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Middle East respiratory syndrome coronavirus (MERS-CoV) is an emerging zoonotic coronavirus. First identified in 2012, MERS-CoV has caused over 2460 infections and a fatality rate of about 35% in humans. Similar to severe acute respiratory syndrome coronavirus (SARS-CoV), MERS-CoV likely originated from bats; however, different from SARS-CoV, which potentially utilized palm civets as its intermediate hosts, MERS-CoV likely transmits to humans through dromedary camels. Animal models, such as humanized mice and nonhuman primates, have been developed for studying MERS-CoV infection. Currently, there are no vaccines and therapeutics approved for the prevention and treatment of MERS-CoV infection, although a number of them have been developed preclinically or tested clinically. This book covers one editorial and 16 articles (including seven review articles and nine original research papers) written by researchers working in the field of MERS-CoV. It describes the following three main aspects: (1) MERS-CoV epidemiology, transmission, and pathogenesis; (2) current progress on MERS-CoV animal models, vaccines, and therapeutics; and (3) challenges and future prospects for MERS-CoV research. Overall, this book will help researchers in the MERS-CoV field to further advance their work on the virus. It also has important implications for other coronaviruses as well as viruses outside the coronavirus family with pandemic potentials.

cell–cell fusion --- hDPP4 --- n/a --- therapeutics --- animal models --- HCoV-229E --- Drivers --- camels --- rabbits --- SARS-CoV --- MERS-CoV --- MVA vaccine --- transmission --- RBD --- MERS-CoV nucleocapsid protein --- complement --- animal model --- pseudotyped virus --- combination --- MERS-coronavirus --- peptide --- mouse model --- spike protein --- receptor-binding domain --- prevention and treatment --- coronaviruses --- coronavirus spike glycoprotein --- therapeutic antibodies --- vaccine platforms --- mutation --- severe acute respiratory syndrome coronavirus --- pathogenesis --- fusion inhibitor --- Coronavirus --- murine CD8+ T cell epitope --- lipidomics --- authentic virus --- correlates of immunity --- vaccines --- neutralizing monoclonal antibodies --- Middle East respiratory syndrome coronavirus --- small-molecule inhibitor --- Middle East Respiratory Syndrome Virus --- DPP4 --- pyroptosis --- cross-neutralization --- inflammation --- Qatar --- spike proteins --- One Health --- HKU4 --- nanobodies --- mechanism of action --- neutralizing antibody --- host factors --- UHPLC–MS

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Pharmacology. Therapy --- Adrenergic mechanisms --- Adrenergic receptors --- Radioligand assay --- Receptors, Adrenergic --- Binding sites --- Adrenaline --- Radioligand Assay --- BINDING SITES --- RECEPTORS, ADRENERGIC --- Receptors --- Binding Sites. --- Radioligand Assay. --- Receptors, Adrenergic. --- -Adrenergic mechanisms --- #Lilly --- Binding assay, Radioligand --- Competitive protein binding assay --- Ligand binding assay (Biochemistry) --- Protein binding assay --- Radioreceptor assay --- Receptor binding assay --- Tissue receptor assay --- Analytical biochemistry --- Ligand binding (Biochemistry) --- Protein binding --- Sympathetic nervous system --- Adrenalin --- Epinephrine --- Bronchodilator agents --- Catecholamines --- Neurotransmitters --- Sympathomimetic agents --- Adrenergic Receptor --- Epinephrine Receptors --- Norepinephrine Receptors --- Adrenergic Receptors --- Adrenoceptors --- Receptors, Epinephrine --- Receptors, Norepinephrine --- Receptor, Adrenergic --- Norepinephrine --- Sympathomimetics --- Racepinephrine --- Protein-Binding Radioassay --- Radioreceptor Assay --- Assay, Radioligand --- Assay, Radioreceptor --- Assays, Radioligand --- Assays, Radioreceptor --- Protein Binding Radioassay --- Protein-Binding Radioassays --- Radioassay, Protein-Binding --- Radioassays, Protein-Binding --- Radioligand Assays --- Radioreceptor Assays --- Ligands --- Protein Binding --- Binding Site --- Combining Site --- Combining Sites --- Site, Binding --- Site, Combining --- Sites, Binding --- Sites, Combining --- Protein Interaction Mapping --- Receptors. --- Binding Sites --- Adrenoreceptors --- Adrenoceptor --- Norepinephrine Receptor --- Receptor, Norepinephrine --- Adrenaline - Receptors

