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Protein tyrosine phosphatases remove phosphates from the phosphotyrosine residues of target proteins and reverse the action of various protein tyrosine kinases. This essential interplay between the opposing actions of protein tyrosine phosphatases and protein tyrosine kinases forms the basis of signaling networks that underlie the cellular workings of human physiology. Initially passed-off as housekeeping genes; these proteins were only acknowledged to maintain a steady background of phosphotyrosine levels in the cell. However, recent progress in studying their role in embryonic development and human disease has established their importance as regulators of signal regulation. Convincing evidence shows the role of mutations in these proteins to cause and/or intensify the severity of various diseases including metabolic and neurological disorders and also cancer. Protein tyrosine phosphatases have slowly, yet convincingly become crucial targets for therapeutic intervention of various human pathophysiologies. This book describes these signaling enzymes using the molecular details of their structure and mechanistic function. Various subtypes of cysteine-based Class I, II, III and the Haloacid dehalogenase related Class IV protein tyrosine phosphatases have been illustrated and explained. The superfamily of proteins is also described vis-a-vis its complimentary protein phosphoserine/phosphoserine phosphatases. Membrane bound receptor forms and the cytosolic non-receptor protein tyrosine phosphatases have been described for their biological function. This book serves as a reference for any reader looking to understand the sequence features, structural elements, molecular mechanism and cellular function of this superfamily of signaling enzymes.

Protein-tyrosine phosphatase. --- Phosphotyrosine phosphatase --- PTPase --- Tyrosine phosphatase --- Tyrosine phosphoprotein phosphatase --- Tyrosyl phosphoprotein phosphatase --- Phosphoprotein phosphatases --- Biochemistry. --- Drug Design. --- Medicinal Chemistry. --- Protein Tyrosine Phosphatase. --- Signalling Proteins.

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Human histology. Human cytology --- Immunology. Immunopathology --- Lymphocyte transformation --- Protein-tyrosine kinase --- Protein-tyrosine-phosphatase --- Receptors, antigen, b-cell --- Receptors, antigen, t-cell --- Receptors, ige

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Tyrosine phosphorylation is a rapid and reversible protein modification catalyzed by the yin and yang activities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs).  A multitude of PTPs have been implicated in human disease, with a growing number of PTPs now known to play major roles in prevalent metabolic diseases including obesity and type 2 diabetes.  Recent studies into PTP function in the context of metabolism highlight the importance of understanding the specific substrates and binding partners of these enzymes, the regulation of PTP activity, and the cell/tissue specificity of PTP functions.  This volume contains chapters which highlight many aspects of PTP function in the context of metabolism.

Biochemistry. --- Endocrinology. --- Life sciences. --- Medicine. --- Protein-tyrosine kinase. --- Protein-tyrosine phosphatase -- Metabolism -- Regulation. --- Protein-tyrosine phosphatase --- Biological Science Disciplines --- Nutritional and Metabolic Diseases --- Metabolic Phenomena --- Protein Kinases --- Phosphoric Monoester Hydrolases --- Natural Science Disciplines --- Phosphotransferases (Alcohol Group Acceptor) --- Esterases --- Phenomena and Processes --- Diseases --- Disciplines and Occupations --- Hydrolases --- Phosphotransferases --- Enzymes --- Transferases --- Enzymes and Coenzymes --- Chemicals and Drugs --- Metabolic Diseases --- Protein-Tyrosine Kinases --- Metabolism --- Protein Tyrosine Phosphatases --- Physiology --- Chemistry --- Physical Sciences & Mathematics --- Biochemistry --- Regulation --- Physiological effect. --- Regulation. --- Control of metabolism --- Metabolic control --- Metabolic regulation --- Regulation of metabolism --- Phosphotyrosine phosphatase --- PTPase --- Tyrosine phosphatase --- Tyrosine phosphoprotein phosphatase --- Tyrosyl phosphoprotein phosphatase --- Proteins. --- Life Sciences. --- Protein Science. --- Biochemistry, general. --- Biomedicine general. --- Biological control systems --- Phosphoprotein phosphatases --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Internal medicine --- Hormones --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Composition --- Proteins . --- Endocrinology . --- Biomedicine, general. --- Health Workforce --- Proteids --- Biomolecules --- Polypeptides --- Proteomics

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The book presents several studies reporting advances on melanoma pathogenesis, diagnosis and therapy. It represents a milestone on the state of the art, updated at 2021, and also presents the current knowledge on the future developments in melanoma field.

