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PloS one, ISSN 1932-6203, 2010, Volume 5, Issue 4, p. 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
Journal Article
Cell metabolism, ISSN 1550-4131, 2011, Volume 14, Issue 5, pp. 684 - 699
Journal Article
Journal Article
American journal of physiology: endocrinology and metabolism, ISSN 1522-1555, 2012, Volume 303, Issue 3, pp. E410 - E421
Cachexia, the metabolic dysregulation leading to sustained loss of muscle and adipose tissue, is a devastating complication of cancer and other chronic... 
Signal transducer and activator of transcription | Incb018424 | Electroporation | Inhibitory peptide | T cell protein tyrosine phosphatase/ protein tyrosine phosphatase | Janus-activated kinase | Interleukin-6 | Atrophy | Burn | Suppressors of cytokine signaling 3 | Lipopolysaccharide | Sepsis | Nonreceptor type 2 | burn | ACTIVATION | CYTOKINES | PHYSIOLOGY | ADENOCARCINOMA | STAT3 | suppressors of cytokine signaling 3 | signal transducer and activator of transcription 3 inhibitory peptide | INDUCTION | interleukin-6 | incb018424 | SIGNALING PATHWAY | T cell protein tyrosine phosphatase/protein tyrosine phosphatase | IN-VIVO | ENDOCRINOLOGY & METABOLISM | atrophy | nonreceptor type 2 | MICE | electroporation | lipopolysaccharide | CILIARY NEUROTROPHIC FACTOR | sepsis | Neoplasms - metabolism | Wasting Syndrome - prevention & control | Wasting Syndrome - metabolism | Cricetulus | Male | Muscle, Skeletal - metabolism | Janus Kinases - metabolism | Neoplasms - complications | Neoplasms - genetics | Muscle, Skeletal - drug effects | Cachexia - etiology | Interleukin-6 - physiology | Female | Interleukin-6 - metabolism | STAT3 Transcription Factor - genetics | STAT3 Transcription Factor - metabolism | CHO Cells | Disease Models, Animal | Pyrazoles - pharmacology | Cricetinae | Cachexia - genetics | Interleukin-6 - genetics | Janus Kinases - genetics | Mice, Inbred C57BL | RNA, Small Interfering - pharmacology | Cells, Cultured | Mutant Proteins - genetics | Mice, Transgenic | Signal Transduction - genetics | Wasting Syndrome - genetics | Cachexia - prevention & control | Mutant Proteins - administration & dosage | Neoplasms - drug therapy | Janus Kinases - antagonists & inhibitors | Protein Kinase Inhibitors - administration & dosage | Pyrazoles - administration & dosage | Animals | Signal Transduction - drug effects | Mice, Nude | Cachexia - pathology | Mice | Protein Kinase Inhibitors - pharmacology | Muscle, Skeletal - pathology | RNA, Small Interfering - administration & dosage | STAT3 Transcription Factor - antagonists & inhibitors | Wasting Syndrome - pathology | Transcription factors | Control | Analysis | Muscles | Genetic aspects | Wasting syndrome | protein tyrosine phosphatase, nonreceptor type 2 | T cell protein tyrosine phosphatase
Journal Article
Blood, ISSN 1528-0020, 2018, Volume 131, Issue 10, pp. 1122 - 1144
Journal Article
Nature immunology, ISSN 1529-2916, 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
Journal Article
Biochemical journal, ISSN 0264-6021, 02/2007, Volume 402, Issue 1, pp. 1 - 15
It is now well established that the members of the PTP (protein tyrosine phosphatase) superfamily play critical roles in fundamental biological processes.... 
