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2003, Methods in enzymology, ISBN 9780121822699, Volume 366., l, 453 p., [4] p. of plates
Book
1998, Methods in molecular biology, ISBN 0896034682, Volume 93., xiii, 316
In Protein Phosphatase Protocols, John Ludlow assembles a collection of cutting-edge techniques for investigating the structure and function of protein... 
Laboratory manuals | Phosphoprotein phosphatases | Microbiology | Biochemistry, general | Biochemistry | Life Sciences
Book
BioMetals, ISSN 0966-0844, 12/2011, Volume 24, Issue 6, pp. 993 - 1004
A series of copper complexes with multi-benzimidazole derivatives, including mono- and di-nuclear, were synthesized and characterized by Fourier transform IR... 
Life Sciences | Biochemistry, general | Protein tyrosine phosphatases | Microbiology | Fluorescence | Plant Physiology | Copper complex | Inhibition | Pharmacology/Toxicology | Medicine/Public Health, general | Cell Biology | CANCER-CELLS | HOMEOSTASIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CATALYTIC DOMAIN | DISOLVATE | APOPTOSIS INDUCERS | STRATEGIES | LIGANDS | PURIFICATION | PROTEASOME INHIBITORS | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism | Humans | Protein Tyrosine Phosphatases - metabolism | Structure-Activity Relationship | Benzimidazoles - chemistry | Enzyme Inhibitors - chemical synthesis | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - chemistry | Protein Tyrosine Phosphatases - antagonists & inhibitors | Protein Tyrosine Phosphatases - chemistry | Protein Tyrosine Phosphatases - genetics | Protein Tyrosine Phosphatases, Non-Receptor - chemistry | Copper - chemistry | Enzyme Inhibitors - chemistry | Protein Tyrosine Phosphatases, Non-Receptor - genetics | Copper - metabolism | Molecular Structure | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - chemistry | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - chemistry | Enzyme Inhibitors - metabolism | Benzimidazoles - chemical synthesis | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - chemistry | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism | Spectrum Analysis - methods | Benzimidazoles - metabolism | Protein Tyrosine Phosphatases, Non-Receptor - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics | Protein Tyrosine Phosphatases, Non-Receptor - antagonists & inhibitors | Tyrosine | Phosphatases | Ionization | Analysis | Phenols | T cells | Mass spectrometry | Proteins | Enzymes | Cellular biology | Copper | Index Medicus
Journal Article
Pancreatology, ISSN 1424-3903, 06/2018, Volume 18, Issue 4, p. S64
Journal Article
Fish and Shellfish Immunology, ISSN 1050-4648, 09/2017, Volume 68, pp. 368 - 376
Dual-specificity MAP kinase (MAPK) phosphatases (DUSPs) are well-established negative modulators in regulating MAPK signaling in mammalian cells and tissues.... 
Immune challenge | Expression induction | Mitogen-activated protein kinase phosphatases | Paralichthys olivaceus | Dual-specificity phosphatase | KINASE PHOSPHATASE | MACROPHAGES | Mitogen-activated protein kinase | IMMUNOLOGY | CELL-LINES | IDENTIFICATION | REGULATOR | SHOCK | FISHERIES | MKP-1 | MARINE & FRESHWATER BIOLOGY | LIPOPOLYSACCHARIDE | VETERINARY SCIENCES | INFECTION | EXPRESSION | phosphatases | Immunity, Innate - genetics | Flatfishes - genetics | Phylogeny | Fish Proteins - genetics | Dual Specificity Phosphatase 2 - immunology | Dual-Specificity Phosphatases - genetics | Cell Culture Techniques | Dual Specificity Phosphatase 2 - genetics | Amino Acid Sequence | Dual Specificity Phosphatase 1 - genetics | Poly I-C - pharmacology | Fish Proteins - chemistry | Fish Proteins - immunology | Dual-Specificity Phosphatases - metabolism | Gene Expression Regulation - immunology | Flatfishes - immunology | Dual-Specificity Phosphatases - immunology | Dual Specificity Phosphatase 1 - immunology | Sequence Alignment - veterinary | Dual-Specificity Phosphatases - chemistry | Gene Expression Regulation - drug effects | Animals | Dual Specificity Phosphatase 1 - chemistry | Lipopolysaccharides - pharmacology | Dual Specificity Phosphatase 1 - metabolism | Dual Specificity Phosphatase 2 - metabolism | Dual Specificity Phosphatase 2 - chemistry | Immune response | Phosphatases | RNA | Fishes | Genes | Genetic research | Comparative analysis | Gene expression | Proteins | Skin | Protein kinases | Cells | Index Medicus
Journal Article
1969, Annals (New York Academy of Sciences), Volume 166 : art.2., c450
Book
PLoS ONE, ISSN 1932-6203, 08/2015, Volume 10, Issue 8, pp. e0134984 - e0134984
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine... 
