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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
Book
2009, Methods in Enzymology, ISBN 9780123746221, Volume 457, 578
In this second of two new volumes covering mitochondria, methods developed to assess the number and function of nuclear-encoded proteins in the mitochondrion... 
Mitochondria | Phosphoprotein phosphatases | Active oxygen | Electron transport | Protein kinases
eBook
PloS one, ISSN 1932-6203, 04/2010, Volume 5, Issue 4, pp. e10290 - e10290
Stat3 is initially dephosphorylated in murine keratinocytes in response to UVB irradiation. Treatment with Na(3)VO(4) desensitized keratinocytes to UVB-induced... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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
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... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | Index Medicus
Journal Article
The FEBS journal, ISSN 1742-464X, 01/2013, Volume 280, Issue 2, pp. 644 - 661
Journal Article