlett, B. S., & Stadtman, E. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231472998 · Cited by 677 · see citing works
Self-citationProtein Oxidation in Aging and Age‐Related Diseases
Stadtman, E. R. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb05632.x · Cited by 660 · see citing works
The role of oxidative damage and stress in aging
Bokov, A. F., Chaudhuri, A. R., & Richardson, A. G. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.07.009 · Cited by 621 · see citing works
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 598 · see citing works
Some Prospective Strategies for Improving Crop Salt Tolerance
Ashraf, M., Athar, H., Harris, P. J. C., & Kwon, T.-R. (2008) · Advances in agronomy · doi:10.1016/s0065-2113(07)00002-8 · Cited by 556 · see citing works
Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 482 · see citing works
High Levels of Intracellular Cysteine Promote Oxidative DNA Damage by Driving the Fenton Reaction
Park, S., & Imlay, J. A. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.6.1942-1950.2003 · Cited by 485 · see citing works
Methionine in proteins defends against oxidative stress
Luo, S., & Levine, R. L. (2008) · The FASEB Journal · doi:10.1096/fj.08-118414 · Cited by 462 · see citing works
Stable markers of oxidant damage to proteins and their application in the study of human disease
Davies, M. J., Fu, S., Wang, H., & Dean, R. T. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00206-3 · Cited by 461 · see citing works
High-quality life extension by the enzyme peptide methionine sulfoxide reductase
Ruan, H., Tang, X. D., Chen, M.-L., Joiner, M.-L. A., Sun, G., Brot, N., Weissbach, H., Heinemann, S. H., Iverson, L., Wu, C., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032671199 · Cited by 454 · see citing works
Self-citationOxidation of Methionine in Proteins: Roles in Antioxidant Defense and Cellular Regulation
Levine, R. L., Moskovitz, J., & Stadtman, E. R. (2000) · IUBMB Life · doi:10.1080/713803735 · Cited by 446 · see citing works
Self-citationLatent tuberculosis: mechanisms of host and bacillus that contribute to persistent infection
Tufariello, J. M., Chan, J., & Flynn, J. L. (2003) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(03)00741-2 · Cited by 401 · see citing works
Methionine oxidation and aging
Stadtman, E. R., Remmen, H. V., Richardson, A. G., Wehr, N. B., & Levine, R. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.010 · Cited by 398 · see citing works
Moskovitz, J., Yim, M. B., & Chock, P. B. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2692 · Cited by 397 · see citing works
Self-citationRegulation of cell function by methionine oxidation and reduction
Hoshi, T., & Heinemann, S. H. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0001j.x · Cited by 384 · see citing works
Grimaud, R., Ezraty, B., Mitchell, J. K., Lafitte, D., Briand, C. M., Derrick, P. J., & Barras, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105509200 · Cited by 360 · see citing works
Roles of Thiol-Redox Pathways in Bacteria
Ritz, D., & Beckwith, J. (2001) · Annual Review of Microbiology · doi:10.1146/annurev.micro.55.1.21 · Cited by 349 · see citing works
Oxidation of Methionine Residues of Proteins: Biological Consequences
Stadtman, E. R., Moskovitz, J., & Levine, R. L. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770310239 · Cited by 344 · see citing works
Self-citationThe yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
Moskovitz, J., Berlett, B. S., Poston, J. M., & Stadtman, E. R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9585 · Cited by 326 · see citing works
Self-citationPeptide Methionine Sulfoxide Reductase: Structure, Mechanism of Action, and Biological Function
Weissbach, H., Etienne, F., Hoshi, T., Heinemann, S. H., Lowther, W. T., Matthews, B. W., John, G. S., Nathan, C., & Brot, N. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2664 · Cited by 325 · see citing works
Self-citationTanaka, M., Earl, A. M., Howell, H. A., Park, M.-J., Eisen, J. A., Peterson, S. N., & Battista, J. R. (2004) · Genetics · doi:10.1534/genetics.104.029249 · Cited by 314 · see citing works
Methionine oxidation and reduction in proteins
Kim, G., Weiss, S. J., & Levine, R. L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.038 · Cited by 311 · see citing works
Moskovitz, J. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.003 · Cited by 302 · see citing works
Self-citationMethionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Weissbach, H., Resnick, L., & Brot, N. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.004 · Cited by 295 · see citing works
