Regulation of antioxidant defense and glyoxalase systems in cyanobacteria
Abstract
Oxidative stress is common consequence of abiotic stress in plants as well as cyanobacteria caused by generation of reactive oxygen species (ROS), an inevitable product of respiration and photosynthetic electron transport. ROS act as signalling molecule at low concentration however, when its production exceeds the endurance capacity of antioxidative defence system, the organisms suffer oxidative stress. A highly toxic metabolite, methylglyoxal (MG) is also produced in cyanobacteria in response to various abiotic stresses which consequently augment the ensuing oxidative damage. Taking recourse to the common lineage of eukaryotic plants and cyanobacteria, it would be worthwhile to explore the regulatory role of glyoxalase system and antioxidative defense mechanism in combating abiotic stress in cyanobacteria. This review provides comprehensive information on the complete glyoxalase system (GlyI, GlyII and GlyIII) in cyanobacteria. Furthermore, it elucidates the recent understanding regarding the production of ROS and MG, noteworthy link between intracellular MG and ROS and its detoxification via synchronization of antioxidants (enzymatic and non-enzymatic) and glyoxalase systems using glutathione (GSH) as common co-factor.
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MDA content serves as a key biomarker of oxidative injury in microalgal cell membranes.
“Furthermore, malondialdehyde (MDA) contents serve as a key biomarker of oxidative injury in microalgal cell membranes, which are rich in polyunsaturated fatty acids prone to oxidation (Rai et al. 2021).”
From Integrated morpho-physiological and biochemical description of the mechanisms leading stress responses in cyanobacteria (Arthrospira platensis) upon exposure to Erythromycin (2025) · cites this paper as Rai et al. 2021
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Rai, S., Yadav, S., Rai, R., Chatterjee, A., Singh, S., & Rai, L. C. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.11.172 · Cited by 16 · see citing works
Self-citationRetractedReactive oxygen species: Metabolism, oxidative stress, and signal transduction
Apel, K., & Hirt, H. (2004) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.55.031903.141701 · Cited by 11,723 · see citing works
Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
Umena, Y., Kawakami, K., Shen, J., & Kamiya, N. (2011) · Nature · doi:10.1038/nature09913 · Cited by 3,920 · see citing works
Hayes, J. D., Flanagan, J. U., & Jowsey, I. R. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095857 · Cited by 3,565 · see citing works
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546 · see citing works
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life
Halliwell, B. B. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.077073 · Cited by 2,402 · see citing works
Gasque, G., Conway, S., Huang, J., Rao, Y., & Vosshall, L. B. (2013) · Scientific Reports · doi:10.1038/srep02120 · Cited by 2,320 · see citing works
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works
Diversity of structures and properties among catalases
Chelikani, P., Fita, I., & Loewen, P. C. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3206-5 · Cited by 1,701 · see citing works
Glutathione in plants: an integrated overview
Noctor, G., Mhamdi, A., Chaouch, S., Han, Y., Neukermans, J., Márquez‐García, B., Queval, G., & Foyer, C. H. (2011) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2011.02400.x · Cited by 1,600 · see citing works
Photoinhibition of photosystem II under environmental stress
Murata, N., Takahashi, S., Nishiyama, Y., & Allakhverdiev, S. I. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.11.019 · Cited by 1,587 · see citing works
Dating the rise of atmospheric oxygen
Bekker, A., Holland, H. D., Wang, P.-L., Rumble, D., Stein, H. J., Hannah, J. L., Coetzee, L. L., & Beukes, N. J. (2004) · Nature · doi:10.1038/nature02260 · Cited by 1,435 · see citing works
Regulation and function of ascorbate peroxidase isoenzymes
Shigeoka, S., Ishikawa, T., Tamoi, M., Miyagawa, Y., Takeda, T., Yabuta, Y., & Yoshimura, K. (2002) · Journal of Experimental Botany · doi:10.1093/jexbot/53.372.1305 · Cited by 1,321 · see citing works
Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
Deponte, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.018 · Cited by 1,104 · see citing works
Reactive oxygen species, oxidative signaling and the regulation of photosynthesis
Foyer, C. H. (2018) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2018.05.003 · Cited by 871 · see citing works
Plant glutathione transferases.
Dixon, D. P., Lapthorn, A. J., & Edwards, R. (2002) · Genome biology · doi:10.1186/gb-2002-3-3-reviews3004 · Cited by 851 · see citing works
Superfamily of plant, fungal and bacterial peroxidases
Welinder, K. G. (1992) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(92)90230-5 · Cited by 836 · see citing works
Oxidative stress in cyanobacteria
Latifi, A., Ruiz, M., & Zhang, C. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00134.x · Cited by 792 · see citing works
A new paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II
Nishiyama, Y., Allakhverdiev, S. I., & Murata, N. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.013 · Cited by 740 · see citing works
An ancient light-harvesting protein is critical for the regulation of algal photosynthesis
Peers, G., Truong, T. B., Ostendorf, E., Busch, A., Elrad, D., Grossman, A. R., Hippler, M., & Niyogi, K. (2009) · Nature · doi:10.1038/nature08587 · Cited by 715 · see citing works
Singlet oxygen in plants: production, detoxification and signaling
Triantaphylidès, C., & Havaux, M. (2009) · Trends in Plant Science · doi:10.1016/j.tplants.2009.01.008 · Cited by 715 · see citing works
Weidinger, A., & Kozlov, A. V. (2015) · Biomolecules · doi:10.3390/biom5020472 · Cited by 648 · see citing works
Glutathione peroxidase family – an evolutionary overview
Margis, R., Dunand, C., Teixeira, F. K., & Margis-Pinheiro, M. M. A. N. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06542.x · Cited by 611 · see citing works
THE MECHANISM OF ACTION OF GLYOXALASE
Racker, E. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56017-8 · Cited by 584 · see citing works
The aldo-keto reductases (AKRs): Overview
Penning, T. M. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.09.024 · Cited by 547 · see citing works
The Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification
Barski, O. A., Tipparaju, S. M., & Bhatnagar, A. (2008) · Drug Metabolism Reviews · doi:10.1080/03602530802431439 · Cited by 543 · see citing works
Oxidative damage and antioxidative system in algae
