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1. Full Text Conformational Motions Regulate Phosphoryl Transfer in Related Protein Tyrosine Phosphatases
by Sean K. Whittier and Alvan C. Hengge and J. Patrick Loria
Science, ISSN 0036-8075, 8/2013, Volume 341, Issue 6148, pp. 899 - 903
Many studies have implicated a role for conformational motions during the catalytic cycle, acting to optimize the binding pocket or facilitate product release,... 
Hydrolysis | Phosphates | Enzymes | Chemical equilibrium | HIV | Interferons | DNA | REPORTS | Retroviridae | Biochemistry | Kinetics | ENZYME CATALYSIS | MULTIDISCIPLINARY SCIENCES | TRIOSEPHOSPHATE ISOMERASE | DIHYDROFOLATE-REDUCTASE | LOOP DYNAMICS | STATE | CHEMICAL-EXCHANGE | Motion | Catalytic Domain | Protein Tyrosine Phosphatases - chemistry | Humans | Phosphates - chemistry | Bacterial Outer Membrane Proteins - chemistry | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Catalysis | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - chemistry | Vanadates - chemistry | Proteins | Phosphorus content | Tyrosine | Catalysts | Cleavage | Closures | Tuning
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2. Full Text Inhibitors of Protein Tyrosine Phosphatases: Next‐Generation Drugs?
by Bialy, Laurent and Waldmann, Herbert
Angewandte Chemie International Edition, ISSN 1433-7851, 06/2005, Volume 44, Issue 25, pp. 3814 - 3839
The protein tyrosine phosphatases (PTPs) constitute a family of closely related key regulatory enzymes that dephosphorylate phosphotyrosine residues in their... 
inhibitors | signal transduction | phosphorylation | medicinal chemistry | phosphatases | Signal transduction | Medicinal chemistry | Phosphorylation | Inhibitors | Phosphatases | PROGRESSIVE MYOCLONUS EPILEPSY | SOLID-PHASE SYNTHESIS | HUMAN BREAST-CANCER | CHEMISTRY, MULTIDISCIPLINARY | ALPHA-KETOCARBOXYLIC ACIDS | SH2-CONTAINING PHOSPHOTYROSINE PHOSPHATASE | GROWTH-FACTOR RECEPTOR | SRC HOMOLOGY-2 DOMAINS | REVERSIBLE COVALENT INHIBITORS | DUAL-SPECIFICITY PHOSPHATASE | INSULIN-RECEPTOR SUBSTRATE-1 | Protein Tyrosine Phosphatases - antagonists & inhibitors | Protein Tyrosine Phosphatases - chemistry | Animals | Stereoisomerism | Enzyme Inhibitors - chemistry | Humans | Molecular Conformation | Drug Design | Enzyme Inhibitors - pharmacology | Models, Molecular | Crystallography, X-Ray | Structure-Activity Relationship
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3. Full Text Protein tyrosine phosphatases PTPδ, PTPσ, and LAR: presynaptic hubs for synapse organization
by Takahashi, Hideto and Craig, Ann Marie
Trends in Neurosciences, ISSN 0166-2236, 2013, Volume 36, Issue 9, pp. 522 - 534
Highlights • Protein tyrosine phosphatases (RPTPs) and neurexins form parallel presynaptic hubs. • RPTPs bind multiple postsynaptic partners in an isoform- and... 
Neurology | Slitrk | TrkC | NGL-3 | synaptogenesis | IL1RAPL1 | neurexin | Neurexin | Synaptogenesis | Nerve Tissue Proteins - metabolism | Protein Tyrosine Phosphatases - chemistry | Protein Tyrosine Phosphatases - genetics | Animals | Synapses - physiology | Humans | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism | Protein Tyrosine Phosphatases - metabolism | Nerve Net - enzymology | Presynaptic Terminals - physiology | Mutation - genetics
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4. Full Text Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2
by Zhou, Tianjun and Sun, Liguang and Humphreys, John and Goldsmith, Elizabeth J and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Structure, ISSN 0969-2126, 2006, Volume 14, Issue 6, pp. 1011 - 1019
MAP kinases bind activating kinases, phosphatases, and substrates through docking interactions. Here, we report a 1.9 Å crystallographic analysis of inactive... 