Self-citationMoskovitz, J., Flescher, E., Berlett, B. S., Azare, J., Poston, J. M., & Stadtman, E. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14071 · Cited by 281 · see citing works
Self-citationWhole-Genome Transcriptional Analysis of Heavy Metal Stresses in Caulobacter crescentus
Hu, P., Brodie, E., Suzuki, Y., McAdams, H. H., & Andersen, G. L. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.24.8437-8449.2005 · Cited by 279 · see citing works
Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase
Kryukov, G. V., Kumar, R. A., Koç, A., Sun, Z., & Gladyshev, V. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072603099 · Cited by 264 · see citing works
Mechanisms through which sulfur amino acids control protein metabolism and oxidative status
Métayer, S., Seiliez, I., Collin, A., Duchêne, S., Mercier, Y., Geraert, P., & Tesseraud, S. (2007) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2007.05.006 · Cited by 260 · see citing works
How oxygen damages microbes: Oxygen tolerance and obligate anaerobiosis
Imlay, J. A. (2002) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(02)46003-1 · Cited by 261 · see citing works
Mostertz, J., Scharf, C., Hecker, M., & Homuth, G. (2004) · Microbiology · doi:10.1099/mic.0.26665-0 · Cited by 240 · see citing works
(2000) · PubMed · Cited by 242 · see citing works
Dukan, S., & Nyström, T. (1998) · Genes & Development · doi:10.1101/gad.12.21.3431 · Cited by 228 · see citing works
Missall, T. A., Lodge, J. K., & McEwen, J. E. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.4.835-846.2004 · Cited by 223 · see citing works
Moskovitz, J., Weissbach, H., & Brot, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.2095 · Cited by 219 · see citing works
Self-citationLinkage Map ofEscherichia coliK-12, Edition 10: The Traditional Map
Berlyn, M. K. B. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.3.814-984.1998 · Cited by 216 · see citing works
John, G. S., Brot, N., Ruan, J., Erdjument‐Bromage, H., Tempst, P., Weissbach, H., & Nathan, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161295398 · Cited by 206 · see citing works
Self-citationThe capsule of Mycobacterium tuberculosis and its implications for pathogenicity
Daffé, M., & Etienne, G. (1999) · Tubercle and Lung Disease · doi:10.1054/tuld.1998.0200 · Cited by 200 · see citing works
The physiological role of reversible methionine oxidation
Drazic, A., & Winter, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.001 · Cited by 198 · see citing works
Boschi‐Müller, S., Azza, S., Cianférani, S., Talfournier, F., van Dorsselear, A., & Branlant, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006137200 · Cited by 193 · see citing works
Moskovitz, J., Poston, J. M., Berlett, B. S., Nosworthy, N. J., Szczepanowski, R. H., & Stadtman, E. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14167 · Cited by 188 · see citing works
Self-citationTesterman, T. L., Vázquez‐Torres, A., Xu, Y., Jones‐Carson, J., Libby, S. J., & Fang, F. C. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02787.x · Cited by 186 · see citing works
Kantorow, M., Hawse, J. R., Cowell, T. L., Benhamed, S., Pizarro, G. O., Reddy, V. N., & Hejtmancik, J. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403532101 · Cited by 181 · see citing works
Protein oxidation and age-dependent alterations in calcium homeostasis
Thomas, C. (2000) · Frontiers in bioscience · doi:10.2741/squier · Cited by 179 · see citing works
Methionine sulfoxide reductases in prokaryotes
Ezraty, B., Aussel, L., & Barras, F. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.017 · Cited by 171 · see citing works
Hassouni, M. E., Chambost, J. P., Expert, D., Gijsegem, F. V., & Barras, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.887 · Cited by 171 · see citing works
Kato, M., Yang, Y.-S., Sutter, B. M., Wang, Y., McKnight, S. L., & Tu, B. P. (2019) · Cell · doi:10.1016/j.cell.2019.02.044 · Cited by 169 · see citing works
Lowther, W. T., Brot, N., Weissbach, H., Honek, J. F., & Matthews, B. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6463 · Cited by 169 · see citing works
Self-citationThioredoxin 2 Is Involved in the Oxidative Stress Response inEscherichia coli
Ritz, D., Patel, H. M., Doan, B., Zheng, M., Åslund, F., Storz, G., & Beckwith, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2505 · Cited by 168 · see citing works
Santos, C. V. D., Cuiné, S., Rouhier, N., & Rey, P. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.062430 · Cited by 166 · see citing works