Rezayian, M., Niknam, V., & Ebrahimzadeh, H. (2019) · Toxicology Reports · doi:10.1016/j.toxrep.2019.10.001 · Cited by 538 · see citing works
Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery
Nishiyama, Y., Yamamoto, H., Allakhverdiev, S. I., Inaba, M., Yokota, A., & Murata, N. (2001) · The EMBO Journal · doi:10.1093/emboj/20.20.5587 · Cited by 532 · see citing works
Applications of cyanobacteria in biotechnology
Abed, R. M. M., Dobretsov, S., & Sudesh, K. (2009) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2008.03918.x · Cited by 528 · see citing works
Ultraviolet light induced generation of reactive oxygen species
de Jager, T. L., Cockrell, A. E., & Du Plessis, S. S. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5_2 · Cited by 523 · see citing works
Ergothioneine; antioxidant potential, physiological function and role in disease
Cheah, I. K., & Halliwell, B. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.09.017 · Cited by 514 · see citing works
Pospı́šil, P. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01950 · Cited by 512 · see citing works
Methylglyoxal in living organisms
Kalapos, M. P. (1999) · Toxicology Letters · doi:10.1016/s0378-4274(99)00160-5 · Cited by 507 · see citing works
Thornalley, P. J. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.125 · Cited by 482 · see citing works
Seo, M. S., Kang, S. W., Kim, K., Baines, I., Lee, T., & Rhee, S. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001943200 · Cited by 473 · see citing works
Evolution of Catalases from Bacteria to Humans
Zámocký, M., Furtmüller, P. G., & Obinger, C. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2046 · Cited by 467 · see citing works
Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione
Yadav, S. K., Singla-Pareek, S. L., Ray, M., Reddy, M. K., & Sopory, S. K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.263 · Cited by 466 · see citing works
The Aldo-Keto Reductase Superfamily
Bohren, K. M., Bullock, B., Wermuth, B., & Gabbay, K. H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60566-6 · Cited by 453 · see citing works
Characterization of a Mammalian Peroxiredoxin That Contains One Conserved Cysteine
Kang, S. W., Baines, I., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6303 · Cited by 448 · see citing works
The function of peroxiredoxins in plant organelle redox metabolism
Dietz, K.-J. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj160 · Cited by 434 · see citing works
Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
Rabbani, N., & Thornalley, P. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0783-0 · Cited by 431 · see citing works
Allakhverdiev, S. I., & Murata, N. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.003 · Cited by 428 · see citing works
Peroxiredoxins in Plants and Cyanobacteria
Dietz, K. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3657 · Cited by 407 · see citing works
Genetic engineering of the glyoxalase pathway in tobacco leads to enhanced salinity tolerance
Singla-Pareek, S. L., Reddy, M. K., & Sopory, S. K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2034667100 · Cited by 406 · see citing works
Glutathione transferases: a structural perspective
Oakley, A. J. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.558093 · Cited by 403 · see citing works
Dps Protects Cells against Multiple Stresses during Stationary Phase
Nair, S., & Finkel, S. E. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.13.4192-4198.2004 · Cited by 383 · see citing works
On the origins of oxygenic photosynthesis and aerobic respiration in Cyanobacteria
Soo, R. M., Hemp, J., Parks, D. H., Fischer, W. W., & Hugenholtz, P. (2017) · Science · doi:10.1126/science.aal3794 · Cited by 383 · see citing works
Ohnishi, N., Allakhverdiev, S. I., Takahashi, S., Higashi, S., Watanabe, M., Nishiyama, Y., & Murata, N. (2005) · Biochemistry · doi:10.1021/bi047518q · Cited by 370 · see citing works
Ehling‐Schulz, M., Bilger, W., & Scherer, S. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.6.1940-1945.1997 · Cited by 368 · see citing works
Seminars in cell and developmental biology
Smyth, I., & Bertram, J. F. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.11.003 · Cited by 351 · see citing works
A new nomenclature for the aldo-keto reductase superfamily
Jez, J. M., Flynn, T. G., & Penning, T. M. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)84253-0 · Cited by 350 · see citing works
Foresi, N. P., Correa‐Aragunde, N., Parisi, G. D., Caló, G., Salerno, G. L., & Lamattina, L. (2010) · The Plant Cell · doi:10.1105/tpc.109.073510 · Cited by 347 · see citing works
Crystal Structure of Manganese Catalase from Lactobacillus plantarum
Barynin, V. V., Whittaker, M. M., Antonyuk, S. V., Lamzin, V. S., Harrison, P. M., Artymiuk, P. J., & Whittaker, J. W. (2001) · Structure · doi:10.1016/s0969-2126(01)00628-1 · Cited by 338 · see citing works
Nishiyama, Y., Allakhverdiev, S. I., Yamamoto, H., Hayashi, H., & Murata, N. (2004) · Biochemistry · doi:10.1021/bi036178q · Cited by 319 · see citing works
The aldo-keto reductase superfamily homepage
Hyndman, D., Bauman, D. R., Heredia, V. V., & Penning, T. M. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00193-x · Cited by 317 · see citing works
Allakhverdiev, S. I., Nishiyama, Y., Miyairi, S., Yamamoto, H., Inagaki, N., Kanesaki, Y., & Murata, N. (2002) · PLANT PHYSIOLOGY · doi:10.1104/pp.011114 · Cited by 304 · see citing works
de la Coba, F., Aguilera, J., Figueroa, F. L., de Gálvez, M. V., & Herrera, E. (2009) · Journal of Applied Phycology · doi:10.1007/s10811-008-9345-1 · Cited by 302 · see citing works
Oxygen and ROS in Photosynthesis
Khorobrykh, S. A., Havurinne, V., Mattila, H., & Tyystjärvi, E. (2020) · Plants · doi:10.3390/plants9010091 · Cited by 285 · see citing works
Comparative transcriptome analysis of arsenate and arsenite stresses in rice seedlings
Chakrabarty, D., Trivedi, P. K., Misra, P., Tiwari, M., Shri, M., Shukla, D., Kumar, S., Rai, A., Pandey, A. K., Nigam, D., et al. (2008) · Chemosphere · doi:10.1016/j.chemosphere.2008.09.082 · Cited by 284 · see citing works
Mycosporine-Like Amino Acids and Their Derivatives as Natural Antioxidants
Wada, N., Sakamoto, T., & Matsugo, S. (2015) · Antioxidants · doi:10.3390/antiox4030603 · Cited by 283 · see citing works
Genes Encoding A-Type Flavoproteins Are Essential for Photoreduction of O2 in Cyanobacteria
Helman, Y., Tchernov, D., Reinhold, L., Shibata, M., Ogawa, T., Schwarz, R., Ohad, I., & Kaplan, A. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00046-0 · Cited by 283 · see citing works
Glutathione: a key component of the cytoplasmic labile iron pool
Hider, R. C., & Kong, X. L. (2011) · BioMetals · doi:10.1007/s10534-011-9476-8 · Cited by 281 · see citing works
