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 | Life Sciences
Laboratory manuals | Phosphoprotein phosphatases | Microbiology | Biochemistry, general | Biochemistry | Life Sciences
Book
Biochemical Journal, ISSN 0264-6021, 01/2009, Volume 417, Issue 2, pp. 401 - 409
Protein phosphorylation appears to be a universal mechanism of protein regulation. Genomics has provided the means to compile inventories of protein...
TFIIF associating component of CTD phosphatase/small CTD phosphatase (FCP1/SCP) | Genomics | Laforin | Phylogenetics | Protein tyrosine phosphatase (PTP) | Kelch phosphatase | Starch excess 4 (SEX4) | laforin | CATALYTIC SUBUNIT | kelch phosphatase | SERINE/THREONINE PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | starch excess 4 (SEX4) | TYROSINE PHOSPHATASES | SACCHAROMYCES-CEREVISIAE | PHOSPHOPROTEOME ANALYSIS | MONOSIGA-BREVICOLLIS | TFIIF associating component of CTD phosphatase/small CTD | protein tyrosine phosphatase (PTP) | BACILLUS-SUBTILIS | CARBOXYL-TERMINAL DOMAIN | genomics | phylogenetics | GENE FAMILY | phosphatase (FCPI/SCP) | SER/THR PHOSPHATASES | Humans | Phosphoprotein Phosphatases - metabolism | Substrate Specificity | Protein Subunits - metabolism | Plants - metabolism | Animals | Phosphoprotein Phosphatases - genetics | Plants - genetics | Phosphoprotein Phosphatases - classification | Enzyme Activation | Evolution, Molecular | Phosphoprotein Phosphatases - chemistry | Protein Subunits - genetics
TFIIF associating component of CTD phosphatase/small CTD phosphatase (FCP1/SCP) | Genomics | Laforin | Phylogenetics | Protein tyrosine phosphatase (PTP) | Kelch phosphatase | Starch excess 4 (SEX4) | laforin | CATALYTIC SUBUNIT | kelch phosphatase | SERINE/THREONINE PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | starch excess 4 (SEX4) | TYROSINE PHOSPHATASES | SACCHAROMYCES-CEREVISIAE | PHOSPHOPROTEOME ANALYSIS | MONOSIGA-BREVICOLLIS | TFIIF associating component of CTD phosphatase/small CTD | protein tyrosine phosphatase (PTP) | BACILLUS-SUBTILIS | CARBOXYL-TERMINAL DOMAIN | genomics | phylogenetics | GENE FAMILY | phosphatase (FCPI/SCP) | SER/THR PHOSPHATASES | Humans | Phosphoprotein Phosphatases - metabolism | Substrate Specificity | Protein Subunits - metabolism | Plants - metabolism | Animals | Phosphoprotein Phosphatases - genetics | Plants - genetics | Phosphoprotein Phosphatases - classification | Enzyme Activation | Evolution, Molecular | Phosphoprotein Phosphatases - chemistry | Protein Subunits - genetics
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2001, Volume 276, Issue 42, pp. 38582 - 38587
Members of the phosphoprotein phosphatase family of serine/threonine phosphatases are thought to exist in different native oligomeric complexes. Protein...
CATALYTIC SUBUNIT | DOMAIN | SERINE/THREONINE PHOSPHATASE | REGULATORY SUBUNITS | NUCLEUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | SERINE THREONINE PHOSPHATASES | IDENTIFICATION | BINDING | FAMILY | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Electrophoresis, Polyacrylamide Gel | Humans | Phosphoprotein Phosphatases - metabolism | Glutathione Transferase - metabolism | Molecular Sequence Data | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Blotting, Western | Precipitin Tests | Point Mutation | Two-Hybrid System Techniques | Gene Deletion | Protein Binding | HeLa Cells | Protein Phosphatase 2 | DNA, Complementary - metabolism | Dimerization | Phosphoprotein Phosphatases - chemistry
CATALYTIC SUBUNIT | DOMAIN | SERINE/THREONINE PHOSPHATASE | REGULATORY SUBUNITS | NUCLEUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | SERINE THREONINE PHOSPHATASES | IDENTIFICATION | BINDING | FAMILY | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Electrophoresis, Polyacrylamide Gel | Humans | Phosphoprotein Phosphatases - metabolism | Glutathione Transferase - metabolism | Molecular Sequence Data | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Blotting, Western | Precipitin Tests | Point Mutation | Two-Hybrid System Techniques | Gene Deletion | Protein Binding | HeLa Cells | Protein Phosphatase 2 | DNA, Complementary - metabolism | Dimerization | Phosphoprotein Phosphatases - chemistry
Journal Article
The Plant Cell, ISSN 1040-4651, 2/2013, Volume 25, Issue 2, pp. 517 - 534
The basic Leucine zipper transcription factor ABSCISIC ACID INSENSITIVE5 (ABI5) is a key regulator of abscisic acid (ABA)-mediated seed germination and...
