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Cystatins. --- Cysteine proteinases --- Cystatin superfamily --- Proteins --- Inhibitors. --- Inhibitors

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Cysteine proteases expressed by pathogenic organisms play key roles in virulence including host entry, feeding and suppression of host immune responses. This book gives comprehensive coverage to all aspects of pathogen cysteine proteases and brings together numerous scientific advances which have been made over many years. Thus, the biochemistry, molecular biology and structure‑function relationships of these important pathogen enzymes are covered in detail. Written by leading researchers from Europe, Australia and North America, this book is essential reading for students and professionals interested in human medicine and infectious disease research.

Cysteine proteinases -- Pathophysiology. --- Microbial enzymes. --- Pathogenic microorganisms. --- Cysteine proteinases --- Microbial enzymes --- Pathogenic microorganisms --- Natural Science Disciplines --- Organisms --- Peptide Hydrolases --- Hydrolases --- Disciplines and Occupations --- Enzymes --- Enzymes and Coenzymes --- Chemicals and Drugs --- Chemistry --- Bacteria --- Eukaryota --- Viruses --- Cysteine Proteases --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Pathophysiology --- Pathophysiology. --- Disease-causing microorganisms --- Micro-organisms, Pathogenic --- Pathogens --- Medicine. --- Molecular biology. --- Biomedicine. --- Biomedicine general. --- Molecular Medicine. --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Microorganisms --- Medical microbiology --- Virulence (Microbiology) --- Microbiological chemistry --- Proteinase --- Health Workforce --- Biomedicine, general.

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Hydrogen sulfide (H2S), which was previously considered to be toxic, is now regarded as a burgeoning endogenous gaseous transmitter. H2S plays a vital role in the mechanism of response/adaptation to adverse environmental conditions as well as crosstalk with other signaling molecules, including ROS, by affecting the corresponding gene expression and subsequent enzyme activities. Both H2S and ROS are potent signaling molecules that can provoke reversible and irreversible oxidative post-translational modifications on cysteine residues of proteins such as sulfenylation or persulfidation, affecting the redox status and function of the target proteins. The dynamic interplay between persulfidation and sulfenylation occurring on cysteine residues is of great importance in response to environmental changes.The present Special Issue of IJMS has the aim of providing the most current findings on the function of signaling molecules, including H2S and ROS, in higher plants, and it is open to different types of manuscripts, including original research papers, perspectives, or reviews where either ROS, H2S, or related molecules could be involved at the biochemical or physiological levels.

Mathematics & science --- Biology, life sciences --- Molecular biology --- antioxidant defense systems --- Cd stress --- hydrogen sulfide --- melatonin --- oxidative stress --- transportation and sequestration --- nitric oxide --- abscisic acid --- Ca2+ --- hydrogen peroxide --- abiotic stresses --- signal transmitters --- stomatal movement --- persulfidation --- drought stress --- nitrate reductase --- l-cysteine desulfhydrase --- chilling stress --- indole-3-acetic acid --- signaling pathway --- calcium deficiency --- endogenous H2S --- reactive oxygen species --- ERF2-bHLH2-CML5 module --- postharvest storage quality --- tomato --- cysteine desulfhydrase --- leaf senescence --- ARF --- auxin --- cold stress --- cucumber --- DREB --- module --- resistance --- root growth --- heavy metal --- salt --- DES1 --- ABI4 --- protein stability --- Brassica rapa --- mercury --- selenium --- biotic stress --- abiotic stress --- salicylic acid --- jasmonic acid --- ethylene --- phytohormones --- Arabidopsis --- manganese stress --- L-cysteine desulfhydrase --- antioxidant enzyme --- Allium --- garlic --- gas detector --- ion-selective microelectrode --- isozymes --- RBOHs --- signaling networks --- n/a

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The endoplasmic reticulum (ER) is a manufacturing unit in eukaryotic cells required for the synthesis of proteins, lipids, metabolites and hormones. Besides supporting cellular signalling networks by its anabolic function, the ER on its own or in communication with other organelles directly initiates signalling processes of physiological significance. Based on the intimate and immediate involvement in stress signalling the ER is considered as sensory organelle on which cells strongly rely to effectively translate environmental cues into adaptive stress responses. The transcellular distribution of the ER providing comprehensive cell-to-cell connections in multicellular organisms probably allows a concerted action of cell alliances and tissue areas towards environmental constraints. At the cellular level, stress adaptation correlates with the capability of the ER machinery to synthesise proteins participating in stress signalling as well as in the activation of ER membrane localised proteins to start cell-protective signalling processes. Importantly, depending on the stress insult, the ER either supports protective strategies or initiates cell death programmes. Recent, genetic, molecular and cell biological studies have drawn an initial picture of underlying signalling events activated by ER membrane localised proteins. In this Research Topic, we will provide a platform for articles describing research on ER morphology and metabolism with a focus on stress translation. The Research Topic will be sub-divided into the following sections: 1. ER in stress signalling and adaptation; 2. ER structure and biosynthetic functions; 3. Regulation of protein processing; 4. Regulation of programmed cell death.

Endoplasmic reticulum. --- Botany. --- Endoplasmic Reticulum Stress. --- Stress, Endoplasmic Reticulum --- Endoplasmic Reticulum Stresses --- Reticulum Stress, Endoplasmic --- Reticulum Stresses, Endoplasmic --- Stresses, Endoplasmic Reticulum --- Unfolded Protein Response --- Endoplasmic Reticulum-Associated Degradation --- Botanical science --- Floristic botany --- Phytobiology --- Phytography --- Phytology --- Plant biology --- Plant science --- Biology --- Natural history --- Plants --- Cell organelles --- Myosins --- cysteine endopeptidase --- ER associated degradation --- ER bodies --- programmed cell death --- bZIP transcription factors --- caspase

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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