Bhat, V. B., & Madyastha, K. M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5195 · Cited by 277 · see citing works
Plant glutathione transferase-mediated stress tolerance: functions and biotechnological applications
Nianiou‐Obeidat, I., Madesis, P. B., Kissoudis, C., Voulgari, G., Chronopoulou, E. G., Tsaftaris, A. S., & Labrou, N. E. (2017) · Plant Cell Reports · doi:10.1007/s00299-017-2139-7 · Cited by 276 · see citing works
mirEX 2.0 - an integrated environment for expression profiling of plant microRNAs
Zieleziński, A., Dolata, J., Alaba, S., Kruszka, K., Pacak, A. M., Świda-Barteczka, A., Knop, K., Stępień, A., Bielewicz, D., Pietrykowska, H., et al. (2015) · BMC Plant Biology · doi:10.1186/s12870-015-0533-2 · Cited by 274 · see citing works
Singla-Pareek, S. L., Yadav, S. K., Pareek, A., Reddy, M. K., & Sopory, S. K. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.073734 · Cited by 261 · see citing works
Veena, Reddy, V. S., & Sopory, S. K. (1999) · The Plant Journal · doi:10.1046/j.1365-313x.1999.00390.x · Cited by 257 · see citing works
The glyoxalase pathway: the first hundred years… and beyond
Silva, M. S., Gomes, R. A., Ferreira, A. E. N., Freire, A. P., & CORDEIRO, C. A. (2013) · Biochemical Journal · doi:10.1042/bj20121743 · Cited by 256 · see citing works
Ross, C., Santiago-Vàzquez, L. Z., & Paul, V. J. (2006) · Aquatic Toxicology · doi:10.1016/j.aquatox.2006.02.007 · Cited by 255 · see citing works
METABOLISM OF METHYLGLYOXAL IN MICROORGANISMS
Cooper, R. A. (1984) · Annual Review of Microbiology · doi:10.1146/annurev.mi.38.100184.000405 · Cited by 252 · see citing works
THE ROLE AND EVOLUTION OF SUPEROXIDE DISMUTASES IN ALGAE<sup>1</sup>
Wolfe‐Simon, F., Grzebyk, D., Schofield, O., & Falkowski, P. G. (2005) · Journal of Phycology · doi:10.1111/j.1529-8817.2005.00086.x · Cited by 239 · see citing works
The aldo-keto reductase (AKR) superfamily: an update
Jez, J. M., & Penning, T. M. (2001) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00295-7 · Cited by 239 · see citing works
Cyanobacteria evolution: Insight from the fossil record
Demoulin, C., Lara, Y. J., Cornet, L., François, C., Baurain, D., Wilmotte, A., & Javaux, E. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.05.007 · Cited by 239 · see citing works
PeroxiBase: The peroxidase database
Passardi, F., Theiler, G., Zámocký, M., Cosio, C., Rouhier, N., Teixera, F., Margis-Pinheiro, M. M. A. N., Ioannidis, V., Penel, C., Falquet, L., et al. (2007) · Phytochemistry · doi:10.1016/j.phytochem.2007.04.005 · Cited by 238 · see citing works
Manganese-oxidizing photosynthesis before the rise of cyanobacteria
Johnson, J. E., Webb, S. M., Thomas, K., Ono, S., Kirschvink, J. L., & Fischer, W. W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305530110 · Cited by 238 · see citing works
Cyanobacteria and ultraviolet radiation (UVR) stress: Mitigation strategies
Singh, S. P., Häder, D., & Sinha, R. P. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.05.004 · Cited by 235 · see citing works
Self-citationAn Update on Vitamin E, Tocopherol and Tocotrienol—Perspectives
Colombo, M. L. (2010) · Molecules · doi:10.3390/molecules15042103 · Cited by 224 · see citing works
Crystal Structure of Mycobacterium tuberculosis Catalase-Peroxidase
Bertrand, T., Eady, N. A. J., Jones, J. N., Bodiguel, J., Jesmin, Nagy, J. M., Raven, E. L., Jamart‐Grégoire, B., & Brown, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402382200 · Cited by 221 · see citing works
Microalgal Metallothioneins and Phytochelatins and Their Potential Use in Bioremediation
Balzano, S., Sardo, A., Blasio, M., Chahine, T. B., Dell’Anno, F., Sansone, C., & Brunet, C. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00517 · Cited by 216 · see citing works
Cyanobacterial photoprotection by the orange carotenoid protein
Kirilovsky, D. L., & Kerfeld, C. A. (2016) · Nature Plants · doi:10.1038/nplants.2016.180 · Cited by 213 · see citing works
The plant multigenic family of thiol peroxidases
Rouhier, N., & Jacquot, J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.037 · Cited by 210 · see citing works
Bhat, V. B., & Madyastha, K. M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5368 · Cited by 207 · see citing works
Glutathione analogs in prokaryotes.
Fahey, R. C. (2013) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2012.10.006 · Cited by 205 · see citing works
Hasanuzzaman, M., Nahar, K., Anee, T. I., & Fujita, M. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.01061 · Cited by 204 · see citing works
Enhancing salt tolerance in a crop plant by overexpression of glyoxalase II
Singla-Pareek, S. L., Yadav, S. K., Pareek, A., Reddy, M. K., & Sopory, S. K. (2007) · Transgenic Research · doi:10.1007/s11248-007-9082-2 · Cited by 194 · see citing works
Li, H., Singh, A. K., McIntyre, L. M., & Sherman, L. A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.11.3331-3345.2004 · Cited by 194 · see citing works
The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli
Cooper, R. A., & Anderson, A. (1970) · FEBS Letters · doi:10.1016/0014-5793(70)80546-4 · Cited by 186 · see citing works
Gorman, A. A., & Rodgers, M. A. J. (1992) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/1011-1344(92)85095-c · Cited by 186 · see citing works
Mostofa, M. G., Hossain, M. A., & Fujita, M. (2014) · PROTOPLASMA · doi:10.1007/s00709-014-0691-3 · Cited by 184 · see citing works
Cyanobacterial bioactive metabolites—A review of their chemistry and biology
Huang, I., & Zimba, P. V. (2019) · Harmful Algae · doi:10.1016/j.hal.2018.11.008 · Cited by 183 · see citing works
Hossain, M. A., Hossain, M. Z., & Fujita, M. (2009) · Australian Journal of Crop Science · Cited by 182 · see citing works
Redox Regulation in Photosynthetic Organisms: Focus on Glutathionylation
Zaffagnini, M., Bedhomme, M., Marchand, C. H., Morisse, S., Trost, P., & Lemaire, S. D. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4255 · Cited by 181 · see citing works
Microbial Diversity in the Genomic Era
Das, S., & Dash, H. R. (2018) · Elsevier eBooks · doi:10.1016/c2017-0-01759-7 · Cited by 181 · see citing works
The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria
Kirilovsky, D. L., & Kerfeld, C. A. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.04.013 · Cited by 180 · see citing works
Methylglyoxal – a signaling molecule in plant abiotic stress responses
Mostofa, M. G., Ghosh, A., Li, Z., Siddiqui, M. N., Fujita, M., & Tran, L. P. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.009 · Cited by 180 · see citing works
Salt stress inhibits photosystems II and I in cyanobacteria
Allakhverdiev, S. I., & Murata, N. (2008) · Photosynthesis Research · doi:10.1007/s11120-008-9334-x · Cited by 179 · see citing works
