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1. Full Text Protein tyrosine phosphatases in lymphocyte activation and autoimmunity
by Rhee, Inmoo and Veillette, André
Nature Immunology, ISSN 1529-2908, 05/2012, Volume 13, Issue 5, pp. 439 - 447
Lymphocyte activation must be tightly regulated to ensure sufficient immunity to pathogens and prevent autoimmunity. Protein tyrosine phosphatases (PTPs) serve... 
SIGNAL-TRANSDUCTION | IMMUNE CELLS | T-CELL-RECEPTOR | PTPN22 ALLELIC VARIANT | IMMUNOLOGY | IMMATURE B-CELLS | SRC-FAMILY KINASES | ANTIGEN RECEPTOR | NEGATIVE REGULATORY TYROSINE | CUTTING EDGE | PHOSPHOTYROSINE PHOSPHATASE | Antigens, CD - immunology | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - immunology | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - immunology | Humans | Autoimmunity - genetics | NK Cell Lectin-Like Receptor Subfamily K - immunology | Protein Tyrosine Phosphatases - metabolism | Leukocyte Common Antigens - immunology | Signal Transduction - immunology | Protein Tyrosine Phosphatases - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 22 - immunology | Signaling Lymphocytic Activation Molecule Family Member 1 | Autoimmunity - immunology | Receptors, Antigen, T-Cell - immunology | Lymphocyte Activation | Protein Tyrosine Phosphatase, Non-Receptor Type 22 - genetics | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - immunology | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Receptors, Cell Surface - immunology | Receptors, Antigen, B-Cell - immunology | Animals | Lymphocytes - enzymology | Mice | Protein Tyrosine Phosphatase, Non-Receptor Type 6 - deficiency | Protein Tyrosine Phosphatase, Non-Receptor Type 12 - immunology | Tyrosine | Autoimmunity | Phosphatases | Immune response | Lymphocytes | Physiological aspects | Research | Properties
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2. Full Text LAR protein tyrosine phosphatase regulates focal adhesions through CDK1
by Sarhan, Adil R and Patel, Trushar R and Cowell, Alana R and Tomlinson, Michael G and Hellberg, Carina and Heath, John K and Cunningham, Debbie L and Hotchin, Neil A
Journal of Cell Science, ISSN 0021-9533, 2016, Volume 129, Issue 15, pp. 2962 - 2971
Focal adhesions are complex multi-molecular structures that link the actin cytoskeleton to the extracellular matrix through integrin adhesion receptors and... 
CDK1 | Focal adhesions | PTPRF | Cell adhesion | LAR phosphatase | INTEGRIN ADHESOME | KINASE-ACTIVITY | COMPLEX | PHOSPHORYLATION | SRC | RECEPTOR | DROSOPHILA FOLLICULAR EPITHELIUM | CELL BIOLOGY | FAK | CELL-MIGRATION | IN-VIVO | Fibronectins - pharmacology | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Cell Adhesion - drug effects | CDC2 Protein Kinase - metabolism | Focal Adhesions - drug effects | Animals | Signal Transduction - drug effects | Models, Biological | Focal Adhesions - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism | Proto-Oncogene Proteins c-abl - metabolism | Mice | Phosphorylation - drug effects | Proto-Oncogene Proteins c-akt - metabolism
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3. Full Text Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase β activity
by Wilson, Matthew and Hogstrand, Christer and Maret, Wolfgang
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 12, pp. 9322 - 9326
As key enzymes in the regulation of biological phosphorylations, protein-tyrosine phosphatases are central to the control of cellular signaling and metabolism.... 
INHIBITION | REDOX REGULATION | FLUCTUATIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ZN(II) | PURIFICATION | CATALYTIC DOMAIN | TARGETS | COORDINATION | CELL | ZN2 | Protein Structure, Tertiary | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - genetics | Signal Transduction | Enzyme Inhibitors - chemistry | Humans | Enzyme Inhibitors - pharmacology | Kinetics | Zinc - pharmacology | Zinc - chemistry | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - chemistry | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - metabolism | Enzymes | Enzyme Inhibitors | Endothelial Cell Physiology | Enzyme Regulation | Zinc Enzymes | Reports | Enzyme Kinetics | Transition Metal Signaling | Metalloenzymes | Protein-tyrosine phosphatases | Zinc
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4. Full Text Receptor-type protein-tyrosine phosphatase ζ is a functional receptor for interleukin-34
by Nandi, Sayan and Cioce, Mario and Yeung, Yee-Guide and Nieves, Edward and Tesfa, Lydia and Lin, Haishan and Hsu, Amy W and Halenbeck, Robert and Cheng, Hui-Yong and Gokhan, Solen and Mehler, Mark F and Stanley, E. Richard
Journal of Biological Chemistry, ISSN 0021-9258, 07/2013, Volume 288, Issue 30, pp. 21972 - 21986
Interleukin-34 (IL-34) is highly expressed in brain. IL-34 signaling via its cognate receptor, colony-stimulating factor-1 receptor (CSF-1R), is required for... 