SIGNALING | SITE | RECOGNITION | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN-KINASES | TYROSINE-PHOSPHATASE | CELL BIOLOGY | SUBSTRATE-SPECIFICITY | PTP-SL | INTERACTION MOTIF | BIOPHYSICS | X-RAY | REGULATORS | Mitogen-Activated Protein Kinase 1 - chemistry | Amino Acid Sequence | Protein Tyrosine Phosphatases - chemistry | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Molecular Sequence Data | Protein Conformation | Enzyme Activation | Protein Tyrosine Phosphatase, Non-Receptor Type 6 | Amino Acid Motifs | Mitogen-Activated Protein Kinase 1 - metabolism | Protein Interaction Mapping | Tyrosine | Phosphatases | Peptides | Phosphotransferases | Analysis
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5. Full Text Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects
by Tanner, John J and Parsons, Zachary D and Cummings, Andrea H and Zhou, Haiying and Gates, Kent S
Antioxidants & Redox Signaling, ISSN 1523-0864, 07/2011, Volume 15, Issue 1, pp. 77 - 97
Protein tyrosine phosphatases (PTPs) are important targets of the H 2 O 2 that is produced during mammalian signal transduction. H 2 O 2 -mediated inactivation... 
Forum Review Articles | SIGNAL-TRANSDUCTION | GROWTH-FACTOR RECEPTOR | SUPEROXIDE RADICAL-ANION | ACTIVE-SITE CYSTEINE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | REVERSIBLE OXIDATION | ENDOCRINOLOGY & METABOLISM | CYSTEINE SULFENIC ACID | HYDROGEN-PEROXIDE | DISULFIDE INTERCHANGE REACTIONS | TUMOR-SUPPRESSOR PTEN | Protein Tyrosine Phosphatases - chemistry | Animals | Oxidation-Reduction | Humans | Protein Tyrosine Phosphatases - metabolism | Structure-Activity Relationship | Hydrogen Peroxide - metabolism | Physiological aspects | Protein tyrosine kinase | Cellular signal transduction | Thiols | Research | Structure
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6. Full Text Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome
by Barr, Alastair J and Ugochukwu, Emilie and Lee, Wen Hwa and King, Oliver N.F and Filippakopoulos, Panagis and Alfano, Ivan and Savitsky, Pavel and Burgess-Brown, Nicola A and Müller, Susanne and Knapp, Stefan
Cell, ISSN 0092-8674, 01/2009, Volume 136, Issue 2, pp. 352 - 363
Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present... 
PROTEINS | SIGNALING | PTP-SIGMA | SUBSTRATE-SPECIFICITY | RPTP-ALPHA | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH | DIFFRACTION DATA | INHIBITOR | RECEPTOR-TYPE-Z | CELL BIOLOGY | Protein Structure, Tertiary | Amino Acid Sequence | Protein Tyrosine Phosphatases - chemistry | Protein Tyrosine Phosphatases - genetics | Sequence Alignment | Humans | Models, Molecular | Crystallography, X-Ray | Protein Tyrosine Phosphatases - metabolism | Structure-Activity Relationship | Dimerization | Tyrosine | Enzymes | Phosphatases | Analysis | Crystals | Phenols | Universities and colleges | Structure | Resource
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7. Full Text Allosteric inhibition of protein tyrosine phosphatase 1B
by Shen, Wang and Erlanson, Daniel A and Taylor, Lisa and Randal, Mike and Kung, Jenny and Fahr, Bruce J and Hansen, Stig K and Zhong, Min and McDowell, Robert S and Wiesmann, Christian and Zhu, Jiang and Barr, Kenneth J
Nature Structural & Molecular Biology, ISSN 1545-9993, 08/2004, Volume 11, Issue 8, pp. 730 - 737
Obesity and type II diabetes are closely linked metabolic syndromes that afflict > 100 million people worldwide. Although protein tyrosine phosphatase 1B... 
VISUALIZATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | IDENTIFICATION | INSULIN SENSITIVITY | CELL BIOLOGY | PTP1B | BIOPHYSICS | INTERMEDIATE | ADIPOSITY | BINDING | DOMAINS | Models, Chemical | Humans | Crystallography, X-Ray | Dose-Response Relationship, Drug | Protein Tyrosine Phosphatases - chemistry | Transfection | Time Factors | Cloning, Molecular | Inhibitory Concentration 50 | Catalysis | Binding Sites | Tyrosine - chemistry | CHO Cells | Binding, Competitive | Protein Structure, Tertiary | Obesity | Catalytic Domain | Cricetinae | Models, Molecular | DNA - chemistry | Animals | Protein Tyrosine Phosphatase, Non-Receptor Type 1 | Allosteric Site | Protein Binding | Ligands | Protein Conformation | Kinetics | Phosphoric Monoester Hydrolases - chemistry | Proteins | Physiological aspects | Phosphatases | Research | Structure | Protein binding
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