Proteins | Phosphorylation | Phosphatases | Plant growth regulators | RESEARCH ARTICLES | Germination | Gene expression regulation | Plants | Plant cells | Seedlings | Seed germination | CATALYTIC SUBUNIT | DROUGHT STRESS TOLERANCE | PIN PHOSPHORYLATION | SEED-GERMINATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTISITE PHOSPHORYLATION | ABA RESPONSE LOCI | NEGATIVE REGULATOR | PLANT SCIENCES | CELL BIOLOGY | SERINE/THREONINE PHOSPHATASES | PROTEIN-PROTEIN INTERACTIONS | TRANSCRIPTION FACTOR | Basic-Leucine Zipper Transcription Factors - metabolism | Phosphoprotein Phosphatases - metabolism | Seedlings - genetics | Seedlings - growth & development | Protein Interaction Maps | Arabidopsis Proteins - metabolism | Seeds - growth & development | Germination - genetics | Plants, Genetically Modified | Gene Expression Regulation, Plant | Abscisic Acid - metabolism | Protein Stability | Protein-Serine-Threonine Kinases - metabolism | Arabidopsis Proteins - genetics | Arabidopsis - drug effects | Signal Transduction | Seeds - genetics | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Basic-Leucine Zipper Transcription Factors - genetics | Arabidopsis - metabolism | Arabidopsis - genetics | Abscisic Acid - pharmacology | Phosphoprotein Phosphatases - genetics | Protein Phosphatase 2 - metabolism | Mutation | Transcription factors | Arabidopsis | Cellular signal transduction | Research | Biological control systems | Observations | Properties
Proteins | Phosphorylation | Phosphatases | Plant growth regulators | RESEARCH ARTICLES | Germination | Gene expression regulation | Plants | Plant cells | Seedlings | Seed germination | CATALYTIC SUBUNIT | DROUGHT STRESS TOLERANCE | PIN PHOSPHORYLATION | SEED-GERMINATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MULTISITE PHOSPHORYLATION | ABA RESPONSE LOCI | NEGATIVE REGULATOR | PLANT SCIENCES | CELL BIOLOGY | SERINE/THREONINE PHOSPHATASES | PROTEIN-PROTEIN INTERACTIONS | TRANSCRIPTION FACTOR | Basic-Leucine Zipper Transcription Factors - metabolism | Phosphoprotein Phosphatases - metabolism | Seedlings - genetics | Seedlings - growth & development | Protein Interaction Maps | Arabidopsis Proteins - metabolism | Seeds - growth & development | Germination - genetics | Plants, Genetically Modified | Gene Expression Regulation, Plant | Abscisic Acid - metabolism | Protein Stability | Protein-Serine-Threonine Kinases - metabolism | Arabidopsis Proteins - genetics | Arabidopsis - drug effects | Signal Transduction | Seeds - genetics | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Basic-Leucine Zipper Transcription Factors - genetics | Arabidopsis - metabolism | Arabidopsis - genetics | Abscisic Acid - pharmacology | Phosphoprotein Phosphatases - genetics | Protein Phosphatase 2 - metabolism | Mutation | Transcription factors | Arabidopsis | Cellular signal transduction | Research | Biological control systems | Observations | Properties
Journal Article
Cell, ISSN 0092-8674, 2011, Volume 144, Issue 2, pp. 187 - 199
is a frequently mutated tumor suppressor gene that opposes the PI3K/AKT pathway through dephosphorylation of phosphoinositide-3,4,5-triphosphate. Recently,...