Allen, J. F., & Martin, W. F. (2007) · Nature · doi:10.1038/445610a · Cited by 178 · see citing works
Bissati, K. E., Delphin, E., Murata, N., Etienne, A., & Kirilovsky, D. L. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00104-3 · Cited by 172 · see citing works
Inhibition of the repair of Photosystem II by oxidative stress in cyanobacteria
Nishiyama, Y., Allakhverdiev, S. I., & Murata, N. (2005) · Photosynthesis Research · doi:10.1007/s11120-004-6434-0 · Cited by 171 · see citing works
Evolution and diversity of glutaredoxins in photosynthetic organisms
Couturier, J., Jacquot, J., & Rouhier, N. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0054-y · Cited by 170 · see citing works
Rastogi, R. P., & Incharoensakdi, A. (2013) · FEMS Microbiology Ecology · doi:10.1111/1574-6941.12220 · Cited by 168 · see citing works
Allakhverdiev, S. I., Nishiyama, Y., Takahashi, S., Miyairi, S., Suzuki, I., & Murata, N. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.054478 · Cited by 164 · see citing works
The 2.0 Å crystal structure of catalase-peroxidase from Haloarcula marismortui
Yamada, Y., Fujiwara, T., Sato, T., Igarashi, N., & Tanaka, N. (2002) · Nature Structural Biology · doi:10.1038/nsb834 · Cited by 163 · see citing works
Simpson, P. J., Tantitadapitak, C., Reed, A. M., Mather, O. C., Bunce, C. M., White, S. A., & Ride, J. P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.023 · Cited by 161 · see citing works
Glyoxalase and Methylglyoxal as Biomarkers for Plant Stress Tolerance
Kaur, C., Singla-Pareek, S. L., & Sopory, S. K. (2014) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2014.904147 · Cited by 158 · see citing works
Pandey, S., Rai, R., & Chand, L. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.10.011 · Cited by 158 · see citing works
Self-citationAldo-keto reductase (AKR) superfamily: Genomics and annotation
Mindnich, R., & Penning, T. M. (2009) · Human Genomics · doi:10.1186/1479-7364-3-4-362 · Cited by 158 · see citing works
Shirkey, B., Kovarcik, D. P., Wright, D. J., Wilmoth, G., Prickett, T., Helm, R. F., Gregory, E. M., & Potts, M. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.1.189-197.2000 · Cited by 158 · see citing works
Cyanobacteria produce high levels of ergothioneine
Pfeiffer, C., Bauer, T., Surek, B., Schömig, E., & Gründemann, D. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.06.047 · Cited by 153 · see citing works
Oxidation of elongation factor G inhibits the synthesis of the D1 protein of photosystem II
Kojima, K., Oshita, M., Nanjo, Y., Kasai, K., Tozawa, Y., Hayashi, H., & Nishiyama, Y. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05836.x · Cited by 152 · see citing works
AN ENZYME CONCERNED WITH THE FORMATION OF HYDROXY ACIDS FROM KETONIC ALDEHYDES
Dakin, H. D., & Dudley, H. W. (1913) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88610-0 · Cited by 151 · see citing works
Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin
Iwema, T., Picciocchi, A., Traoré, D. A. K., Ferrer, J.-L., Chauvat, F., & Jacquamet, L. (2009) · Biochemistry · doi:10.1021/bi900440m · Cited by 149 · see citing works
Differential expression of members of a cyanobacterial psbA gene family in response to light
Schaefer, M. R., & Golden, S. S. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.7.3973-3981.1989 · Cited by 145 · see citing works
Mustafiz, A., Ghosh, A., Tripathi, A. K., Kaur, C., Ganguly, A. K., Bhavesh, N. S., Tripathi, J. K., Pareek, A., Sopory, S. K., & Singla-Pareek, S. L. (2014) · The Plant Journal · doi:10.1111/tpj.12521 · Cited by 144 · see citing works
He, M. M., Clugston, S. L., Honek, J. F., & Matthews, B. W. (2000) · Biochemistry · doi:10.1021/bi000856g · Cited by 142 · see citing works
Schlegel, B. P., Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi9723055 · Cited by 139 · see citing works
Antonyuk, S. V., Melik-Adamyan, V. R., Popov, A. N., Lamzin, V. S., Hempstead, P. D., Harrison, P. M., Artymyuk, P. J., & Barynin, V. V. (2000) · Crystallography Reports · doi:10.1134/1.171145 · Cited by 139 · see citing works
Havaux, M., Guedeney, G., He, Q., & Grossman, A. R. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00391-2 · Cited by 138 · see citing works
AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase
Poole, L. B., Reynolds, C. M., Wood, Z. A., Karplus, P. A., Ellis, H. R., & Calzi, M. L. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01704.x · Cited by 134 · see citing works
The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher
Sedoud, A., López‐Igual, R., Rehman, A. U., Wilson, A., Perreau, F., Boulay, C., Vass, I., Krieger‐Liszkay, A., & Kirilovsky, D. L. (2014) · The Plant Cell · doi:10.1105/tpc.114.123802 · Cited by 132 · see citing works
Origin and Evolution of Water Oxidation before the Last Common Ancestor of the Cyanobacteria
Cardona, T., Murray, J. W., & Rutherford, A. W. (2015) · Molecular Biology and Evolution · doi:10.1093/molbev/msv024 · Cited by 131 · see citing works
Hsp31 of Escherichia coli K‐12 is glyoxalase III
Subedi, K. P., Choi, D., Kim, I., Min, B., & Park, C. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07736.x · Cited by 129 · see citing works
Nitric-oxide synthase: A cytochrome P450 family foster child
Gorren, A. C. F., & Mayer, B. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.08.019 · Cited by 129 · see citing works
Thornalley, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311372 · Cited by 128 · see citing works
Glutathione in Plant Growth, Development, and Stress Tolerance
Tran, L. P., Fujita, M., Burritt, D. J., Díaz‐Vivancos, P., Mostofa, M. G., & Hossain, M. A. (2017) · Springer eBooks · doi:10.1007/978-3-319-66682-2 · Cited by 127 · see citing works
Dueholm, M. S., Andersen, K. S., McIlroy, S. J., Kristensen, J. M., Yashiro, E., Karst, S. M., Albertsen, M., & Nielsen, P. H. (2020) · mBio · doi:10.1128/mbio.01557-20 · Cited by 127 · see citing works
Mella–Flores, D., Six, C., Ratin, M., Partensky, F., Boutte, C., Corguillé, G. L., Marie, D., Blot, N., Gourvil, P., Kolowrat, C., et al. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00285 · Cited by 126 · see citing works
Ghosh, A., Pareek, A., Sopory, S. K., & Singla-Pareek, S. L. (2014) · The Plant Journal · doi:10.1111/tpj.12621 · Cited by 125 · see citing works
Xu, Y., Alvey, R. M., Byrne, P. O., Graham, J. E., Shen, G., & Bryant, D. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-925-3_21 · Cited by 124 · see citing works
In Vivo Role of Catalase-Peroxidase in Synechocystis sp. Strain PCC 6803
Tichý, M., & Vermaas, W. F. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.6.1875-1882.1999 · Cited by 121 · see citing works
How did life survive Earth's great oxygenation?