Paxillin - metabolism | NIH 3T3 Cells | Humans | Molecular Sequence Data | Interleukins - metabolism | Receptor, Macrophage Colony-Stimulating Factor - metabolism | Brain - metabolism | Receptors, Interleukin - metabolism | Glioblastoma - genetics | RNA Interference | Base Sequence | Mass Spectrometry | Glioblastoma - metabolism | Interleukins - pharmacology | Phosphorylation - drug effects | Amino Acid Sequence | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - genetics | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Receptors, Interleukin - genetics | Blotting, Western | Tyrosine - metabolism | Animals | Glioblastoma - pathology | Cell Line, Tumor | Protein Binding | Cell Proliferation - drug effects | Mice | Microscopy, Fluorescence | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - metabolism | Brain | CSF-1 Receptor | Signal Transduction | Interleukin | Glioblastoma | Neurobiology | Development | Phosphotyrosine Signaling | Cell Surface Receptor | Tyrosine Protein Phosphatase (Tyrosine Phosphatase)
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5. Full Text Effects of vascular-endothelial protein tyrosine phosphatase inhibition on breast cancer vasculature and metastatic progression
by Goel, Shom and Gupta, Nisha and Walcott, Brian P and Snuderl, Matija and Kesler, Cristina T and Kirkpatrick, Nathaniel D and Heishi, Takahiro and Huang, Yuhui and Martin, John D and Ager, Eleanor and Samuel, Rekha and Wang, Shuhan and Yazbek, John and Vakoc, Benjamin J and Peterson, Randall T and Padera, Timothy P and Duda, Dan G and Fukumura, Dai and Jain, Rakesh K
Journal of the National Cancer Institute, ISSN 0027-8874, 08/2013, Volume 105, Issue 16, pp. 1188 - 1201
The solid tumor microvasculature is characterized by structural and functional abnormality and mediates several deleterious aspects of tumor behavior. Here we... 
SURVIVAL | ANTIANGIOGENIC THERAPY | OVEREXPRESSING ANGIOPOIETIN-1 | ANGIOGENESIS | ONCOLOGY | BLOOD-VESSEL DEVELOPMENT | VEGF | OXYGENATION | NORMALIZATION | PERFUSION | TUMOR-GROWTH | Human Umbilical Vein Endothelial Cells | Zebrafish Proteins - metabolism | Mice, Inbred C57BL | Enzyme Inhibitors - pharmacology | Angiogenesis Inhibitors - pharmacology | Zebrafish | Breast Neoplasms - blood supply | Enzyme Activation - drug effects | Disease Progression | Drug Synergism | Xenograft Model Antitumor Assays | Animals | Lung Neoplasms - prevention & control | Lung Neoplasms - secondary | Breast Neoplasms - pathology | Neovascularization, Pathologic - drug therapy | Female | Receptor, TIE-2 - metabolism | Antineoplastic Agents - pharmacology | Mice | Nitric Oxide Synthase Type III - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - antagonists & inhibitors | Phosphatases | Blood-vessels | Physiological aspects | Development and progression | Vascular endothelium | Breast cancer | Research | Tumors
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6. 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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7. Full Text Role of chondroitin sulfate (CS) modification in the regulation of protein-tyrosine phosphatase receptor type Z (PTPRZ) activity: Pleiotrophin-PTPRZ-A signaling is involved in oligodendrocyte differentiation
by Kuboyama, Kazuya and Fujikawa, Akihiro and Suzuki, Ryoko and Tanga, Naomi and Noda, Masaharu
Journal of Biological Chemistry, ISSN 0021-9258, 08/2016, Volume 291, Issue 35, pp. 18117 - 18128
Protein-tyrosine phosphatase receptor type Z (PTPRZ) is predominantly expressed in the developing brain as a CS proteoglycan. PTPRZ has long (PTPRZ-A) and... 
