| 000 | 04963naaaa2201213uu 4500 | ||
|---|---|---|---|
| 001 | https://directory.doabooks.org/handle/20.500.12854/60894 | ||
| 005 | 20220220100035.0 | ||
| 020 | _abooks978-3-03897-837-4 | ||
| 020 | _a9783038978374 | ||
| 020 | _a9783038978367 | ||
| 024 | 7 |
_a10.3390/books978-3-03897-837-4 _cdoi |
|
| 041 | 0 | _aEnglish | |
| 042 | _adc | ||
| 100 | 1 |
_aZaffagnini, Mirko _4auth |
|
| 700 | 1 |
_aJacquot, Jean-Pierre _4auth |
|
| 245 | 1 | 0 | _aThioredoxin and Glutaredoxin Systems |
| 260 |
_bMDPI - Multidisciplinary Digital Publishing Institute _c2019 |
||
| 300 | _a1 electronic resource (280 p.) | ||
| 506 | 0 |
_aOpen Access _2star _fUnrestricted online access |
|
| 520 | _aThis 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. | ||
| 540 |
_aCreative Commons _fhttps://creativecommons.org/licenses/by-nc-nd/4.0/ _2cc _4https://creativecommons.org/licenses/by-nc-nd/4.0/ |
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| 546 | _aEnglish | ||
| 653 | _an/a | ||
| 653 | _aregeneration | ||
| 653 | _aposttranslational modification | ||
| 653 | _aH2O2 | ||
| 653 | _achilling stress | ||
| 653 | _athioredoxin reductase | ||
| 653 | _aX-ray crystallography | ||
| 653 | _aphotosynthesis | ||
| 653 | _aChlamydomonas reinhardtii | ||
| 653 | _aprotein | ||
| 653 | _amonodehydroascorbate reductase | ||
| 653 | _amethionine sulfoxide | ||
| 653 | _acysteine reactivity | ||
| 653 | _asymbiosis | ||
| 653 | _aplant | ||
| 653 | _aMALDI-TOF mass spectrometry | ||
| 653 | _athioredoxins | ||
| 653 | _aredox homeostasis | ||
| 653 | _amethionine sulfoxide reductases | ||
| 653 | _aredox | ||
| 653 | _aredox signalling | ||
| 653 | _achloroplast | ||
| 653 | _aprotein-protein recognition | ||
| 653 | _acyanobacteria | ||
| 653 | _aspecificity | ||
| 653 | _awheat | ||
| 653 | _amethanoarchaea | ||
| 653 | _astress | ||
| 653 | _aredox regulation | ||
| 653 | _adough rheology | ||
| 653 | _amethionine sulfoxide reductase | ||
| 653 | _aelectrostatic surface | ||
| 653 | _aCalvin cycle | ||
| 653 | _aALAD | ||
| 653 | _ametazoan | ||
| 653 | _aArabidopsis thaliana | ||
| 653 | _abaking | ||
| 653 | _acold temperature | ||
| 653 | _amacromolecular crystallography | ||
| 653 | _aprotein oxidation | ||
| 653 | _afunction | ||
| 653 | _amethionine oxidation | ||
| 653 | _adevelopment | ||
| 653 | _airon–sulfur cluster | ||
| 653 | _atetrapyrrole biosynthesis | ||
| 653 | _alegume plant | ||
| 653 | _aglutathionylation | ||
| 653 | _aCalvin-Benson cycle | ||
| 653 | _aadult stem cells | ||
| 653 | _acarbon fixation | ||
| 653 | _aplastidial | ||
| 653 | _amethionine | ||
| 653 | _aredox active site | ||
| 653 | _aROS | ||
| 653 | _awater stress | ||
| 653 | _aNADPH | ||
| 653 | _arepair | ||
| 653 | _aphysiological function | ||
| 653 | _asignaling | ||
| 653 | _athioredoxin | ||
| 653 | _aantioxidants | ||
| 653 | _aglutathione | ||
| 653 | _aglutaredoxin | ||
| 653 | _aflavin | ||
| 653 | _aIsocitrate dehydrogenase | ||
| 653 | _athiol redox network | ||
| 653 | _aageing | ||
| 653 | _adisulfide | ||
| 653 | _amitochondria | ||
| 653 | _achlorophyll | ||
| 653 | _aproteomic | ||
| 653 | _acysteine alkylation | ||
| 653 | _aferredoxin-thioredoxin reductase | ||
| 653 | _aSAXS | ||
| 653 | _aregulation | ||
| 653 | _aoxidized protein repair | ||
| 653 | _aascorbate | ||
| 653 | _aredox control | ||
| 653 | _anitrosylation | ||
| 856 | 4 | 0 |
_awww.oapen.org _uhttps://mdpi.com/books/pdfview/book/1289 _70 _zDOAB: download the publication |
| 856 | 4 | 0 |
_awww.oapen.org _uhttps://directory.doabooks.org/handle/20.500.12854/60894 _70 _zDOAB: description of the publication |
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_c80083 _d80083 |
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