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Contractility describes the relative ability of the heart to eject a stroke volume (SV) at a given prevailing afterload (arterial pressure) and preload (end-diastolic volume; EDV). Various measures of contractility are related to the fraction as the SV/EDV or the ejection fraction, and the dynamics of ejection as determined from maximum pressure rise in the ventricles or arteries or from aortic flow velocities determined by echocardiography. At the cellular level, the ultimate determinant of contractility is the relative tension generation and shortening capability of the molecular motors (myosin cross-bridges) of the sarcomeres as determined by the rates and extent of Ca activation, the turnover kinetics of the cross-bridges, and the relative Ca responsiveness of the sarcomeres. Engagement of the regulatory signaling cascades controlling contractility occurs with occupancy and signal transduction by receptors for neurohumors of the autonomic nervous system as well as growth and stress signaling pathways. Contractility is also determined by the prevailing conditions of pH, temperature, and redox state. Short-term control of contractility is fully expressed during exercise. In long-term responses to stresses on the heart, contractility is modified by cellular remodeling and altered signaling that may compensate for a time but which ultimately may fail, leading to disorders.

Heart --- Contraction --- Regulation. --- Myocardial Contraction. --- Afterload --- Preload --- Length-dependent activation --- Ca regulation --- Sarcomere --- Protein phosphorylation

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Protein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein phosphorylation is implicated in the onset and progression of human diseases such as cancer and neurodegenerative disorders. In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritizing phosphosites and assessing their functional relevance. Some computational approaches also address the inference of specificity determinants of protein kinases/phosphatases and the identification of phosphoresidue recognition domains. In this context, several challenging issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. Furthermore, the determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signaling. The articles included in this Research Topic illustrate the very diverse aspects of phosphorylation, ranging from structural changes induced by phosphorylation to the peculiarities of phosphosite evolution. Some also provide a glimpse into the huge complexity of phosphorylation networks and pathways in health and disease, and underscore that a deeper knowledge of such processes is essential to identify disease biomarkers, on one hand, and design more effective therapeutic strategies, on the other.

protein structure --- kinases --- Phosphatases --- bioinformatics --- evolution --- Protein phosphorylation --- network biology --- Systems Biology --- Human Disease

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Stomata, the tiny pores on leaf surface, are the gateways for CO2 uptake during photosynthesis as well as water loss in transpiration. Further, plants use stomatal closure as a defensive response, often triggered by elicitors, to prevent the entry of pathogens. The guard cells are popular model systems to study the signalling mechanism in plant cells. The messengers that mediate closure upon perception of elicitors or microbe associated molecular patterns (MAMPs) are quite similar to those during ABA effects. These components include reactive oxygen species (ROS), nitric oxide (NO), cytosolic pH and intracellular Ca2+. The main components are ROS, NO and cytosolic free Ca2+. The list extends to others, such as G-proteins, protein phosphatases, protein kinases, phospholipids and ion channels. The sequence of these signalling components and their interaction during stomatal signalling are complex and quite interesting. The present e-Book provides a set of authoritative articles from ‘Special Research Topic’ on selected areas of stomatal guard cells. In the first set of two articles, an overview of ABA and MAMPs as signals is presented. The next set of 4 articles, emphasize the role of ROS, NO, Ca2+ as well as pH, as secondary messengers. The next group of 3 articles highlight the recent advances on post-translational modification of guard cell proteins, with emphasis on 14-3-3 proteins and MAPK cascades. The last article described the method to isolate epidermis of grass species and monitor stomatal responses to different signals. Our e-Book is a valuable and excellent source of information for all those interested in guard cell function as well as signal transduction in plant cells.

ABA --- Methyl Jasmonate --- Reactive Oxygen Species --- innate immunity --- Proteomics --- Epidermis --- Nitric Oxide --- Protein phosphorylation --- secondary messengers --- elicitors

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Due to their lightweight and high specific strength, Mg-based alloys are considered as substitutes to their heavier counterparts in applications in which corrosion is non-relevant and weight saving is of importance. Furthermore, due to the biocompatibility of Mg, some alloys with controlled corrosion rates are used as degradable implant materials in the medical sector. The typical processing route of Mg parts incorporates a casting step and, subsequently, a thermo–mechanical treatment. In order to achieve the desired macroscopic properties and thus fulfill the service requirements, thorough knowledge of the relationship between the microstructure, the processing steps, and the resulting property profile is necessary. This Special Issue covers in situ and ex situ experimental and computational investigations of the behavior under thermo–mechanical load of Mg-based alloys utilizing modern characterization and simulation techniques. The papers cover investigations on the effect of rare earth additions on the mechanical properties of different Mg alloys, including the effect of long-period stacking-ordered (LPSO) structures, and the experimental and computational investigation of the effect of different processing routes