SUBSTRATE-TRAPPING SYSTEM | chondroitin sulfate | BIOCHEMISTRY & MOLECULAR BIOLOGY | oligodendrocyte | 6B4 PROTEOGLYCAN/PHOSPHACAN | proteoglycan | phosphotyrosine signaling | MYELIN BASIC-PROTEIN | EXTRACELLULAR VARIANT | pleiotrophin | MULTIPLE-SCLEROSIS | BINDING GROWTH-FACTOR | CENTRAL-NERVOUS-SYSTEM | ZETA RPTP-BETA | ZETA/RPTP-BETA | DEVELOPMENTAL EXPRESSION | Oligodendroglia - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - genetics | Chondroitin Sulfates - genetics | Chondroitin Sulfates - metabolism | Cytokines - metabolism | Signal Transduction | Humans | Neural Stem Cells - cytology | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Mice, Mutant Strains | Cell Differentiation | Mice | Oligodendroglia - cytology | Cytokines - genetics | Neural Stem Cells - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 5 - metabolism | Cell Biology
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8. Full Text Targeting protein tyrosine phosphatase σ after myocardial infarction restores cardiac sympathetic innervation and prevents arrhythmias
by Gardner, R.T and Wang, L and Lang, B.T and Cregg, J.M and Dunbar, C.L and Woodward, W.R and Silver, J and Ripplinger, C.M and Habecker, B.A
Nature Communications, ISSN 2041-1723, 2015, Volume 6, Issue 1, p. 6235
Millions of people suffer a myocardial infarction (MI) every year, and those who survive have increased risk of arrhythmias and sudden cardiac death. Recent... 
Arrhythmias, Cardiac - prevention & control | Calcium - metabolism | Male | Mice, Transgenic | Sympathetic Nervous System - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - antagonists & inhibitors | Animals | Myocardial Infarction - drug therapy | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism | Electrocardiography | Female | Mice | Mice, Inbred BALB C | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - genetics | Receptors, Adrenergic, beta - metabolism | Peptides - therapeutic use
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9. Full Text Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling
by Arora, Deepika and Stopp, Sabine and Böhmer, Sylvia-Annette and Schons, Julia and Godfrey, Rinesh and Masson, Kristina and Razumovskaya, Elena and Rönnstrand, Lars and Tänzer, Simone and Bauer, Reinhard and Böhmer, Frank-D and Mü Ller, Jörg P and Lund University and BioCARE: Biomarkers in Cancer Medicine improving Health Care, Education and Innovation and Lunds universitet and Institutionen för translationell medicin and Department of Translational Medicine
Journal of Biological Chemistry, ISSN 0021-9258, 04/2011, Volume 286, Issue 13, pp. 10918 - 10929
Fms-like tyrosine kinase 3 (FLT3) plays an important role in hematopoietic differentiation, and constitutively active FLT3 mutant proteins contribute to the... 
TRANSFORMATION | ACTIVATION | JUXTAMEMBRANE DOMAIN | 32D CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACUTE MYELOGENOUS LEUKEMIA | GROWTH | ACUTE MYELOID-LEUKEMIA | MUTATIONS | ONCOGENIC FLT3 | IDENTIFICATION | Phosphorylation | Humans | Male | Leukemia - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - genetics | Mutation, Missense | Cell Transformation, Neoplastic - metabolism | fms-Like Tyrosine Kinase 3 - metabolism | Gene Knockdown Techniques | fms-Like Tyrosine Kinase 3 - genetics | STAT5 Transcription Factor - genetics | STAT5 Transcription Factor - metabolism | Animals | Cell Transformation, Neoplastic - genetics | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism | HEK293 Cells | Cell Line, Tumor | Signal Transduction - physiology | Mice | Enzyme Activation - physiology | Leukemia - genetics | Amino Acid Substitution | siRNA | Signal Transduction | Phosphatase | shRNA | Cell Biology | Receptor Tyrosine Kinase | Medicinal Chemistry | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Läkemedelskemi | Medicinska och farmaceutiska grundvetenskaper
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10. Full Text Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice
by Fry, Elizabeth J and Chagnon, Melanie J and López‐Vales, Rubèn and Tremblay, Michel L and David, Samuel
Glia, ISSN 0894-1491, 03/2010, Volume 58, Issue 4, pp. 423 - 433
Receptor protein tyrosine phosphatase sigma (RPTPσ) plays a role in inhibiting axon growth during development. It has also been shown to slow axon regeneration... 