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Proteins represent one of the most abundant classes of biological macromolecules and play crucial roles in a vast array of physiological and pathological processes. The knowledge of the 3D structure of a protein, as well as the possible conformational transitions occurring upon interaction with diverse ligands, are essential to fully comprehend its biological function.In addition to globular, well-folded proteins, over the past few years, intrinsically disordered proteins (IDPs) have received a lot of attention. IDPs are usually aggregation-prone and may form toxic amyloid fibers and oligomers associated with several human pathologies. Peptides are smaller in size than proteins but similarly represent key elements of cells. A few peptides are able to work as tumor markers and find applications in the diagnostic and therapeutic fields. The conformational analysis of bioactive peptides is important to design novel potential drugs acting as selective modulators of specific receptors or enzymes. Nevertheless, synthetic peptides reproducing different protein fragments have frequently been implemented as model systems in folding studies relying on structural investigations in water and/or other environments.This book contains contributions (seven original research articles and five reviews published in the journal Molecules) on the above-described topics and, in detail, it includes structural studies on globular folded proteins, IDPs and bioactive peptides. These works were conducted usingdifferent experimental methods.

mass spectrometric epitope mapping --- gas phase immune complex dissociation --- apparent gas phase dissociation constants --- apparent gas phase activation energies --- ITEM-TWO --- native mass spectrometry --- TRIOBP --- cancer --- deafness --- hearing loss --- mental illness --- schizophrenia --- actin --- cytoskeleton --- disordered structure --- protein aggregation --- solid-state NMR --- ELDOR-detected NMR --- ATP hydrolysis --- ATP analogues --- DnaB helicase --- ABC transporter --- biopesticides --- antifungal activity --- insecticidal activity --- mechanism of action --- transgenic crops --- protein folding --- NMR --- High Hydrostatic Pressure --- ACE2 --- viral spike receptor-binding domain --- SARS-CoV-2 --- transmission --- bioinformatics --- IDP 1 --- binding 2 --- molecular dynamics 3 --- MELD×MD 4 --- advanced sampling 5 --- p53 6 --- MDM2 7 --- NAD(P)H-dependent oxidoreductase --- zinc-containing alcohol dehydrogenase --- cofactor binding and release --- interdomain cleft dynamics --- molecular dynamics simulations --- denatured state ensemble --- protein coil library --- peptides --- intrinsically disordered proteins --- ion-pairing interaction --- side-chain length --- charged amino acids --- β-hairpin --- peptide --- Friedman’s test --- backbone atom coordinate variances and uncertainties --- superimposition --- nanobody --- protein structure --- immunoglobulin domain --- n/a --- Friedman's test

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Few neurotransmitter systems have fascinated as much as the opioid system (i.e., opioid ligands and their receptors). Over the years, scientific studies of the endogenous opioid system have uncovered a complex and subtle system that exhibits impressive diversity, based on its critical role in modulating a large number of sensory, motivational, emotional and cognitive functions. Additionally, its important therapeutic value for the treatment of many human disorders, including pain, affective and addictive disorders, and gastrointestinal motility disorders, has been of persistent interest. This book specifically covers a broad area of the opioid research, offering up-to-date and new perspectives about opioid drug discovery. The diversity among the discussed topics ranging from medicinal chemistry to opioid pharmacology, from basic science to translational research, is a testimony to the complexity of the opioid system that results from the expression, regulation and functional role of opioid ligands and their receptors. This book will serve as a useful reference to scientists while also stimulating continuous research in the chemistry and pharmacology of the opioid system, with the prospective for finding improved therapies of human diseases where the opioid system plays a central role.

thiazole --- piperazine --- tail-clip --- hot-plate --- acetic acid-induced writhing test --- opioid --- prodynorphin --- epigenetics --- transcription --- human brain --- morphine dosing --- behavior --- locomotor activity --- tolerance --- µ-opioid receptor --- DAMGO --- SR-17018 --- buprenorphine --- nalbuphine --- kappa opioid receptor agonist --- pruritis --- scratching --- mice --- TAT-HIV --- cholestasis --- chloroquine --- deoxycholic acid --- analgesic --- δ opioid receptor --- G-protein-biased agonist --- opioid peptide --- rubiscolins --- µ-opioid analgesics --- angiotensin receptors --- chronic pain --- neuropathic pain --- delta opioid receptor --- inverse agonist --- irreversible antagonist --- non-competitive antagonist --- molecular pharmacology --- free fatty acid receptors --- lipids --- opioid receptor --- colitis --- chemotype --- high-throughput screen --- allosteric modulation --- beta-arrestin --- molecular dynamics --- opioid receptors --- β-amino acids --- peptide synthesis --- receptor binding studies --- functional assay --- nociceptin/orphanin FQ receptor --- NOP receptor --- ligands --- nociceptin --- N/OFQ --- analgesia --- GPCR --- HS-731 --- peripheral opioid agonist --- binding --- selectivity --- molecular docking --- molecular dynamics simulations --- n/a --- fluorescence cross-correlation spectroscopy (FCCS) --- G protein-coupled receptor (GPCR) --- serotonin

