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In contrast to the situation in heterotrophic organisms, plant genomes code for a significantly larger number of oxidoreductases such as thioredoxins (TRXs) and glutaredoxins (GRXs). These proteins provide a biochemical mechanism that allows the rapid and reversible activation or deactivation of protein functions in response to changing environmental conditions, as oxidative conditions caused by excessive photosynthesis. Indeed, owing to the fact that cysteines are sensitive to oxidation, TRXs and GRXs play an essential role in controlling the redox state of protein thiol groups. These redox-dependent post-translational modifications have proven to be critical for many cellular functions constituting regulatory, signalling or protective mechanisms. The articles contained in this Research Topic provide timely overviews and new insights into thiol-dependent redox regulation mechanisms with a focus on TRX- and GRX-based reduction systems in plants. The different contexts discussed take into account physiological, developmental and environmental conditions.

Homeostasis. --- Thioredoxin. --- Botany. --- redox signaling --- redox regulation --- thioredoxin --- Plants --- glutaredoxin --- Glutathione

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In contrast to the situation in heterotrophic organisms, plant genomes code for a significantly larger number of oxidoreductases such as thioredoxins (TRXs) and glutaredoxins (GRXs). These proteins provide a biochemical mechanism that allows the rapid and reversible activation or deactivation of protein functions in response to changing environmental conditions, as oxidative conditions caused by excessive photosynthesis. Indeed, owing to the fact that cysteines are sensitive to oxidation, TRXs and GRXs play an essential role in controlling the redox state of protein thiol groups. These redox-dependent post-translational modifications have proven to be critical for many cellular functions constituting regulatory, signalling or protective mechanisms. The articles contained in this Research Topic provide timely overviews and new insights into thiol-dependent redox regulation mechanisms with a focus on TRX- and GRX-based reduction systems in plants. The different contexts discussed take into account physiological, developmental and environmental conditions.

Homeostasis. --- Thioredoxin. --- Botany. --- redox signaling --- redox regulation --- thioredoxin --- Plants --- glutaredoxin --- Glutathione

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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.

n/a --- regeneration --- posttranslational modification --- H2O2 --- chilling stress --- thioredoxin reductase --- X-ray crystallography --- photosynthesis --- Chlamydomonas reinhardtii --- protein --- monodehydroascorbate reductase --- methionine sulfoxide --- cysteine reactivity --- symbiosis --- plant --- MALDI-TOF mass spectrometry --- thioredoxins --- redox homeostasis --- methionine sulfoxide reductases --- redox --- redox signalling --- chloroplast --- protein-protein recognition --- cyanobacteria --- specificity --- wheat --- methanoarchaea --- stress --- redox regulation --- dough rheology --- methionine sulfoxide reductase --- electrostatic surface --- Calvin cycle --- ALAD --- metazoan --- Arabidopsis thaliana --- baking --- cold temperature --- macromolecular crystallography --- protein oxidation --- function --- methionine oxidation --- development --- iron–sulfur cluster --- tetrapyrrole biosynthesis --- legume plant --- glutathionylation --- Calvin-Benson cycle --- adult stem cells --- carbon fixation --- plastidial --- methionine --- redox active site --- ROS --- water stress --- NADPH --- repair --- physiological function --- signaling --- thioredoxin --- antioxidants --- glutathione --- glutaredoxin --- flavin --- Isocitrate dehydrogenase --- thiol redox network --- ageing --- disulfide --- mitochondria --- chlorophyll --- proteomic --- cysteine alkylation --- ferredoxin-thioredoxin reductase --- SAXS --- regulation --- oxidized protein repair --- ascorbate --- redox control --- nitrosylation --- iron-sulfur cluster

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This Special Issue examines state-of-the-art in-cell NMR spectroscopy as it relates to biological systems of increasing complexity. The compendia of research and recent innovations from prominent laboratories in the field of solid state and solution in-cell NMR spectroscopy, metabolomics and technology development are presented. The work establishes in-cell NMR spectroscopy as the premier method for determining the structures and interaction capabilities of biological molecules at high resolution within the delicately intricate interior of living cells, and the means of utilizing cells as living laboratories to directly assess the effects of exogenous and endogenous stimuli on cell physiology.]