Substrate identification | Tyrosine phosphorylation | Protein tyrosine phosphatase (PTP) | Substrate-trapping | KINASE-ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | FACTOR RECEPTOR | NEGATIVE REGULATOR | SIGNAL-TRANSDUCTION | INSULIN-RECEPTOR | protein tyrosine phosphatase (PTP) | EPIDERMAL-GROWTH-FACTOR | IN-VIVO | HELICOBACTER-PYLORI CAGA | substrate-trapping | tyrosine phosphorylation | PTP-PEST | substrate identification | T-CELLS | Protein Structure, Tertiary | Phosphorylation | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Humans | Substrate Specificity | Protein Tyrosine Phosphatases - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Protein Tyrosine Phosphatases - genetics | Tyrosine - metabolism | Animals | Models, Biological | Protein Tyrosine Phosphatase, Non-Receptor Type 1 | Binding Sites | serine | SH, Src homology | CSK, C-terminal Src kinase | RNAi, RNA interference | PTK, protein tyrosine kinase | MKP, MAPK phosphatase | IRS, IR substrate | CSF-1, colony-stimulating factor 1 | SHP, SH2-domain-containing protein tyrosine phosphatase | ERK, extracellular-signal-regulated kinase | PIR-B, paired immunoglobulin-like receptor B | ZAP-70, ζ-chain-associated protein kinase of 70 kDa | KIM, kinase-interacting motif | FAK, focal adhesion kinase | EGFR, epidermal growth factor receptor | STEP, striatal-enriched PTP | LYP, lymphoid phosphatase | MAPK, mitogen-activated protein kinase | PTP, protein tyrosine phosphatase | SNARE, NSF-attachment protein receptor | TCR, T-cell receptor | PI3K, phosphoinositide 3-kinase | Gab1, Grb2-associated binder-1 | PAG, phosphoprotein associated with glycosphingolipid-enriched membrane microdomains | Cbp, C-terminal Src kinase-binding protein | SNP, single-nucleotide polymorphism | Review | WASP, Wiskott–Aldrich syndrome protein | NSF, N-ethylmaleimide-sensitive factor | PDGFR, platelet-derived growth factor receptor | AP-1, activator protein 1 | PEP, PEST (Pro-Glu-Ser-Thr) domain phosphatase | SFK, Src family kinase | DSP, dual-specificity phosphatase | PSTPIP, proline | NS, Noonan syndrome | IR, insulin receptor | IFN, interferon | STAT, signal transducer and activator of transcription | NFAT, nuclear factor of activated T-cells | IGF-1, insulin-like growth factor 1 | BIT, brain immunoglobulin-like molecule with tyrosine-based activation motifs | threonine-phosphatase-interacting protein | TCPTP, T-cell PTP | JAK, Janus kinase | MEF, mouse embryonic fibroblast | BCR, B-cell receptor | GAP, GTPase-activating protein | HGF, hepatocyte growth factor
Journal Article
Nature (London), ISSN 1476-4687, 2017, Volume 547, Issue 7664, pp. 413 - 418
Immunotherapy with PD-1 checkpoint blockade is effective in only a minority of patients with cancer, suggesting that additional treatment strategies are... 
CELLS | GENE | MULTIDISCIPLINARY SCIENCES | CD94/NKG2A | BLOCKADE | EXPRESSION | PD-1 | HLA-E | Tumor Escape - drug effects | Immunotherapy - methods | Loss of Function Mutation | Tumor Escape - genetics | Genomics | Humans | NF-kappa B - metabolism | Interferons - immunology | Melanoma, Experimental - immunology | T-Lymphocytes - drug effects | Tumor Escape - immunology | Melanoma, Experimental - therapy | Melanoma, Experimental - pathology | Antigen Presentation - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - deficiency | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Antigen Presentation - immunology | Unfolded Protein Response | CRISPR-Cas Systems - genetics | Gene Editing | Xenograft Model Antitumor Assays | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism | Animals | Melanoma, Experimental - genetics | T-Lymphocytes - immunology | Mice | Care and treatment | Analysis | Immunotherapy | Diagnosis | Genetic screening | Methods | Cancer | Animal models | PD-1 protein | Genes | Genomes | Synergism | Proteins | Signal transduction | Clonal deletion | Lymphocytes | Protein folding | Tyrosine | Antigen presentation | NF-κB protein | CRISPR | Melanoma | Medical screening | Patients | Screening | Signaling | Immune checkpoint | PD-L1 protein | Interferon | Genetic testing | Tumors | Protein-tyrosine-phosphatase | PTPN2 protein
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2018, Volume 175, Issue 5, pp. 1289 - 1306.e20
Obesity is a major driver of cancer, especially hepatocellular carcinoma (HCC). The prevailing view is that non-alcoholic steatohepatitis (NASH) and fibrosis... 