Arabidopsis --- abiotic stress response --- photosynthesis --- phosphoglycolate phosphatase --- photorespiration --- 2-phosphoglycolate --- Arabidopsis thaliana --- glycolate oxidase --- protein phosphorylation --- Zea mays --- Portulaca grandiflora --- C4 photosynthesis --- Crassulacean acid metabolism (CAM), evolution --- development --- PEP carboxylase --- Portulacaceae --- glycine decarboxylase --- metabolite signaling/acclimation --- TCA cycle --- Calvin–Benson cycle --- photoperiodic changes --- redox-regulation --- environmental adaptation --- Glycolate oxidase --- evolution --- Archaeplastida --- Cyanobacteria --- MCF --- oxidative phosphorylation --- mitochondrial carriers --- transporters --- energy balancing --- cyclic electron flux --- malate valve --- C3 cycle --- acclimation --- chlorophyll a fluorescence --- fluctuating light --- natural variation --- pyruvate kinase --- glycolysis --- respiratory metabolism --- n/a --- Calvin-Benson cycle

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Cellular Responses to Stress brings together a group of scientists who work on different but interrelated aspects of cellular stress responses. The book provides state-of-the-art information on the wide spectrum of ways in which cells can respond to different forms of stress induced by chemicals, oxidants, and DNA-damaging agents. Mechanisms are described that involve altered uptake and efflux of chemical agents, intracellular detoxification, and DNA damage responses. Many of these changes trigger a cascade of reactions mediated by stress-activated signaling pathways, which have the capacity to determine whether a cell will survive or die. The spectrum of topics covered in this book aims to provide a broad overview of our current knowledge of the different forms of adaptive response systems.It is hoped that this text will stimulate further research to establish the relative cellular role of specific response pathways and will enable us to gain a deeper understanding of the mechanisms that allow cells to live or die. This book will be valued by university researchers at all levels, industrial scientists in the pharmaceutical and biotechnology industries, and clinical researchers.Originally published in 1999.The Princeton Legacy Library uses the latest print-on-demand technology to again make available previously out-of-print books from the distinguished backlist of Princeton University Press. These editions preserve the original texts of these important books while presenting them in durable paperback and hardcover editions. The goal of the Princeton Legacy Library is to vastly increase access to the rich scholarly heritage found in the thousands of books published by Princeton University Press since its founding in 1905.

Stress (Physiology) --- Cell metabolism --- Cellular control mechanisms --- Cells --- Metabolism --- Regulation --- AMPK. --- ASK1. --- Actin. --- Activation. --- Angiogenesis. --- Antibody. --- Antigen. --- Apoptosis. --- Autoimmunity. --- Autophosphorylation. --- C-Fos. --- C-Jun N-terminal kinases. --- C-terminus. --- Cell Cycle Arrest. --- Cell Line, Transformed. --- Cell cycle. --- Cell membrane. --- Cell migration. --- Cell surface receptor. --- Cellular differentiation. --- Cellular stress response. --- Conformational change. --- Cytochrome P450. --- Cytokine receptor. --- Cytokine. --- Cytotoxicity. --- DNA-PKcs. --- Drug metabolism. --- Ectopic expression. --- Effector (biology). --- Endonuclease. --- Enzyme. --- Epidermal growth factor receptor. --- Epidermal growth factor. --- Extracellular signal–regulated kinases. --- Fibroblast growth factor. --- Gene expression. --- Gene therapy. --- Gene. --- Germinal center. --- Glutathione S-transferase. --- HMG-CoA reductase. --- Heat shock. --- Histidine kinase. --- Hormone-sensitive lipase. --- Hsp27. --- Immortalised cell line. --- Immunodeficiency. --- Immunoglobulins. --- Immunoprecipitation. --- In vitro. --- Inducer. --- Inflammation. --- Jurkat cells. --- Kinase. --- Lymphotoxin. --- Macrophage colony-stimulating factor. --- Mechanism of action. --- Mechanistic target of rapamycin. --- Metabolism. --- Mitogen-activated protein kinase kinase. --- Mitogen-activated protein kinase. --- Mitogen. --- Mitosis. --- Model organism. --- Neuropeptide. --- Neurotoxin. --- Osmotic shock. --- Oxidative phosphorylation. --- Oxidative stress. --- P38 mitogen-activated protein kinases. --- Pathogenesis. --- Peptide. --- Peroxidase. --- Phosphatase. --- Phosphoinositide 3-kinase. --- Phosphorylation cascade. --- Phosphorylation. --- Post-translational modification. --- Protease. --- Protein kinase. --- Protein phosphorylation. --- Protein synthesis inhibitor. --- Protein. --- Proteolysis. --- RNA interference. --- Receptor (biochemistry). --- Receptor tyrosine kinase. --- Repressor. --- Response element. --- Signal transduction. --- Ternary Complex Factors. --- Thrombin. --- Transcription factor. --- Transcriptional regulation. --- Transfection. --- Transposable element. --- Tumor necrosis factor superfamily. --- Turgor pressure. --- Vascular endothelial growth factor.