protein NMR --- time-resolved NMR --- Ribosome --- structural calculation 4 --- crystalline and amorphous starch --- in-cell NMR --- protein dynamics --- DNP --- protein modification --- Tau --- spectrum reconstruction 3 --- mRNA --- Thioredoxin --- protein structure --- protein interactions --- drug discovery --- protein structure determination 1 --- review --- enzyme activity --- MARK2 phosphorylation --- post-translational modifications --- Dihydrofolate reductase --- mammalian cells --- target engagement --- non-uniform sampling 2 --- paramagnetic effects --- protein structure-function --- cross-correlated relaxation --- structure function --- rRNA --- 2D INADEQUATE --- lipid membrane --- Thymidylate synthase --- whole cell NMR --- enzyme kinetics --- magic-angle spinning --- live cell --- solid-state NMR --- Adenylate kinase --- DNA --- in-situ NMR --- antimicrobial peptide --- NMR spectroscopy --- intrinsically disordered proteins

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The trace mineral selenium is still regarded as one of the most interesting and health-beneficial elements. In addition to the Editorial containing a dedication to Dr. Leopold Flohé, this Special Issue contains 13 research articles and 8 reviews, with over 120 different contributors covering many of the most important subjects concerning the study of selenium. The articles address both selenium as well as selenoproteins and their molecular roles, providing important considerations regarding this trace element’s impact on human and animal health and disease.

Research & information: general --- Biology, life sciences --- selenoproteome --- selenoprotein hierarchy --- nonradioactive isotopes --- SEC-ICP MS --- glutathione peroxidase --- thioredoxin reductase --- SECIS --- translation regulation --- autoimmune thyroid disease --- diabetes mellitus --- Graves’ disease --- Hashimoto thyroiditis --- infection --- inflammation --- long-COVID --- rheumatoid arthritis --- selenoprotein P --- sepsis --- selenoprotein W --- thioredoxin --- 14-3-3 --- Akt --- cell death --- Selenof --- selenium --- selenoprotein --- colon cancer --- barrier integrity --- cardiovascular --- heart --- selenoproteins --- Keshan’s Disease --- bacteria --- selenite --- selenium delivery system --- Trsp --- hypothalamus --- Agrp neuron --- sex differences --- diet-induced obesity --- leptin resistance --- macrophage --- differentiation --- redox signaling --- NRF2 --- NF-κB --- lipid mediators --- seleocysteine --- autoimmunity --- lymphocyte --- cadmium cytotoxicity --- cancer therapy --- cisplatin --- ICP-MS --- nonsynonymous mutation --- selenium homeostasis --- ZIP8 --- Trit1 --- isopentenylation --- tRNA[Ser]Sec --- selenocysteine --- genetic variance --- human disease --- selenophosphate synthetase --- endothelial cell --- reactive oxygen species --- cell growth --- angiogenesis --- SEPHS1 --- early embryogenesis --- embryonic lethality --- prostate --- cancer --- tumor suppressor --- selenoprotein deficiency --- SECISBP2 --- Sec-tRNA[Ser]Sec --- SEPSECS --- antioxidative defense --- autoantibody --- Hashimoto’s thyroiditis --- trace element --- recoding --- SECIS-binding protein --- translation termination --- nonsense-mediated decay --- ribosome rescue --- health --- mouse models --- selenocysteine (Sec) --- virus --- viral --- antioxidant --- HIV --- HCV --- HBV --- coxsackie virus --- influenza --- n/a --- HIV-1 --- viral infection --- SELENOS --- SELENOO --- primary T cells --- Jurkat --- SupT1 --- translational control --- Graves' disease --- Keshan's Disease --- Hashimoto's thyroiditis