nonalcoholic fatty liver disease | protein tyrosine phosphatase | STAT-1 | fibrosis | STAT-3 | T cells | hepatocellular carcinoma | obesity | oxidative stress | PTPN2 | non-alcoholic steatohepatitis | CELLS | HEPATOCELLULAR-CARCINOMA | METABOLIC SYNDROME | ACTIVATION | FATTY LIVER-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMICAL HEPATOCARCINOGENESIS | NONALCOHOLIC STEATOHEPATITIS | INSULIN SENSITIVITY | CANCER | PROTEIN-TYROSINE-PHOSPHATASE | CELL BIOLOGY | Non-alcoholic Fatty Liver Disease - pathology | Liver - pathology | Oxidative Stress | Humans | Hepatocytes - metabolism | STAT1 Transcription Factor - metabolism | Diet, High-Fat | Liver Cirrhosis - metabolism | CD8-Positive T-Lymphocytes - metabolism | Liver Neoplasms - pathology | STAT3 Transcription Factor - metabolism | Disease Models, Animal | Signal Transduction | Liver - metabolism | Mice, Inbred C57BL | Non-alcoholic Fatty Liver Disease - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - deficiency | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - genetics | Mice, Knockout | Obesity - metabolism | Obesity - pathology | Protein Tyrosine Phosphatase, Non-Receptor Type 2 - metabolism | Animals | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Liver Cirrhosis - pathology | Mice | CD8-Positive T-Lymphocytes - immunology | Carcinoma, Hepatocellular - metabolism | Tyrosine | Obesity | Liver cancer | Phosphatases | Liver | Alcoholics | Liver cirrhosis
Journal Article
Nature chemical biology, ISSN 1552-4469, 2014, Volume 10, Issue 7, pp. 558 - 566
PTP1B, a validated therapeutic target for diabetes and obesity, has a critical positive role in HER2 signaling in breast tumorigenesis. Efforts to develop... 
LAPATINIB | OVEREXPRESSION | TYROSINE-PHOSPHATASE 1B | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACQUIRED-RESISTANCE | BINDING-SITE | MECHANISMS | INDUCTION | HUMAN BREAST-CANCER | CONTRIBUTES | TUMORS | Receptor, ErbB-2 - genetics | Humans | Gene Expression Regulation, Neoplastic | Receptor, ErbB-2 - metabolism | Molecular Targeted Therapy | Mammary Neoplasms, Experimental - genetics | Breast Neoplasms - enzymology | Protein Binding - drug effects | Mammary Neoplasms, Experimental - pathology | Female | Antineoplastic Agents - pharmacology | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - genetics | Mammary Neoplasms, Experimental - enzymology | Spermine - analogs & derivatives | Mammary Neoplasms, Experimental - drug therapy | Allosteric Regulation - drug effects | Protein Structure, Tertiary | Catalytic Domain | Protein Structure, Secondary | Signal Transduction | Allosteric Site - drug effects | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors | Spermine - chemistry | Models, Molecular | Antineoplastic Agents - chemistry | Breast Neoplasms - drug therapy | Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism | Animals | Breast Neoplasms - genetics | Spermine - pharmacology | Breast Neoplasms - pathology | Cholestanes - chemistry | Cholestanes - pharmacology | Mice | Kinetics | Breast cancer | Tumorigenesis | Diabetes | Drug therapy | Cholestanes | Allosteric Regulation | Breast Neoplasms | Life Sciences | Biomolecules | Biochemistry, Molecular Biology | Antineoplastic Agents | Spermine | Protein Tyrosine Phosphatase, Non-Receptor Type 1 | Mammary Neoplasms, Experimental | Allosteric Site | Protein Binding | Receptor, ErbB-2
Journal Article