CELL LUNG-CANCER | CDC25 PHOSPHATASE | ANGSTROM RESOLUTION | ACTIVATION | VIRUS | CRYSTAL-STRUCTURE | KINASE PHOSPHATASE-1 | MULTIDISCIPLINARY SCIENCES | PROTEIN-TYROSINE PHOSPHATASES | INHIBITORS | CATALYTIC MECHANISM | Dual Specificity Phosphatase 1 - genetics | Signal Transduction | Dual-Specificity Phosphatases - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Substrate Specificity | Dual Specificity Phosphatase 3 - genetics | cdc25 Phosphatases - genetics | Phylogeny | Recombinant Proteins | Mitogen-Activated Protein Kinase Phosphatases - genetics | Amino Acid Motifs | Phosphotyrosine - metabolism | Phosphoprotein Phosphatases - genetics | Dual-Specificity Phosphatases - genetics | Protein Array Analysis | Dual Specificity Phosphatase 1 - metabolism | cdc25 Phosphatases - metabolism | Dual Specificity Phosphatase 3 - metabolism | Mitogen-Activated Protein Kinase Phosphatases - metabolism | Physiological aspects | Phosphorylation | Genetic aspects | Phosphatases | Research | Cluster analysis | Residues | Peptides | Laboratories | Phosphotyrosine | Biochemistry | Catalytic activity | Dephosphorylation | Structure-activity relationships | Kinases | Phosphatase | Crystallography | Subgroups | Proteins | Signal transduction | Cell growth | Pathways | Substrate specificity | Armed forces | Catalysis | Localization | Pharmaceutical sciences | Tyrosine | Smallpox | Medical research | Enzymes | Cell division | Clustering | Substrates | Signaling | Chemistry | Infectious diseases | Alzheimers disease | Recognition | Cancer | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 4, pp. e10290 - e10290
Stat3 is initially dephosphorylated in murine keratinocytes in response to UVB irradiation. Treatment with Na3VO4 desensitized keratinocytes to UVB-induced... 
GROWTH-FACTOR RECEPTOR | ACTIVATION | TRANSCRIPTION 3 | PROMOTION STAGES | EPITHELIAL CARCINOGENESIS | SUBSTRATE | BIOLOGY | SKIN CARCINOGENESIS | PROLIFERATION | SIGNAL TRANSDUCER | NEGATIVE REGULATOR | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - radiation effects | Apoptosis - radiation effects | Keratinocytes - radiation effects | RNA, Small Interfering - pharmacology | Cells, Cultured | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - physiology | STAT3 Transcription Factor - radiation effects | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - physiology | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - radiation effects | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - genetics | Protein Tyrosine Phosphatases, Non-Receptor - physiology | Ultraviolet Rays - adverse effects | Protein Tyrosine Phosphatases, Non-Receptor - radiation effects | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - radiation effects | Phosphorylation - radiation effects | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - physiology | Animals | Keratinocytes - metabolism | Protein Tyrosine Phosphatases, Non-Receptor - genetics | Mice | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics | STAT3 Transcription Factor - metabolism | Tyrosine | Phenols | Skin | Phosphatases | Apoptosis | Pediatrics | Phosphorylation | Transcription factors | SHP-1 protein | c-Myc protein | Genomes | Myc protein | Dephosphorylation | Cyclin D1 | Phosphatase | Experiments | Carcinogenesis | Proteins | Signal transduction | Carcinogens | Toxicology | Cell growth | Epidermal growth factor | Rodents | Cell cycle | Translocation | Desensitization | U.V. radiation | RNA-mediated interference | Stat3 protein | Keratinocytes | Epidermis | siRNA | Nuclear transport | Studies | Irradiation | Diabetes | Endoplasmic reticulum | Cytoplasm | Protein-tyrosine-phosphatase | Tumors | Cancer | Index Medicus
Journal Article
2007, Methods in molecular biology, ISBN 9781588297112, Volume 365., xv, 387
Book
Journal of Inorganic Biochemistry, ISSN 0162-0134, 2011, Volume 105, Issue 9, pp. 1138 - 1147
Three dinuclear copper complexes of organic claw ligands (2,2′,2″,2‴-(5-R-2-hydroxy-1,3-phenylene)bis(methylene)bis(azanetriyl)tetraacetic acid, R = methyl (H... 