Romero, H. M., Berlett, B. S., Jensen, P. J., Pell, E. J., & Tien, M. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.046656 · Cited by 150 · see citing works
Plant methionine sulfoxide reductase A and B multigenic families
Rouhier, N., Santos, C. V. D., Tarrago, L., & Rey, P. (2006) · Photosynthesis Research · doi:10.1007/s11120-006-9097-1 · Cited by 148 · see citing works
Moskovitz, J., Singh, V. K., Requena, J. R., Wilkinson, B. J., Jayaswal, R. K., & Stadtman, E. R. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6171 · Cited by 148 · see citing works
Self-citationSeib, K. L., Wu, H., Kidd, S. P., Apicella, M. A., Jennings, M. P., & McEwan, A. G. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00044-05 · Cited by 143 · see citing works
Sun, H., Gao, J., Ferrington, D. A., Biesiada, H., Williams, T. D., & Squier, T. C. (1998) · Biochemistry · doi:10.1021/bi981295k · Cited by 146 · see citing works
Methionine in Proteins: It’s Not Just for Protein Initiation Anymore
Lim, J. M., Kim, G., & Levine, R. L. (2018) · Neurochemical Research · doi:10.1007/s11064-017-2460-0 · Cited by 144 · see citing works
Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme,
Lowther, W. T., Brot, N., Weissbach, H., & Matthews, B. W. (2000) · Biochemistry · doi:10.1021/bi0020269 · Cited by 142 · see citing works
Self-citationWizemann, T. M., Moskovitz, J., Pearce, B. J., Cundell, D. R., Arvidson, C. G., So, M., Weissbach, H., Brot, N., & Masure, H. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7985 · Cited by 137 · see citing works
Self-citationMoskovitz, J., Jenkins, N. A., Gilbert, D. J., Copeland, N. G., Jurský, F., Weissbach, H., & Brot, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3205 · Cited by 134 · see citing works
Self-citationStadtman, E. R. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00904-8 · Cited by 133 · see citing works
Salmon, A. B., Pérez, V., Bokov, A. F., Jernigan, A., Kim, G., Zhao, H., Levine, R. L., & Richardson, A. (2009) · The FASEB Journal · doi:10.1096/fj.08-127415 · Cited by 131 · see citing works
Petropoulos, I., Mary, J., Perichon, M., & Friguet, B. (2001) · Biochemical Journal · doi:10.1042/bj3550819 · Cited by 131 · see citing works
Skaar, E. P., Tobiason, D. M., Quick, J., Judd, R. C., Weissbach, H., Etienne, F., Brot, N., & Seifert, H. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152334799 · Cited by 127 · see citing works
Self-citationBechtold, U., Murphy, D. J., & Mullineaux, P. M. (2004) · The Plant Cell · doi:10.1105/tpc.015818 · Cited by 124 · see citing works
Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress
Grose, J. H., Joss, L., Velick, S. F., & Roth, J. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602494103 · Cited by 123 · see citing works
Peptide Methionine Sulfoxide Reductase (MsrA) Is a Virulence Determinant in Mycoplasma genitalium
Dhandayuthapani, S., Blaylock, M. W., Bébéar, C., Rasmussen, W. G., & Baseman, J. B. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.19.5645-5650.2001 · Cited by 122 · see citing works
Ramoutar, R. R., & Brumaghim, J. L. (2010) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-010-9088-x · Cited by 120 · see citing works
Châtelain, E., Satour, P., Laugier, E., Vu, B. L., Payet, N., Rey, P., & Montrichard, F. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220589110 · Cited by 120 · see citing works
Methionine Sulfoxide Reductases
Cabreiro, F., Picot, C. R., Friguet, B., & Petropoulos, I. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1354.006 · Cited by 120 · see citing works
Origin and evolution of the protein‐repairing enzymes methionine sulphoxide reductases
Zhang, X., & Weissbach, H. (2008) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2008.00042.x · Cited by 114 · see citing works
Self-citationSingh, V. K., Jayaswal, R. K., & Wilkinson, B. J. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb10654.x · Cited by 114 · see citing works
Vougier, S., Mary, J., & Friguet, B. (2003) · Biochemical Journal · doi:10.1042/bj20030443 · Cited by 112 · see citing works
Proteasome inactivation upon aging and on oxidation-effect of HSP 90
Conconi, M., & Friguet, B. (1997) · Molecular Biology Reports · doi:10.1023/a:1006852506884 · Cited by 111 · see citing works
Lourenço dos Santos, S., Petropoulos, I., & Friguet, B. (2018) · Antioxidants · doi:10.3390/antiox7120191 · Cited by 109 · see citing works
Jung, I. L., & Kim, I. G. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00064-0 · Cited by 109 · see citing works
Tesseraud, S., Métayer, S., Collin, A., & Seiliez, I. (2008) · British Journal Of Nutrition · doi:10.1017/s0007114508159025 · Cited by 108 · see citing works