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Energy Metabolism. --- Radiochemistry. --- Receptors, Cell Surface. --- Tomography, Emission-Computed. --- Biochemistry --- -Energy metabolism --- -Radioligand assay --- -Tomography, Emission --- -Computerized emission tomography --- Emission tomography --- PET (Tomography) --- PET-CT (Tomography) --- Positron emission tomography --- Positron emission transaxial tomography --- Radionuclide tomography --- Scintigraphy, Tomographic --- Tomography, Radionuclide --- Diagnosis --- Diagnostic imaging --- Positrons --- Radioisotope scanning --- Binding assay, Radioligand --- Competitive protein binding assay --- Ligand binding assay (Biochemistry) --- Protein binding assay --- Radioreceptor assay --- Receptor binding assay --- Tissue receptor assay --- Analytical biochemistry --- Ligand binding (Biochemistry) --- Protein binding --- Bioenergetics --- Metabolism --- Microbial respiration --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Cell Surface Hormone Receptors --- Endogenous Substances Receptors --- Cell Surface Receptors --- Hormone Receptors, Cell Surface --- Receptors, Endogenous Substances --- Binding Sites --- Hormones --- Ligands --- Receptor Cross-Talk --- Radiochemistries --- Energy Expenditure --- Bioenergetic --- Energy Expenditures --- Energy Metabolisms --- Expenditure, Energy --- Expenditures, Energy --- Metabolism, Energy --- Metabolisms, Energy --- Technique --- -Congresses --- Measurement --- Congresses --- Data processing --- Emission --- Composition --- Energy metabolism --- Radioligand assay --- Tomography, Emission --- Energy Metabolism --- Radiochemistry --- Receptors, Cell Surface --- Tomography, Emission-Computed --- Computed Tomographic Scintigraphy --- Emission-Computed Tomography --- Radionuclide Computer-Assisted Tomography --- Radionuclide Computerized Tomography --- Radionuclide-Computed Tomography --- Radionuclide-Emission Computed Tomography --- Tomography, Computerized Emission --- CAT Scan, Radionuclide --- CT Scan, Radionuclide --- Computerized Emission Tomography --- Radionuclide Tomography, Computed --- Scintigraphy, Computed Tomographic --- Tomography, Radionuclide-Computed --- CAT Scans, Radionuclide --- CT Scans, Radionuclide --- Computed Radionuclide Tomography --- Computed Tomography, Radionuclide-Emission --- Computer-Assisted Tomographies, Radionuclide --- Computer-Assisted Tomography, Radionuclide --- Computerized Tomography, Radionuclide --- Emission Computed Tomography --- Emission Tomography, Computerized --- Radionuclide CAT Scan --- Radionuclide CAT Scans --- Radionuclide CT Scan --- Radionuclide CT Scans --- Radionuclide Computed Tomography --- Radionuclide Computer Assisted Tomography --- Radionuclide Computer-Assisted Tomographies --- Radionuclide Emission Computed Tomography --- Scan, Radionuclide CAT --- Scan, Radionuclide CT --- Scans, Radionuclide CAT --- Scans, Radionuclide CT --- Tomographic Scintigraphy, Computed --- Tomographies, Radionuclide Computer-Assisted --- Tomography, Computed Radionuclide --- Tomography, Emission Computed --- Tomography, Radionuclide Computed --- Tomography, Radionuclide Computer-Assisted --- Tomography, Radionuclide Computerized --- Tomography, Radionuclide-Emission Computed --- Technique&delete& --- Measurement&delete& --- Positronen-Emissions-Tomografie --- Cell Surface Receptor --- Receptor, Cell Surface --- Surface Receptor, Cell --- Positronen-Emissions-Tomografie.