Fischer, W. W., Hemp, J., & Valentine, J. S. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.03.013 · Cited by 121 · see citing works
Götz, T., Windhövel, U., Böger, P., & Sandmann, G. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.120.2.599 · Cited by 117 · see citing works
The DpsA Protein of Synechococcus sp. Strain PCC7942 Is a DNA-binding Hemoprotein
Peña, M. M. O., & Bullerjahn, G. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.38.22478 · Cited by 116 · see citing works
Oyamada, C., Kaneniwa, M., Ebitani, K., Murata, M., & Ishihara, K. (2008) · Marine Biotechnology · doi:10.1007/s10126-007-9043-z · Cited by 115 · see citing works
Zhu, Y., Graham, J. E., Ludwig, M., Xiong, W., Alvey, R. M., Shen, G., & Bryant, D. A. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.07.007 · Cited by 114 · see citing works
Kobayashi, M., Ishizuka, T., Katayama, M., Kanehisa, M. I., Bhattacharyya‐Pakrasi, M., Pakrasi, H. B., & Ikeuchi, M. (2004) · Plant and Cell Physiology · doi:10.1093/pcp/pch034 · Cited by 114 · see citing works
Viveros, M. F. Á., Inostroza‐Blancheteau, C., Timmermann, T., González, M., & Arce‐Johnson, P. (2013) · Molecular Biology Reports · doi:10.1007/s11033-012-2403-4 · Cited by 114 · see citing works
Pospı́šil, P., Prasad, A., & Rác, M. (2019) · Biomolecules · doi:10.3390/biom9070258 · Cited by 114 · see citing works
Wang, J., Zhu, J., Liu, S., Liu, B., Gao, Y., & Wu, Z. (2011) · Chemosphere · doi:10.1016/j.chemosphere.2011.06.076 · Cited by 113 · see citing works
Probing the structure and bifunctionality of catalase-peroxidase (KatG)
Smulevich, G., Jakopitsch, C., Droghetti, E., & Obinger, C. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.01.033 · Cited by 113 · see citing works
Microbial aldo-keto reductases
Ellis, E. M. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11425.x · Cited by 113 · see citing works
Cameron, J. C., & Pakrasi, H. B. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.162990 · Cited by 113 · see citing works
Vicente, J. B., Gomes, C. M., Wasserfallen, A., & Teixeira, M. S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00434-5 · Cited by 111 · see citing works
Anti-oxidative Stress System in Cyanobacteria
Hosoya‐Matsuda, N., Motohashi, K., Yoshimura, H., Nozaki, A., Inoue, K., Ohmori, M., & Hisabori, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411493200 · Cited by 110 · see citing works
Herbert, S., Samson, G., FORK, D. C., & Laudenbach, D. E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8716 · Cited by 110 · see citing works
Jagt, D. L. V., Hassebrook, R. K., Hunsaker, L. A., Brown, W. M., & Royer, R. E. (2001) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00298-2 · Cited by 107 · see citing works
Avoiding high-valent iron intermediates: Superoxide reductase and rubrerythrin
Kurtz, D. M. J. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.12.017 · Cited by 106 · see citing works
Matsui, K., Nazifi, E., Kunita, S., Wada, N., Matsugo, S., & Sakamoto, T. (2011) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2011.07.003 · Cited by 104 · see citing works
The glutathione transferase kappa family
Morel, F., & Aninat, C. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.556122 · Cited by 100 · see citing works
Subcellular compartmentation of glutathione in dicotyledonous plants
Zechmann, B., & Müller, M. (2010) · PROTOPLASMA · doi:10.1007/s00709-010-0111-2 · Cited by 100 · see citing works
Origins of Life on the Earth and in the Cosmos
Zubay, G. (2000) · Elsevier eBooks · doi:10.1016/b978-0-12-781910-5.x5000-0 · Cited by 99 · see citing works
Antioxidant properties and polyphenolic content in terrestrial cyanobacteria
Singh, D. P., Prabha, R., Verma, S., Meena, K. K., & Yandigeri, M. S. (2017) · 3 Biotech · doi:10.1007/s13205-017-0786-6 · Cited by 99 · see citing works
Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803
Yamamoto, H., Miyake, C., Dietz, K., Tomizawa, K., Murata, N., & Yokota, A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00309-9 · Cited by 98 · see citing works
Gattungen einzelliger Algen physiologisch und systematisch bearbeitet,
N©Þgeli, C. (1849) · doi:10.5962/bhl.title.142975 · Cited by 94 · see citing works
Photosynthesis Research Protocols
Carpentier, R. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-925-3 · Cited by 94 · see citing works
Ultraviolet Light in Human Health, Diseases and Environment
Ahmad, S. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-56017-5 · Cited by 94 · see citing works
Comparative analysis of cyanobacterial superoxide dismutases to discriminate canonical forms
Priya, B., Jagadeesan, P., Dhanalakshmi, R. T., Seethalakshmi, T., Uma, L., Prabaharan, D., & Subramanian, G. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-435 · Cited by 93 · see citing works
Kong, W., Shiota, S., Shi, Y., Nakayama, H., & Nakayama, K. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510107 · Cited by 93 · see citing works
Fan-Yun, L. I. N., Xu, J., Shi, J., Li, H., & Li, B. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9578-3 · Cited by 92 · see citing works
Zang, T. M., Hollman, D. A., Crawford, P. A., Crowder, M. W., & Makaroff, C. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005090200 · Cited by 91 · see citing works
Soule, T. T., García‐Pichel, F., & Stout, V. (2009) · Journal of Bacteriology · doi:10.1128/jb.00134-09 · Cited by 90 · see citing works
Chrismas, N. A. M., Anesio, A. M., & Sánchez‐Baracaldo, P. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01070 · Cited by 90 · see citing works
Isolation of methylglyoxal synthase from goat liver.
