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2003, Methods in enzymology, ISBN 9780121822699, Volume 366, l, 453 p., [4] p. of plates
Book
Biochemical journal, ISSN 1470-8728, 2009, Volume 418, Issue 3, pp. 475 - 489
Journal Article
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
Journal Article
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
PLoS ONE, ISSN 1932-6203, 08/2015, Volume 10, Issue 8, p. e0134984
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine... 
OVEREXPRESSION | ACTIVATION | OVERPRODUCTION | CRYSTAL-STRUCTURE | KINASE PHOSPHATASE-1 | MULTIDISCIPLINARY SCIENCES | PURIFICATION | PROTEIN-TYROSINE PHOSPHATASES | INHIBITORS | CATALYTIC MECHANISM | CANCER | 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 | Proteomes | Alzheimers disease | Recognition | Cancer
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