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Thioredoxin and Glutaredoxin Systems

dc.contributor.authorZaffagnini, Mirko*
dc.contributor.authorJacquot, Jean-Pierre*
dc.date.accessioned2021-02-12T05:53:27Z
dc.date.available2021-02-12T05:53:27Z
dc.date.issued2019*
dc.date.submitted2019-06-26 08:44:06*
dc.identifier33636*
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/60894
dc.description.abstractThis Special Issue features recent data concerning thioredoxins and glutaredoxins from various biological systems, including bacteria, mammals, and plants. Four of the sixteen articles are review papers that deal with the regulation of development of the effect of hydrogen peroxide and the interactions between oxidants and reductants, the description of methionine sulfoxide reductases, detoxification enzymes that require thioredoxin or glutaredoxin, and the response of plants to cold stress, respectively. This is followed by eleven research articles that focus on a reductant of thioredoxin in bacteria, a thioredoxin reductase, and a variety of plant and bacterial thioredoxins, including the m, f, o, and h isoforms and their targets. Various parameters are studied, including genetic, structural, and physiological properties of these systems. The redox regulation of monodehydroascorbate reductase, aminolevulinic acid dehydratase, and cytosolic isocitrate dehydrogenase could have very important consequences in plant metabolism. Also, the properties of the mitochondrial o-type thioredoxins and their unexpected capacity to bind iron–sulfur center (ISC) structures open new developments concerning the redox mitochondrial function and possibly ISC assembly in mitochondria. The final paper discusses interesting biotechnological applications of thioredoxin for breadmaking.*
dc.languageEnglish*
dc.subjectQH301-705.5*
dc.subjectQ1-390*
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.othern/a*
dc.subject.otherregeneration*
dc.subject.otherposttranslational modification*
dc.subject.otherH2O2*
dc.subject.otherchilling stress*
dc.subject.otherthioredoxin reductase*
dc.subject.otherX-ray crystallography*
dc.subject.otherphotosynthesis*
dc.subject.otherChlamydomonas reinhardtii*
dc.subject.otherprotein*
dc.subject.othermonodehydroascorbate reductase*
dc.subject.othermethionine sulfoxide*
dc.subject.othercysteine reactivity*
dc.subject.othersymbiosis*
dc.subject.otherplant*
dc.subject.otherMALDI-TOF mass spectrometry*
dc.subject.otherthioredoxins*
dc.subject.otherredox homeostasis*
dc.subject.othermethionine sulfoxide reductases*
dc.subject.otherredox*
dc.subject.otherredox signalling*
dc.subject.otherchloroplast*
dc.subject.otherprotein-protein recognition*
dc.subject.othercyanobacteria*
dc.subject.otherspecificity*
dc.subject.otherwheat*
dc.subject.othermethanoarchaea*
dc.subject.otherstress*
dc.subject.otherredox regulation*
dc.subject.otherdough rheology*
dc.subject.othermethionine sulfoxide reductase*
dc.subject.otherelectrostatic surface*
dc.subject.otherCalvin cycle*
dc.subject.otherALAD*
dc.subject.othermetazoan*
dc.subject.otherArabidopsis thaliana*
dc.subject.otherbaking*
dc.subject.othercold temperature*
dc.subject.othermacromolecular crystallography*
dc.subject.otherprotein oxidation*
dc.subject.otherfunction*
dc.subject.othermethionine oxidation*
dc.subject.otherdevelopment*
dc.subject.otheriron–sulfur cluster*
dc.subject.othertetrapyrrole biosynthesis*
dc.subject.otherlegume plant*
dc.subject.otherglutathionylation*
dc.subject.otherCalvin-Benson cycle*
dc.subject.otheradult stem cells*
dc.subject.othercarbon fixation*
dc.subject.otherplastidial*
dc.subject.othermethionine*
dc.subject.otherredox active site*
dc.subject.otherROS*
dc.subject.otherwater stress*
dc.subject.otherNADPH*
dc.subject.otherrepair*
dc.subject.otherphysiological function*
dc.subject.othersignaling*
dc.subject.otherthioredoxin*
dc.subject.otherantioxidants*
dc.subject.otherglutathione*
dc.subject.otherglutaredoxin*
dc.subject.otherflavin*
dc.subject.otherIsocitrate dehydrogenase*
dc.subject.otherthiol redox network*
dc.subject.otherageing*
dc.subject.otherdisulfide*
dc.subject.othermitochondria*
dc.subject.otherchlorophyll*
dc.subject.otherproteomic*
dc.subject.othercysteine alkylation*
dc.subject.otherferredoxin-thioredoxin reductase*
dc.subject.otherSAXS*
dc.subject.otherregulation*
dc.subject.otheroxidized protein repair*
dc.subject.otherascorbate*
dc.subject.otherredox control*
dc.subject.othernitrosylation*
dc.titleThioredoxin and Glutaredoxin Systems*
dc.typebook
oapen.identifier.doi10.3390/books978-3-03897-837-4*
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0*
oapen.relation.isbn9783038978374*
oapen.relation.isbn9783038978367*
oapen.pages280*
oapen.edition1st*


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