Ray, S., & Ray, M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69151-9 · Cited by 89 · see citing works
He, P., & Moran, G. R. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.06.006 · Cited by 89 · see citing works
Hasim, S., Hussin, N. A., Alomar, F. A., Bidasee, K. R., Nickerson, K. W., & Wilson, M. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505784 · Cited by 87 · see citing works
Glyoxalase Goes Green: The Expanding Roles of Glyoxalase in Plants
Sankaranarayanan, S., Jamshed, M., Abhinandan, K., Skori, L., Scandola, S., Wang, T., Spiegel, D. A., & Samuel, M. A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040898 · Cited by 86 · see citing works
Photosynthetic production of hydrogen peroxide by Ulva rigida C. Ag. (Chlorophyta)
Collén, J., del Río, M. J., Garcia-Reina, G., & Pedersén, M. (1995) · Planta · doi:10.1007/bf00201378 · Cited by 85 · see citing works
Comparative proteomics unveils cross species variations in Anabaena under salt stress
Rai, S., Agrawal, C., Shrivastava, A. K., Singh, P. K., & Rai, L. C. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2013.12.020 · Cited by 85 · see citing works
Self-citationNovel glyoxalases from A rabidopsis thaliana
Kwon, K., Choi, D., Hyun, J., Jung, H. S., Baek, K., & Park, C. (2013) · FEBS Journal · doi:10.1111/febs.12321 · Cited by 84 · see citing works
Ghosh, A., & Islam, T. (2016) · BMC Plant Biology · doi:10.1186/s12870-016-0773-9 · Cited by 84 · see citing works
Manganese and the Evolution of Photosynthesis
Fischer, W. W., Hemp, J., & Johnson, J. E. (2015) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-015-9442-5 · Cited by 81 · see citing works
Proteomic De-Regulation in Cyanobacteria in Response to Abiotic Stresses
Babele, P. K., Kumar, J., & Chaturvedi, V. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01315 · Cited by 81 · see citing works
Narainsamy, K., Farci, S., Braun, E. J., Junot, C., Cassier‐Chauvat, C., & Chauvat, F. (2015) · Molecular Microbiology · doi:10.1111/mmi.13296 · Cited by 80 · see citing works
S‐Glutathionylation of Keap1: a new role for glutathioneS‐transferase pi in neuronal protection
Carvalho, A. N., Marques, C., Guedes, R. C., Castro‐Caldas, M., Rodrigues, E., van Horssen, J., & Gama, M. J. (2016) · FEBS Letters · doi:10.1002/1873-3468.12177 · Cited by 80 · see citing works
Unusual Cys-Tyr Covalent Bond in a Large Catalase
Díaz-Vilchis, A., Horjales, E., Rudiño-Piñera, E., Arreola, R., & Hansberg, W. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.027 · Cited by 77 · see citing works
Thomas, D. J., Avenson, T. J., Thomas, J. B., & Herbert, S. K. (1998) · PLANT PHYSIOLOGY · doi:10.1104/pp.116.4.1593 · Cited by 77 · see citing works
Stork, T., Michel, K., Pistorius, E. K., & Dietz, K. (2005) · Journal of Experimental Botany · doi:10.1093/jxb/eri316 · Cited by 77 · see citing works
Evaluation of the Antioxidant Activity of Cell Extracts from Microalgae
Guedes, A. C., Gião, M. S., Seabra, R., Ferreira, A. L. A., Tamagnini, P., Moradas‐Ferreira, P., & Malcata, F. X. (2013) · Marine Drugs · doi:10.3390/md11041256 · Cited by 77 · see citing works
Cyanobacterial heat-shock response: role and regulation of molecular chaperones
Rajaram, H., Chaurasia, A. K., & Apte, S. K. (2014) · Microbiology · doi:10.1099/mic.0.073478-0 · Cited by 77 · see citing works
Glyoxalase system in yeasts: Structure, function, and physiology
Inoue, Y., Maeta, K., & Nomura, W. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.02.002 · Cited by 73 · see citing works
Mudimu, O., Koopmann, I. K., Rybalka, N., Friedl, T., Schulz, R., & Bilger, W. (2017) · Journal of Applied Phycology · doi:10.1007/s10811-017-1188-1 · Cited by 72 · see citing works
Mutsuda, M., Ishikawa, T., Takeda, T., & Shigeoka, S. (1996) · Biochemical Journal · doi:10.1042/bj3160251 · Cited by 71 · see citing works
Li, T., Huang, X., Zhou, R., Liu, Y., Li, B., Nomura, C. T., & Zhao, J. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.18.5096-5103.2002 · Cited by 71 · see citing works
Perelman, A., Uzan, A., Hacohen, D., & Schwarz, R. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.12.3654-3660.2003 · Cited by 69 · see citing works
Structural Biology of the Aldo-Keto Reductase Family of Enzymes: Catalysis and Cofactor Binding
Sanli, G., Dudley, J. I., & Blaber, M. (2003) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:38:1:79 · Cited by 69 · see citing works
Wiktelius, E., & Stenberg, G. (2007) · Biochemical Journal · doi:10.1042/bj20070328 · Cited by 67 · see citing works
Ni, Y., Li, C., Ma, H., Zhang, J., & Xu, J. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2941-4 · Cited by 66 · see citing works
Tozum, S. R. D., & Gallon, J. (1979) · Journal of General Microbiology · doi:10.1099/00221287-111-2-313 · Cited by 66 · see citing works
Sinha, R. P., Klisch, M., Vaishampayan, A., & Häder, D. (1999) · Acta Protozoologica · Cited by 64 · see citing works
Suttisansanee, U., & Honek, J. F. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.02.004 · Cited by 62 · see citing works
Gaber, A., Tamoi, M., Takeda, T., Nakano, Y., & Shigeoka, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02517-0 · Cited by 61 · see citing works
Zhao, W., Ye, Z., & Zhao, J. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05994.x · Cited by 61 · see citing works