McGhee, G. C., & Jones, A. L. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.11.4897-4907.2000 · Cited by 108 · see citing works
Gustavsson, N., Kokke, B. P. A., Härndahl, U., Silow, M., Bechtold, U., Poghosyan, Z. P., Murphy, D. J., Boelens, W. C., & Sundby, C. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.029005545.x · Cited by 106 · see citing works
Methionine sulfoxide reductase A is a stereospecific methionine oxidase
Lim, J. C., You, Z., Kim, G., & Levine, R. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101275108 · Cited by 105 · see citing works
Moskovitz, J., & Stadtman, E. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332607100 · Cited by 105 · see citing works
Self-citationStructure and regulation of opioid receptors
Chaturvedi, K., Christoffers, K. H., Singh, K., & Howells, R. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:4 · Cited by 89 · see citing works
Self-citationPedersen, M. B., Garrigues, C., Tuphile, K., Brun, C., Vido, K., Bennedsen, M., Møllgaard, H., Gaudu, P., & Gruss, A. (2008) · Journal of Bacteriology · doi:10.1128/jb.00447-08 · Cited by 103 · see citing works
Chen, Z., Hartke, A., Sorda, M. L., Posteraro, B., Laplace, J., Auffray, Y., & Sanguinetti, M. (2010) · Infection and Immunity · doi:10.1128/iai.00165-10 · Cited by 103 · see citing works
Sadanandom, A., Poghosyan, Z. P., Fairbairn, D. J., & Murphy, D. J. (2000) · PLANT PHYSIOLOGY · doi:10.1104/pp.123.1.255 · Cited by 95 · see citing works
Reducing systems protecting the bacterial cell envelope from oxidative damage
Arts, I. S., Gennaris, A., & Collet, J. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.04.057 · Cited by 90 · see citing works
Alamuri, P., & Maier, R. J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04190.x · Cited by 90 · see citing works
Favier, F., Cobessi, D., Boschi‐Müller, S., Azza, S., Branlant, G., & Aubry, A. (2000) · Structure · doi:10.1016/s0969-2126(00)00526-8 · Cited by 89 · see citing works
Duewel, H. S., Daub, E., Robinson, V. J., & Honek, J. F. (1997) · Biochemistry · doi:10.1021/bi9617973 · Cited by 88 · see citing works
Enzymatic reactions involved in the repair of oxidized proteins
Mary, J., Vougier, S., Picot, C. R., Perichon, M., Petropoulos, I., & Friguet, B. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.06.008 · Cited by 87 · see citing works
Roles of Methionine Suldfoxide Reductases in Antioxidant Defense, Protein Regulation and Survival
Moskovitz, J. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612053507846 · Cited by 84 · see citing works
Self-citationVisick, J. E., Cai, H., & Clarke, S. G. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.10.2623-2629.1998 · Cited by 83 · see citing works
Methionine oxidation activates pyruvate kinase M2 to promote pancreatic cancer metastasis
He, D., Feng, H., Sundberg, B., Yang, J., Powers, J., Christian, A. H., Wilkinson, J. E., Monnin, C., Avizonis, D. Z., Thomas, C. J., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.06.005 · Cited by 77 · see citing works
Kim, M.-A., Cho, H.-J., Bae, S.-H., Lee, B., Oh, S., Kwon, T.-J., Ryoo, Z. Y., Kim, H., Cho, J., Kim, U., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6442 · Cited by 79 · see citing works
Douglas, T., Daniel, D., Parida, B. K., Jagannath, C., & Dhandayuthapani, S. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.11.3590-3598.2004 · Cited by 77 · see citing works
- Authors
- Moskovitz, J., Rahman, M. A., Strassman, J., Yancey, S. O., Kushner, S. R., Brot, N., & Weissbach, H.
- Affiliations
- Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1995-02
- Volume
- 177
- Issue
- 3
- Pages
- 502-507
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC176620
- OpenAlex
- W2107508146
- Cited by
- 294
- References
- 31
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 5 · 2021: 7 · 2020: 4 · 2019: 9 · 2018: 8 · 2017: 4 · 2016: 9 · 2015: 9 · 2014: 3 · 2013: 10 · 2012: 7
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KU ScholarWorks (University of Kansas) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- Escherichia coli, msrA gene, methionine sulfoxide reductase, gene expression regulation, promoter analysis, transcription start sites, oxidative stress sensitivity, oxidative damage protection
- MeSH terms
- Base Sequence, Escherichia coli, Genes, Bacterial, Methionine, Molecular Sequence Data, Mutation, Oxidoreductases, RNA, Messenger, Gene Expression Regulation, Bacterial, Oxidative Stress, Methionine Sulfoxide Reductases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review