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Aldehyde dehydrogenase --- Congresses --- Aldose reductase --- Alcohol dehydrogenase --- Carbonyl compounds --- Metabolism --- ALDEHYDE DEHYDROGENASE --- ALDEHYDE REDUCTASE --- ALCOHOL DEHYDROGENASE --- PHYSIOLOGY

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Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease examines the biochemical protein interactions of the multi-dimensional protein GAPDH, further considering the regulatory mechanisms through which cells control their functional diversity. This protein's diverse activities range from nuclear tRNA export and the maintenance of genomic integrity, to cytoplasmic post-transcriptional control of gene expression and receptor mediated cell signaling, to membrane facilitation of iron metabolism, trafficking and fusion. This book will be of great interest to basic scientists, clinicians and students, including molecular and cell biologists, immunologists, pathologists and clinical researchers who are interested in the biochemistry of GAPDH in health and disease.--

Glycolysis. --- Aldehyde dehydrogenase. --- Aldehyde oxidoreductase --- Dehydrogenases --- Glucolysis --- Blood --- Pathology --- Sugar in the body --- Examination

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Keratitis --- Corneal Stroma --- Cornea --- Aldehyde Dehydrogenase --- Antigen-Antibody Complex --- immunology --- immunology --- immunology --- chemistry --- metabolism

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GAPDH (glyceraldehyde 3-phosphate dehydrogenase) is more than just a glycolytic enzyme. An unprecedented amount of literature demonstrates that GAPDH has an astounding multiplicity of function. This diversity is not simply due to cell compartmentation (i.e. redistributing glycolytic energy to where it is needed), although this feature is undoubtedly important and discussed in the book. GAPDH integrates glycolysis with other cellular processes. This concept of integration cannot be understated. But, there is more. GAPDH actively participates in numerous non-glycolytic cellular events that fall into very broad categories including the cell infrastructure and the transmission of genetic information. Some of GAPDH’s biological properties are completely non-intuitive given the current undergraduate textbook understanding of this glycolytic enzyme. For example, GAPDH binds to select phospholipids and catalyzes organelle biogenesis. It has fusogenic properties, enabling it to be actively involved in nuclear envelop reassembly, autophagy and membrane trafficking. Human macrophages exhibit surface-localized GAPDH with receptor function. As scientists, we are trained to consider GAPDH as a soluble cytosolic dehydrogenase enzyme. The literature observations - as described in this book - tell us something quite different. Besides oxidoreductase activity, GAPDH exhibits peroxidase, uracil DNA glycosylase, nitrosylase, mono-ADP-ribosylase, esterase and phosphotransferase activity. GAPDH binds membrane transport proteins, G-proteins, poly-nucleotides, adenines, specific lipids, select carbohydrates, cytoskeletal proteins, nuclear import and export proteins, diverse ATPases, molecular chaperones and other molecules.

Food Hypersensitivity -- immunology. --- Aldehyde dehydrogenase --- Glycolysis --- Carbohydrate Metabolism --- Gene Expression Regulation --- Phenomena and Processes --- Aldehyde Oxidoreductases --- Anatomy --- Cell Physiological Processes --- Oxidoreductases Acting on Aldehyde or Oxo Group Donors --- Genetic Processes --- Biochemical Processes --- Oxidoreductases --- Biochemical Phenomena --- Genetic Phenomena --- Enzymes --- Chemical Phenomena --- Enzymes and Coenzymes --- Chemicals and Drugs --- Glyceraldehyde-3-Phosphate Dehydrogenases --- Gene Expression Regulation, Enzymologic --- Endocytosis --- Cells --- Cell Physiological Phenomena --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Enzymology. --- Glycolysis. --- Synthesis. --- Glucolysis --- Enzyme synthesis --- Medicine. --- Chemistry. --- Biochemistry. --- Biomedicine. --- Biomedicine general. --- Biochemistry, general. --- Chemistry/Food Science, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Physical sciences --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Composition --- Blood --- Sugar in the body --- Biochemistry --- Examination --- Health Workforce --- Biomedicine, general.

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Overall, the 19 contributions in this Special Issue “Plant Responses and Tolerance to Salt Stress: Physiological and Molecular Interventions” discuss the various aspects of salt stress responses in plants. It also discusses various mechanisms and approaches to conferring salt tolerance on plants. These types of research studies provide further directions in the development of crop plants for the saline environment in the era of climate change.

Research & information: general --- Biology, life sciences --- CPA gene family --- RsNHX1 --- over-expression --- virus-induced gene silence --- salt resistance --- radish --- 14-3-3 gene family --- Triticum aestivum L. --- bioinformatics analysis --- salt tolerance --- protein-protein interactions --- Populus simonii × P. nigra --- PsnNAC036 --- transcription factor --- salt stress --- HT tolerance --- ion transport --- osmotic homeostasis --- hormone mediation --- cell wall regulation --- salt adaptation --- proteomics --- microtubules --- tubulin --- phenolic metabolites --- lemon balm --- chlorophyll fluorescence --- medicinal plants --- secondary metabolites --- abiotic elicitors --- salinity --- betaine aldehyde dehydrogenase 1 (BADH1) --- domestication --- cultivated rice --- wild rice --- Hordeum vulgare L. --- RNA-seq analysis --- differentially expressed genes --- tolerance --- candidate genes --- C3–CAM intermediate --- common ice plant --- Mesembryanthemum crystallinum --- osmotic stress --- abiotic stress --- antioxidant defense --- climate change --- hydrogen peroxide --- lipid peroxidation --- oxidative stress --- phytohormones --- stress signaling --- mulberry --- TMT proteomics --- phenylpropanoid metabolism --- apoplast --- functional screening --- Hordeum vulgare --- seedling --- halophyte species --- NADPH oxidases --- NOX --- respiratory burst oxidase homolog RBOH gene expression --- saline adaptations --- C2H2 zinc finger protein --- heterologous expression --- Millettia pinnata --- thaumatin-like proteins (TLPs) --- bolTLP1 --- broccoli --- drought stress --- antioxidants --- carbohydrates --- carotenoids --- xanthophyll cycle --- osmoprotectants --- ROS-scavengers --- α-/γ-tocopherols --- quantitative trait locus (QTL) --- association analysis --- marker-assisted selection (MAS) --- rice (Oryza sativa L.) --- hydroxyindole-O-methyltransferase gene --- melatonin --- ROS --- ABA --- ion homeostasis --- amino acids --- Malus domestica --- calcium --- calcineurin B-like proteins --- Na+ accumulation --- n/a --- C3-CAM intermediate