Obinger, C., Regelsberger, G., Strasser, G., Burner, U., & Peschek, G. A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6847 · Cited by 61 · see citing works
Banerjee, M., Raghavan, P. S., Ballal, A. D., Rajaram, H., & Apte, S. K. (2013) · Photosynthesis Research · doi:10.1007/s11120-013-9929-8 · Cited by 61 · see citing works
Clugston, S. L., Yajima, R., & Honek, J. F. (2004) · Biochemical Journal · doi:10.1042/bj20030271 · Cited by 61 · see citing works
Ryan-Keogh, T. J., Macey, A. I., Cockshutt, A. M., Moore, C. M., & Bibby, T. S. (2011) · Journal of Phycology · doi:10.1111/j.1529-8817.2011.01092.x · Cited by 61 · see citing works
Baran, R., Ivanova, N., Jose, N., García‐Pichel, F., Kyrpides, N. C., Gugger, M. F., & Northen, T. R. (2013) · Marine Drugs · doi:10.3390/md11103617 · Cited by 61 · see citing works
Serrano, A., Rivas, J., & Losada, M. (1984) · Journal of Bacteriology · doi:10.1128/jb.158.1.317-324.1984 · Cited by 60 · see citing works
Benov, L., Kredich, N. M., & Fridovich, I. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.35.21037 · Cited by 60 · see citing works
Convergent Evolution of Ergothioneine Biosynthesis in Cyanobacteria
Liao, C., & Seebeck, F. P. (2017) · ChemBioChem · doi:10.1002/cbic.201700354 · Cited by 58 · see citing works
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The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes
Cassier‐Chauvat, C., Marceau, F., Farci, S., Ouchane, S., & Chauvat, F. (2023) · Antioxidants · doi:10.3390/antiox12061199 · Cited by 126 · see citing works
Jalil, S., Alghanem, S. M. S., AL‐Huqail, A. A., Nazir, M. M., Zulfiqar, F., Ahmed, T., Ali, S., Abeed, A. H. A., Siddique, K. H. M., & Jin, X. (2023) · Chemosphere · doi:10.1016/j.chemosphere.2023.139566 · Cited by 72 · see citing works
Liu, S., Liu, W., Lai, J., Liu, Q., Zhang, W., Chen, Z., Gao, J., Song, S., Liu, J., & Xiao, Y. (2022) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2022.04.028 · Cited by 53 · see citing works
Yu, B., Zhang, Y., Wu, H., Yan, W., Meng, Y., Hu, C., Liu, Z., Ding, J., & Zhang, H. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.167650 · Cited by 35 · see citing works
Wang, Y., Chen, C., He, C., Dong, W., Yang, X., Wu, Y., Liu, J., Kong, Q., He, J., & Yan, B. (2023) · Materials & Design · doi:10.1016/j.matdes.2023.112620 · Cited by 33 · see citing works
Guo, L., Long, L., Wang, X., Cheng, T., Wang, H., & Ruan, Y. (2023) · BMC Plant Biology · doi:10.1186/s12870-023-04089-y · Cited by 32 · see citing works
Engineering plant family TPS into cyanobacterial host for terpenoids production
Rautela, A., & Kumar, S. (2022) · Plant Cell Reports · doi:10.1007/s00299-022-02892-9 · Cited by 31 · see citing works
The role of microbial partners in heavy metal metabolism in plants: a review
Fu, S., Iqbal, B., Li, G., Alabbosh, K. F., Khan, K. A., Zhao, X., Raheem, A., & Du, D. (2024) · Plant Cell Reports · doi:10.1007/s00299-024-03194-y · Cited by 27 · see citing works
Hou, Y., Zeng, W., Ao, C., & Huang, J. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.02.004 · Cited by 22 · see citing works
Shivani, S., Grewal, S. K., Gill, R. K., Virk, H. K., & Bhardwaj, R. D. (2022) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2022.02.007 · Cited by 21 · see citing works
Amin, N., Jaiswal, M., & Kannaujiya, V. K. (2024) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2024.109186 · Cited by 18 · see citing works
Liu, X., Keyhani, N. O., Liu, H., Zhang, Y., Xia, Y., & Cao, Y. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012431 · Cited by 17 · see citing works
Liu, J., Wang, S., Yi, R., Long, X., Luo, G., Zhao, X., & He, Y. (2022) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-022-09991-9 · Cited by 15 · see citing works
Guo, Z., Hu, J., Li, J., & Xia, X. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.138671 · Cited by 14 · see citing works
Modulating plant-soil microcosm with green synthesized ZnONPs in arsenic contaminated soil
Rehman, A. U., Rahman, S. U., Li, P., Shah, I. H., Manzoor, M. A., Azam, M., Cao, J., Malik, M. S., Jeridi, M., Ahmad, N., et al. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.134130 · Cited by 13 · see citing works
Timson, R. C., Khan, A., Uygur, B., Saad, M., Yeh, H.-W., DelGaudio, N. L., Weber, R. A., Alwaseem, H., Gao, J., Yang, C., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105645 · Cited by 11 · see citing works
Salinity pretreatment synergies heat shock toxicity in cyanobacterium Anabaena PCC7120
Srivastava, R., Kanda, T., Yadav, S., Singh, N., Yadav, S., Prajapati, R., Kesari, V., & Atri, N. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1061927 · Cited by 9 · see citing works
Lao, A., Wu, H., Huang, X., Huang, K., Luo, X., & Zheng, Z. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.173904 · Cited by 9 · see citing works
Ainas, M., Touzout, N., Tahraoui, H., Mokeddem, H. E., Moussa, H., Kherbouche, S., Mebrouk, S., Zhang, J., & Amrane, A. (2025) · Ecotoxicology · doi:10.1007/s10646-025-02888-7 · Cited by 8 · see citing works
“Furthermore, malondialdehyde (MDA) contents serve as a key biomarker of oxidative injury in microalgal cell membranes, which are rich in polyunsaturated fatty acids prone to oxidation (Rai et al. 2021).”