spinal cord injury | axon regeneration | receptor protein tyrosine phosphatase | Spinal cord injury | Axon regeneration | Receptor protein tyrosine phosphatase | AXONAL REGENERATION | CNS | GUIDANCE | NEUROSCIENCES | PTP-SIGMA | GROWTH CONES | REPAIR | MYELIN | NEURITE OUTGROWTH | CRYP-ALPHA | CENTRAL-NERVOUS-SYSTEM | Nerve Regeneration - physiology | Cells, Cultured | Chondroitin Sulfate Proteoglycans - metabolism | Axons - physiology | Cerebellum - physiopathology | Mice, Knockout | Myelin Sheath - metabolism | Pyramidal Tracts - physiopathology | Animals | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism | Neurons - physiology | Female | Mice | Mice, Inbred BALB C | Spinal Cord Injuries - physiopathology | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - genetics
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11. Full Text Receptor-type tyrosine-protein phosphatase κ directly targets STAT3 activation for tumor suppression in nasal NK/T-cell lymphoma
by Chen, Yun-Wen and Chen, Yun-Wen and Guo, Tianhuan and Guo, Tianhuan and Shen, Lijun and Shen, Lijun and Wong, Kai-Yau and Wong, Kai-Yau and Tao, Qian and Tao, Qian and Choi, William W. L and Choi, William W. L and Au-Yeung, Rex K. H and Au-Yeung, Rex K. H and Chan, Yuen-Piu and Chan, Yuen-Piu and Wong, Michelle L. Y and Wong, Michelle L. Y and Tang, Johnny C. O and Tang, Johnny C. O and Liu, Wei-Ping and Liu, Wei-Ping and Li, Gan-Di and Li, Gan-Di and Shimizu, Norio and Shimizu, Norio and Loong, Florence and Loong, Florence and Tse, Eric and Tse, Eric and Kwong, Yok-Lam and Kwong, Yok-Lam and Srivastava, Gopesh and Srivastava, Gopesh
Blood, ISSN 0006-4971, 2015, Volume 125, Issue 10, pp. 1589 - 1600
Nasal-type natural killer/T-cell lymphoma(NKTCL) is an aggressive disease characterized by frequent deletions on 6q, and constitutive activation of signal... 
LYMPHOMA/LEUKEMIA | CONSISTENT PATTERNS | R-PTP-KAPPA | GENE | KILLER (NK)/T-CELL LYMPHOMA | GROWTH | LEUKEMIA | COMPARATIVE GENOMIC HYBRIDIZATION | IDENTIFICATION | HEMATOLOGY | SMILE CHEMOTHERAPY | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - deficiency | Phosphorylation | Cell Proliferation | Prognosis | Humans | Middle Aged | Male | STAT3 Transcription Factor - chemistry | RNA, Messenger - metabolism | RNA, Neoplasm - metabolism | Gene Knockdown Techniques | Lymphoma, Extranodal NK-T-Cell - genetics | DNA Methylation | Caspases - metabolism | Cell Nucleus - metabolism | DNA Mutational Analysis | Tumor Suppressor Proteins - deficiency | Gene Deletion | Tumor Suppressor Proteins - genetics | Female | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - genetics | Nose Neoplasms - metabolism | STAT3 Transcription Factor - metabolism | Promoter Regions, Genetic | Nose Neoplasms - pathology | Tumor Suppressor Proteins - metabolism | Neoplasm Invasiveness | Down-Regulation | RNA, Messenger - genetics | Nose Neoplasms - genetics | Lymphoma, Extranodal NK-T-Cell - pathology | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism | Cell Line, Tumor | Protein Binding | RNA, Neoplasm - genetics | Apoptosis | Lymphoma, Extranodal NK-T-Cell - metabolism
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12. Full Text PTPRD (protein tyrosine phosphatase receptor type delta) is associated with restless legs syndrome
by Schormair, Barbara and Kemlink, David and Roeske, Darina and Eckstein, Gertrud and Xiong, Lan and Lichtner, Peter and Ripke, Stephan and Trenkwalder, Claudia and Zimprich, Alexander and Stiasny-Kolster, Karin and Oertel, Wolfgang and Bachmann, Cornelius G and Paulus, Walter and Högl, Birgit and Frauscher, Birgit and Gschliesser, Viola and Poewe, Werner and Peglau, Ines and Vodicka, Pavel and Vávrová, Jana and Sonka, Karel and Nevsimalova, Sona and Montplaisir, Jacques and Turecki, Gustavo and Rouleau, Guy and Gieger, Christian and Illig, Thomas and Wichmann, H-Erich and Holsboer, Florian and Müller-Myhsok, Bertram and Meitinger, Thomas and Winkelmann, Juliane
Nature Genetics, ISSN 1061-4036, 2008, Volume 40, Issue 8, pp. 946 - 948
We identified association of restless legs syndrome (RLS) with PTPRD at 9p23-24 in 2,458 affected individuals and 4,749 controls from Germany, Austria, Czechia... 
CHROMOSOME 9P | SLEEP | PERIODIC LIMB MOVEMENTS | GENETICS & HEREDITY | GENETIC RISK-FACTOR | LINKAGE | LOCUS | CANCER | FAMILY | Canada | Austria | Czech Republic | Genetic Predisposition to Disease | Humans | 5' Untranslated Regions - genetics | Polymorphism, Single Nucleotide | Receptor-Like Protein Tyrosine Phosphatases, Class 2 - genetics | Case-Control Studies | Germany | Restless Legs Syndrome - genetics | Restless legs syndrome | Protein research | Genetic aspects | Research | Single nucleotide polymorphisms | Gene expression | Medical research | Statistical analysis | Sample size | Genetics | Mass spectrometry | Chromosomes | Cell adhesion & migration
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