Thioredoxin and Glutaredoxin Systems
This 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 interacti...
Saved in:
| Main Author: | |
|---|---|
| Other Authors: | |
| Format: | Book Chapter |
| Published: |
MDPI - Multidisciplinary Digital Publishing Institute
2019
|
| Subjects: | |
| Online Access: | Get Fullteks DOAB: description of the publication |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| LEADER | 04871naaaa2201201uu 4500 | ||
|---|---|---|---|
| 001 | doab_20_500_12854_60894 | ||
| 005 | 20210212 | ||
| 020 | |a books978-3-03897-837-4 | ||
| 020 | |a 9783038978374 | ||
| 020 | |a 9783038978367 | ||
| 024 | 7 | |a 10.3390/books978-3-03897-837-4 |c doi | |
| 041 | 0 | |a English | |
| 042 | |a dc | ||
| 100 | 1 | |a Zaffagnini, Mirko |4 auth | |
| 700 | 1 | |a Jacquot, Jean-Pierre |4 auth | |
| 245 | 1 | 0 | |a Thioredoxin and Glutaredoxin Systems |
| 260 | |b MDPI - Multidisciplinary Digital Publishing Institute |c 2019 | ||
| 300 | |a 1 electronic resource (280 p.) | ||
| 506 | 0 | |a Open Access |2 star |f Unrestricted online access | |
| 520 | |a This 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 | |a Creative Commons |f https://creativecommons.org/licenses/by-nc-nd/4.0/ |2 cc |4 https://creativecommons.org/licenses/by-nc-nd/4.0/ | ||
| 546 | |a English | ||
| 653 | |a n/a | ||
| 653 | |a regeneration | ||
| 653 | |a posttranslational modification | ||
| 653 | |a H2O2 | ||
| 653 | |a chilling stress | ||
| 653 | |a thioredoxin reductase | ||
| 653 | |a X-ray crystallography | ||
| 653 | |a photosynthesis | ||
| 653 | |a Chlamydomonas reinhardtii | ||
| 653 | |a protein | ||
| 653 | |a monodehydroascorbate reductase | ||
| 653 | |a methionine sulfoxide | ||
| 653 | |a cysteine reactivity | ||
| 653 | |a symbiosis | ||
| 653 | |a plant | ||
| 653 | |a MALDI-TOF mass spectrometry | ||
| 653 | |a thioredoxins | ||
| 653 | |a redox homeostasis | ||
| 653 | |a methionine sulfoxide reductases | ||
| 653 | |a redox | ||
| 653 | |a redox signalling | ||
| 653 | |a chloroplast | ||
| 653 | |a protein-protein recognition | ||
| 653 | |a cyanobacteria | ||
| 653 | |a specificity | ||
| 653 | |a wheat | ||
| 653 | |a methanoarchaea | ||
| 653 | |a stress | ||
| 653 | |a redox regulation | ||
| 653 | |a dough rheology | ||
| 653 | |a methionine sulfoxide reductase | ||
| 653 | |a electrostatic surface | ||
| 653 | |a Calvin cycle | ||
| 653 | |a ALAD | ||
| 653 | |a metazoan | ||
| 653 | |a Arabidopsis thaliana | ||
| 653 | |a baking | ||
| 653 | |a cold temperature | ||
| 653 | |a macromolecular crystallography | ||
| 653 | |a protein oxidation | ||
| 653 | |a function | ||
| 653 | |a methionine oxidation | ||
| 653 | |a development | ||
| 653 | |a iron-sulfur cluster | ||
| 653 | |a tetrapyrrole biosynthesis | ||
| 653 | |a legume plant | ||
| 653 | |a glutathionylation | ||
| 653 | |a Calvin-Benson cycle | ||
| 653 | |a adult stem cells | ||
| 653 | |a carbon fixation | ||
| 653 | |a plastidial | ||
| 653 | |a methionine | ||
| 653 | |a redox active site | ||
| 653 | |a ROS | ||
| 653 | |a water stress | ||
| 653 | |a NADPH | ||
| 653 | |a repair | ||
| 653 | |a physiological function | ||
| 653 | |a signaling | ||
| 653 | |a thioredoxin | ||
| 653 | |a antioxidants | ||
| 653 | |a glutathione | ||
| 653 | |a glutaredoxin | ||
| 653 | |a flavin | ||
| 653 | |a Isocitrate dehydrogenase | ||
| 653 | |a thiol redox network | ||
| 653 | |a ageing | ||
| 653 | |a disulfide | ||
| 653 | |a mitochondria | ||
| 653 | |a chlorophyll | ||
| 653 | |a proteomic | ||
| 653 | |a cysteine alkylation | ||
| 653 | |a ferredoxin-thioredoxin reductase | ||
| 653 | |a SAXS | ||
| 653 | |a regulation | ||
| 653 | |a oxidized protein repair | ||
| 653 | |a ascorbate | ||
| 653 | |a redox control | ||
| 653 | |a nitrosylation | ||
| 856 | 4 | 0 | |a www.oapen.org |u https://mdpi.com/books/pdfview/book/1289 |7 0 |z Get Fullteks |
| 856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/60894 |7 0 |z DOAB: description of the publication |