Touzout, N., Tahraoui, H., Lekmine, S., Benchidi, T., Bouchibane, M., Ahmad, I., Mihoub, A., Moussa, H., Danish, S., & Amrane, A. (2025) · Water Air & Soil Pollution · doi:10.1007/s11270-025-08171-z · Cited by 7 · see citing works
Weiss, E. L., Fang, M., Taton, A., Szubin, R., Palsson, B. Ø., Mitchell, B. G., & Golden, S. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2211789119 · Cited by 6 · see citing works
Arnold, N. D., Paper, M., Fuchs, T., Ahmad, N., Jung, P., Lakatos, M., Rodewald, K., Rieger, B., Qoura, F., Kandawa‐Schulz, M., et al. (2024) · MicrobiologyOpen · doi:10.1002/mbo3.70000 · Cited by 6 · see citing works
Nivedha, R. M., & Prasanna, R. (2025) · Archives of Microbiology · doi:10.1007/s00203-025-04449-2 · Cited by 6 · see citing works
Cai, Y., Zhang, X., Qian, H., Huang, G., & Yan, T. (2024) · Metabolic Brain Disease · doi:10.1007/s11011-024-01449-x · Cited by 6 · see citing works
Khalofah, A., Khan, M. Q. N., & Hayat, H. S. (2025) · Journal of soil science and plant nutrition · doi:10.1007/s42729-025-02450-8 · Cited by 6 · see citing works
Behera, A. K., Parida, S., Mandal, A. K., Patra, S., & Jena, M. (2025) · Archives of Microbiology · doi:10.1007/s00203-025-04462-5 · Cited by 6 · see citing works
Li, B., Li, J., Gao, J., Guo, Z., & Li, J. (2023) · Chemosphere · doi:10.1016/j.chemosphere.2023.139365 · Cited by 5 · see citing works
Abiotic Stress Tolerance in Plants by Genome Editing Applications
Urhan, E. K. (2023) · Wiley eBooks · doi:10.1002/9781394183913.ch10 · Cited by 5 · see citing works
Unraveling the Constrained Cell Growth in Engineered Living Materials
Sun, S.-S., Ding, C.-C., Yu, H., Yuan, X.-Z., Wang, S., & Xia, P. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00378 · Cited by 3 · see citing works
Stress genomics of the toxigenic cyanobacteria: environmental and biotechnological perspectives
Srivastava, A., Chot, E., Gupta, V., Singhvi, N., & Shukla, P. (2025) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-025-04509-1 · Cited by 3 · see citing works
Responses to arsenic stress by the Andean benthic-extremophile cyanobacteria Rivularia halophila
Rueda, E. S., Borgnino, L., Bia, G. L., Gil, P. I., Bisbal, M., Pietrasiak, N., & Mlewski, E. C. (2023) · Algal Research · doi:10.1016/j.algal.2023.103286 · Cited by 3 · see citing works
Ji, K., Zhang, Y., Zhang, T., Li, D., Yuan, Y., Wang, L., Huang, Q., & Chen, W. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00564-24 · Cited by 2 · see citing works
Genetic engineering to improve resistance against heavy metal stress in Synechocystis sp. PCC 6803
Yang, Y., Zheng, C., Gao, L., Jiang, X., Xu, J., Zhang, W., Peng, Y., Han, J., Sun, M., Ma, W., et al. (2026) · Applied and Environmental Microbiology · doi:10.1128/aem.02473-25 · Cited by 2 · see citing works
Haroon, M., Wang, L., Yu, H., Zhou, X., Basit, A., Awan, K. M., Malik, O., Raza, S., Ahmad, D., & Vatsadze, S. Z. (2026) · European Polymer Journal · doi:10.1016/j.eurpolymj.2026.114681 · Cited by 2 · see citing works
Microbial Antioxidants in Food Products
Sood, D., Devi, S., Devi, B., & Arya, P. (2022) · Microorganisms for sustainability · doi:10.1007/978-981-19-5711-6_3 · Cited by 2 · see citing works
Stefano, G. D., Fagliarone, C., Locato, V., Giacinti, V., Rigano, G., Gara, L. D., & Billi, D. (2025) · Algal Research · doi:10.1016/j.algal.2025.104287 · Cited by 1 · see citing works
Maurya, N., Sharma, A., Jaiswal, S., & Sundaram, S. (2025) · International Microbiology · doi:10.1007/s10123-025-00731-x · Cited by 1 · see citing works
Yao, L., Cao, Q., You, B., Yan, J., & Zhang, L. (2025) · Environmental Earth Sciences · doi:10.1007/s12665-025-12684-5 · Cited by 1 · see citing works
Li, C., Chen, Z., Chen, L., Jin, Y., Wang, Z., & Wang, G. (2025) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2025.110769 · Cited by 1 · see citing works
Unveiling a novel broad-host-range cyanomyovirus cross-infecting Prochlorococcus and Synechococcus
Wei, S., Cai, L., Zheng, H., Wei, S., Xu, B., Zhang, R., Xu, Y., & Li, J. (2025) · BMC Biology · doi:10.1186/s12915-025-02481-8 · Cited by 1 · see citing works
In-depth comparative transcriptome analysis of Purpureocillium sp. CB1 under cadmium stress
Kurt‐Kızıldoğan, A., Otur, Ç., Yıldırım, K., Kavas, M., & Abanoz-Seçgin, B. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12655-5 · Cited by 1 · see citing works
Yan, H., & Senavirathna, M. D. H. J. (2023) · Microorganisms · doi:10.3390/microorganisms11112760 · Cited by 1 · see citing works
Molecular Identification of Some Selected Cyanobacteria and Their Antioxidant Activities
Dedvisitsakul, P., Watla‐iad, K., Chittapun, S., Charoenrat, T., & Piyapittayanun, C. (2024) · Trends in Sciences · doi:10.48048/tis.2025.8950 · Cited by 1 · see citing works
A mouse model to study glutathione limitation in vivoPreprint
Timson, R. C., Khan, A., Uygur, B., Saad, M., Yeh, H.-W., DelGaudio, N. L., Weber, R. A., Alwaseem, H., Gao, J., Yang, C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.08.574722 · Cited by 1 · see citing works
Antioxidant profiling of cyanobacterial bioactive compounds
Singh, V. K., Jha, S., Rana, P., Tripathi, R., Singh, A. P., & Sinha, R. P. (2024) · Food Nutrition Chemistry · doi:10.18686/fnc254
Unravelling the constrained cell growth in engineered living materialsPreprint
Sun, S.-S., Ding, C.-C., Yu, H., Yuan, X.-Z., Wang, S., & Xia, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.21.655284
Eutrophication level constrains treatment efficacy of calcium peroxide in aquatic environments
Zhang, Y., Fang, L., Qi, Q., Tian, C., Wan, D., Song, G., Mi, W., Huang, W., Bi, Y., & Liu, C. (2025) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2025.118846
Guo, L., Ling, L., Wang, X., Cheng, T., Wang, H., & Ruan, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26565627
Leveraging Cyanobacteria for Alleviating Climate Change-Induced Abiotic Stress in Crop Plants
Rani, V., Jaiswal, P., Mahawar, H., Khati, P., Arora, A., & Musa, I. O. (2026) · Springer eBooks · doi:10.1007/978-981-95-8883-1_15
Yadav, A., Singh, L. A., Sharma, S., Bhardwaj, R., Kumari, P., Swapnil, P., & Meena, M. (2026) · Scientific Reports · doi:10.1038/s41598-026-57838-y
Bácsi, I., Riba, M., Márton, K., B‐Béres, V., T‐Krasznai, E., Pirger, Z., & Vasas, G. (2026) · Harmful Algae · doi:10.1016/j.hal.2026.103181
- Authors
- Rai, R., Singh, S., Rai, K. K., Raj, A., Sriwastaw, S., & Rai, L. C.
- Affiliations
- Banaras Hindu University (IN)
- Corresponding author
- Rai, L.C.
- Venue
- Plant Physiology and Biochemistry
- Publisher
- Elsevier BV
- Published
- 2021-11
- Volume
- 168
- Pages
- 353-372
- ISSN
- 0981-9428 (ISSN-L)
- OpenAlex
- W3205425525
- Cited by
- 51
- References
- 309
- Citations by year
- 2026: 5 · 2025: 15 · 2024: 14 · 2023: 11 · 2022: 6
- FWCI
- 0.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Plant Physiology and Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Keywords
- cyanobacteria, oxidative stress, reactive oxygen species, methylglyoxal, glyoxalase system, antioxidant defense, glutathione, abiotic stress, glyoxalase I, glyoxalase II, detoxification
- MeSH terms
- Cyanobacteria, Antioxidants, Plants, Pyruvaldehyde, Reactive Oxygen Species
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