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Adenosine Triphosphatases --- DNA Replication --- metabolism --- drug effects

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In recent years, a number of groundbreaking structural and mechanistic studies deepened our understanding of helicase mechanisms and established new approaches for their analyses. Many fundamental mechanistic questions ranging from the mechanism of force generation, mechanochemical coupling to distinct mechanisms by which the same enzyme translocates on DNA removing obstacles, unwinds DNA and/or remodels nucleoprotein complexes, however, remain to be answered. It is even less understood how the helicase motors are incorporated into a wide range of genome maintenance and repair machines. The field has reached a stage when the studies of molecular mechanisms and basic biology of helicases can and shall be integrated with the studies of development, cancer and longevity. The objective of this book is to provide the first systematic overview of structure, function and regulation of DNA helicases and related molecular motors. By integrating the knowledge obtained through the diverse technical approaches ranging from single-molecule biophysics to cellular and molecular biological studies the editors aim to provide a unified view on how helicases function in the cell, are regulated in response to different cellular stresses and are integrated into large macromolecular assemblies to form a complex and adaptive living system.

Bacterial genetics. --- DNA helicases. --- DNA polymerases. --- Isomerases --- Adenosine Triphosphatases --- Multiprotein Complexes --- Acid Anhydride Hydrolases --- Enzymes --- Macromolecular Substances --- Enzymes and Coenzymes --- Hydrolases --- Chemicals and Drugs --- Molecular Motor Proteins --- DNA Helicases --- Medicine --- Human Anatomy & Physiology --- Biology --- Health & Biological Sciences --- Animal Biochemistry --- Genetics --- Pathology --- DNA-protein interactions. --- DNA-protein binding --- Interactions, DNA-protein --- Protein-DNA interactions --- Helicases, DNA --- Medicine. --- Human genetics. --- Biochemistry. --- Cell biology. --- Biomedicine. --- Human Genetics. --- Biochemistry, general. --- Cell Biology. --- Biomedicine general. --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Heredity, Human --- Human biology --- Physical anthropology --- Clinical sciences --- Medical profession --- Life sciences --- Physicians --- Composition --- DNA-ligand interactions --- Protein binding --- Cytology. --- Health Workforce --- Biomedicine, general.

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Vascular smooth muscle (VSM) constitutes most of the tunica media in blood vessels and plays an important role in the control of vascular tone. Ca2+ is a major regulator of VSM contraction and is strictly regulated by an intricate system of Ca2+ mobilization and Ca2+ homeostatic mechanisms. The interaction of a physiological agonist with its plasma membrane receptor stimulates the hydrolysis of membrane phospholipids and increases the generation of inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 stimulates Ca2+ release from the intracellular stores in the sarcoplasmic reticulum. Agonists also stimulate Ca2+ influx from the extracellular space via voltage-gated, receptor-operated, and store-operated channels. Ca2+ homeostatic mechanisms tend to decrease the intracellular free Ca2+ concentration ([Ca2+]i) by activating Ca2+ extrusion via the plasmalemmal Ca2+ pump and the Na+/Ca2+ exchanger and the uptake of excess Ca2+ by the sarcoplasmic reticulum and possibly the mitochondria. A threshold increase in [Ca2+]i activates Ca2+-dependent myosin light chain (MLC) phosphorylation, stimulates actin-myosin interaction, and initiates VSM contraction. The agonist-induced maintained increase in DAG also activates specific protein kinase C (PKC) isoforms, which in turn cause phosphorylation of cytoplasmic substrates that increase the contractile myofilaments force sensitivity to Ca2+ and thereby enhance VSM contraction. Agonists could also activate Rho kinase (ROCK), leading to inhibition of MLC phosphatase and further enhancement of the myofilaments force sensitivity to Ca2+. The combined increases in [Ca2+]i, PKC and ROCK activity cause significant vasoconstriction and could also stimulate VSM hypertrophy and hyperplasia. The protracted and progressive activation of these processes could lead to pathological vascular remodeling and vascular disease.

Muscle contraction. --- Vascular diseases. --- Vascular smooth muscle. --- Ion Channels --- Muscle Proteins --- Microfilament Proteins --- Hemodynamics --- Muscle, Smooth --- Molecular Motor Proteins --- Cardiovascular Diseases --- Blood Vessels --- Diseases --- Muscles --- Contractile Proteins --- Cardiovascular Physiological Processes --- Cardiovascular System --- Adenosine Triphosphatases --- Membrane Glycoproteins --- Biopolymers --- Membrane Transport Proteins --- Cytoskeletal Proteins --- Polymers --- Tissues --- Carrier Proteins --- Acid Anhydride Hydrolases --- Proteins --- Cardiovascular Physiological Phenomena --- Membrane Proteins --- Anatomy --- Musculoskeletal System --- Amino Acids, Peptides, and Proteins --- Circulatory and Respiratory Physiological Phenomena --- Macromolecular Substances --- Hydrolases --- Chemicals and Drugs --- Phenomena and Processes --- Enzymes --- Enzymes and Coenzymes --- Myosins --- Muscle, Smooth, Vascular --- Vasoconstriction --- Calcium Channels --- Vascular Diseases --- Human Anatomy & Physiology --- Health & Biological Sciences --- Physiology --- Vascular resistance. --- Blood pressure. --- Vascular smooth muscle --- Physiology. --- physiology. --- Signal transduction --- Calcium --- Blood pressure --- AngII, angiotensin II --- ATP, adenosine triphosphate --- CPI-17, PKC-potentiated phosphatase inhibitor protein-17 kDa --- CAM, calmodulin --- DAG, diacylglycerol --- ET-1, endothelin --- IP3, inositol 1,4,5-trisphosphate --- MAPK, mitogen-activated protein kinase --- MARCKs, myristoylated alanine-rich C-kinase substrate --- MEK, MAPK kinase --- MLC, myosin light chain --- NCX, Na+-Ca2+ exchanger --- PDBu, phorbol 12,13-dibutyrate; PIP2, phosphatidylinositol 4,5-bisphosphate --- PKC, protein kinase C --- PMA, phorbol myristate acetate --- RACKs, receptors for activated C-kinase --- ROCK, Rho-kinase --- VSMC, vascular smooth muscle cell