Medicine --- melanoma --- invasion --- WNT5A --- MARCKS --- phosphorylation --- MANS peptide --- nanoparticles --- cell therapy --- tumor microenvironment --- sex/gender --- sex-hormones --- immunity --- microRNAs --- immunotherapy --- BRAF-mutant melanoma --- BRAF inhibitor --- mechanism of action --- targeted therapy --- tumour microenvironment --- plasmacytoid dendritic cells --- lactate dehydrogenase --- TLR --- interferon --- CXCL10 --- TPC2 --- HIPPO --- SOCE --- metastasis --- essential oils --- angiogenesis --- apoptosis --- uveal melanoma (UM) --- metastatic uveal melanoma (mUM) --- prognostication --- adjuvant therapy --- metastatic therapy --- metastatic dormancy --- liver-directed-therapies --- targeted-therapy --- combined therapy --- protein tyrosine phosphatase --- PTPs inhibitors --- melanoma immune infiltrate --- BRAF inhibitors --- microenvironment --- resistance --- therapy --- therapeutic resistance --- exosomes --- extracellular vesicles --- diagnosis --- prognosis --- ctDNA --- liquid biopsy --- prediction --- patient stratification --- BRAF --- arthralgia --- rheumatoid arthritis --- carbonic anhydrase --- hedgehog --- cyclopamine --- small molecules --- acetazolamide --- motility --- metalloproteinases --- FAK --- cancer --- mucosal melanoma --- nivolumab --- pembrolizumab --- ipilimumab --- radiotherapy --- cholinergic system --- acetylcholine --- muscarinic receptors --- nicotinic receptors --- melanoma metastasis --- ShcD adaptor protein --- amoeboid motility --- Rac1 --- DOCK4 --- melanoma PDX --- target therapy --- cancer stem cells --- slow cycling phenotype --- drug resistance --- OXPHOS --- lipid metabolism --- cancer associated fibroblast --- melanomagenesis --- biomarkers --- checkpoint inhibitor --- PD-1 --- melanoma markers --- cytokines --- machine learning --- Support Vector Machine --- principal component analysis --- BCL2L10 --- STAT3 --- cytotoxicity --- survival --- ABT-737 --- Bcl-2 family --- ML258 --- HuR --- MITF --- metastases --- siRNA --- melanoma --- invasion --- WNT5A --- MARCKS --- phosphorylation --- MANS peptide --- nanoparticles --- cell therapy --- tumor microenvironment --- sex/gender --- sex-hormones --- immunity --- microRNAs --- immunotherapy --- BRAF-mutant melanoma --- BRAF inhibitor --- mechanism of action --- targeted therapy --- tumour microenvironment --- plasmacytoid dendritic cells --- lactate dehydrogenase --- TLR --- interferon --- CXCL10 --- TPC2 --- HIPPO --- SOCE --- metastasis --- essential oils --- angiogenesis --- apoptosis --- uveal melanoma (UM) --- metastatic uveal melanoma (mUM) --- prognostication --- adjuvant therapy --- metastatic therapy --- metastatic dormancy --- liver-directed-therapies --- targeted-therapy --- combined therapy --- protein tyrosine phosphatase --- PTPs inhibitors --- melanoma immune infiltrate --- BRAF inhibitors --- microenvironment --- resistance --- therapy --- therapeutic resistance --- exosomes --- extracellular vesicles --- diagnosis --- prognosis --- ctDNA --- liquid biopsy --- prediction --- patient stratification --- BRAF --- arthralgia --- rheumatoid arthritis --- carbonic anhydrase --- hedgehog --- cyclopamine --- small molecules --- acetazolamide --- motility --- metalloproteinases --- FAK --- cancer --- mucosal melanoma --- nivolumab --- pembrolizumab --- ipilimumab --- radiotherapy --- cholinergic system --- acetylcholine --- muscarinic receptors --- nicotinic receptors --- melanoma metastasis --- ShcD adaptor protein --- amoeboid motility --- Rac1 --- DOCK4 --- melanoma PDX --- target therapy --- cancer stem cells --- slow cycling phenotype --- drug resistance --- OXPHOS --- lipid metabolism --- cancer associated fibroblast --- melanomagenesis --- biomarkers --- checkpoint inhibitor --- PD-1 --- melanoma markers --- cytokines --- machine learning --- Support Vector Machine --- principal component analysis --- BCL2L10 --- STAT3 --- cytotoxicity --- survival --- ABT-737 --- Bcl-2 family --- ML258 --- HuR --- MITF --- metastases --- siRNA

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Mitogen-activated protein kinases (MAPK) are a large family of enzymes that function as signal transducers to regulate a diverse range of physiological responses. However, signaling via extracellular signal-regulated kinase (ERK), c-Jun amino terminal kinase (JNK), and p38 MAPK also underpin many disease processes. This Special Issue provides new insights into how MAPK signaling contributes to specific pathological processes across a range of conditions, including disorders of lung development, type 2 diabetes, proliferative skin diseases, cardiovascular diseases, and neurological diseases.

Rabdosia inflexa --- inflammation --- gastric ulcer --- cytokines --- MAPK --- NF-κB --- extracellular signal-regulated kinases 1/2 --- hyperoxia --- bronchopulmonary dysplasia --- HPAECs --- angiogenesis --- cell cycle --- SIRT1 --- oxidative stress --- psoriasis --- antimicrobial peptide --- cecropin A --- tight junction protein --- MEK/ERK signaling --- porcine intestinal epithelial cell --- extracellular signal-regulated kinase 5 (ERK5) --- Kv4.2 --- PC12 cells --- infantile myofibromatosis --- receptor tyrosine kinases --- platelet-derived growth factor receptor --- protein kinase inhibitors --- sunitinib --- erlotinib --- FR180204 --- U0126 --- targeted therapy --- apoptosis --- ERK1/2 --- JNKs --- mitochondrial dysfunction --- neurodegeneration --- neuro-inflammation --- p38 MAPKs --- Parkinson’s disease --- mitogen-activated protein kinases (MAPKs) --- MAPK kinetics --- osteoclast differentiation --- bone remodeling --- DAPK --- ERK --- p38 --- JNK --- mitogen-activated protein kinase pathway (MAPK pathway) --- protein tyrosine phosphatase interacting protein 51 (PTPIP51) --- protein-protein interaction (PPI) --- cancer signaling --- SR --- CR --- Compatibility --- T2DM --- metabolic profiling --- MAPK/PI3K/Akt signaling pathway --- reactive oxygen species --- PTPN6 --- SRC --- DOK4 --- MKK4 --- MKK7 --- p53 --- DUSP1 --- SIRT2 --- atherosclerosis --- aortic valve sclerosis --- aortic valve stenosis --- naphthalimide-metal complex conjugates --- N-heterocyclic carbene --- mitochondria --- ROS --- p38 MAPK --- cancer --- FGF-induced signaling --- FRS2 --- phosphorylation --- downregulation --- n/a --- Parkinson's disease