PTPs | Inhibitor | Selectivity | Dinuclear copper complexes | MOLECULAR CALCULATIONS | RICH COORDINATION ENVIRONMENTS | MECHANISM | EFFECTIVE CORE POTENTIALS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CATALYTIC DOMAIN | CHEMISTRY, INORGANIC & NUCLEAR | TC-PTP | THERAPY | DNA | PURIFICATION | DISEASE | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism | Escherichia coli | Humans | Substrate Specificity | Crystallography, X-Ray | Enzyme Inhibitors - chemical synthesis | Spectrometry, Mass, Electrospray Ionization | Transformation, Bacterial | X-Ray Diffraction | Protein Tyrosine Phosphatases, Non-Receptor - genetics | Acids, Heterocyclic - chemical synthesis | Cloning, Molecular | Copper - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics | Acids, Heterocyclic - pharmacology | Recombinant Proteins - metabolism | Recombinant Proteins - antagonists & inhibitors | Enzyme Inhibitors - pharmacology | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - antagonists & inhibitors | Models, Molecular | Recombinant Proteins - genetics | Chelating Agents - pharmacology | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Potentiometry | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - metabolism | Signal Transduction - drug effects | Protein Tyrosine Phosphatases, Non-Receptor - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - antagonists & inhibitors | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - antagonists & inhibitors | Ligands | Signal Transduction - physiology | Kinetics | Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics | Chelating Agents - chemical synthesis | Protein Tyrosine Phosphatases, Non-Receptor - antagonists & inhibitors | Tyrosine | Phenols | Phosphatases | Analysis | Index Medicus
Journal Article
Experimental Hematology, ISSN 0301-472X, 09/2017, Volume 53, pp. S55 - S55
Journal Article
Journal Article
Current Genetics: Lower Eukaryotes and Organelles, ISSN 0172-8083, 02/2018, Volume 64, Issue 1, p. 43
To access, purchase, authenticate, or subscribe to the full-text of this article, please visit this link: http://dx.doi.org/10.1007/s00294-017-0721-8 The... 
Phosphatases
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 10/2015, Volume 87, pp. S109 - S110
Journal Article
The Journal of Physiology, ISSN 0022-3751, 10/2017, Volume 595, Issue 19, pp. 6231 - 6247
Smooth muscle myosin regulatory light chain (RLC) is phosphorylated by Ca 2+ /calmodulin‐dependent myosin light chain kinase and dephosphorylated by myosin... 
airway smooth muscle | contraction | myosin light chain phosphatase | myosin regulatory light chain phosphorylation | myosin light chain kinase | LIGHT-CHAIN KINASE | PROTEIN PHOSPHATASE-1 | RHO-ASSOCIATED KINASE | CA2+ SENSITIZATION | SKELETAL-MUSCLE | PHYSIOLOGY | MYOGENIC RESPONSE | SALT-INDUCED HYPERTENSION | NEUROSCIENCES | BLOOD-PRESSURE | PHOSPHATASE TARGETING SUBUNIT-1 | CALCIUM SENSITIZATION | Phosphorylation | Signal Transduction | Trachea - cytology | Mice, Inbred C57BL | Myosin-Light-Chain Phosphatase - genetics | Cells, Cultured | Myocytes, Smooth Muscle - physiology | Male | Trachea - metabolism | Carbachol - pharmacology | Protein Phosphatase 1 - metabolism | Animals | Cattle | Myosin-Light-Chain Phosphatase - metabolism | Protein Phosphatase 1 - genetics | Mice | Myosin Light Chains - metabolism | Protein Processing, Post-Translational | Myocytes, Smooth Muscle - drug effects | Myocytes, Smooth Muscle - metabolism | Cholinergic Agonists - pharmacology | Phosphatases | Genetically modified organisms | Myosin | Physiological aspects | Smooth muscle | Calcium-binding proteins | Muscle proteins | Electric fields | Protein kinase C | Calcium | Acetylcholine receptors (muscarinic) | Phosphoprotein phosphatase | Modules | Chains | Stimulation | Dephosphorylation | Phosphatase | Physiological responses | Myosin-light-chain kinase | Myosin-light-chain-phosphatase | Proteins | Respiratory tract | Neostigmine | Rodents | Calcium-binding protein | Light | Nerves | Physiology | Catalysis | Trachea | Genetic modific