MUTATIONAL SPECTRA | GENOMIC STABILITY | GENE | ANAPHASE-PROMOTING COMPLEX/CYCLOSOME | AURORA KINASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH IN-VIVO | CELLULAR SENESCENCE | CHROMOSOME-10 PTEN | EXPRESSION | SMALL-MOLECULE INHIBITOR | CELL BIOLOGY | Anaphase-Promoting Complex-Cyclosome | Neoplasm Transplantation | PTEN Phosphohydrolase - genetics | Prostatic Neoplasms - metabolism | Prostatic Neoplasms - pathology | Cadherins - metabolism | Humans | PTEN Phosphohydrolase - metabolism | Male | Transplantation, Heterologous | Aurora Kinases | Animals | Cell Nucleus - metabolism | Ubiquitin-Protein Ligase Complexes - metabolism | Cellular Senescence | Cell Line, Tumor | Mice | Phosphoric Monoester Hydrolases - metabolism | Protein-Serine-Threonine Kinases - metabolism | Phosphotransferases | Phosphatases
MUTATIONAL SPECTRA | GENOMIC STABILITY | GENE | ANAPHASE-PROMOTING COMPLEX/CYCLOSOME | AURORA KINASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH IN-VIVO | CELLULAR SENESCENCE | CHROMOSOME-10 PTEN | EXPRESSION | SMALL-MOLECULE INHIBITOR | CELL BIOLOGY | Anaphase-Promoting Complex-Cyclosome | Neoplasm Transplantation | PTEN Phosphohydrolase - genetics | Prostatic Neoplasms - metabolism | Prostatic Neoplasms - pathology | Cadherins - metabolism | Humans | PTEN Phosphohydrolase - metabolism | Male | Transplantation, Heterologous | Aurora Kinases | Animals | Cell Nucleus - metabolism | Ubiquitin-Protein Ligase Complexes - metabolism | Cellular Senescence | Cell Line, Tumor | Mice | Phosphoric Monoester Hydrolases - metabolism | Protein-Serine-Threonine Kinases - metabolism | Phosphotransferases | Phosphatases
Journal Article
The FEBS Journal, ISSN 1742-464X, 01/2013, Volume 280, Issue 2, pp. 324 - 325
This review traces the historical origins and conceptual developments leading to the current state of knowledge of the three superfamilies of protein Ser/Thr...
Nobel prize | phosphorylase kinases | Cori | TCA | glycogen | okadaic acid | phosphorylation | microcystin | CATALYTIC SUBUNIT | MUSCLE MYOSIN PHOSPHATASE | LIGHT-CHAIN PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RABBIT SKELETAL-MUSCLE | PHOSPHORYLASE-PHOSPHATASE | SMALL-T-ANTIGEN | SMOOTH-MUSCLE | AMINO-ACID-SEQUENCE | GLYCOGEN-SYNTHASE PHOSPHATASE | HEART PHOSPHOPROTEIN PHOSPHATASE | Phosphorylation | Y-Box-Binding Protein 1 - metabolism | Signal Transduction | Models, Biological | Humans | Phosphoprotein Phosphatases - metabolism | Protein Phosphatase 2C | Threonine - metabolism | Serine - metabolism | Protein Subunits - metabolism
Nobel prize | phosphorylase kinases | Cori | TCA | glycogen | okadaic acid | phosphorylation | microcystin | CATALYTIC SUBUNIT | MUSCLE MYOSIN PHOSPHATASE | LIGHT-CHAIN PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RABBIT SKELETAL-MUSCLE | PHOSPHORYLASE-PHOSPHATASE | SMALL-T-ANTIGEN | SMOOTH-MUSCLE | AMINO-ACID-SEQUENCE | GLYCOGEN-SYNTHASE PHOSPHATASE | HEART PHOSPHOPROTEIN PHOSPHATASE | Phosphorylation | Y-Box-Binding Protein 1 - metabolism | Signal Transduction | Models, Biological | Humans | Phosphoprotein Phosphatases - metabolism | Protein Phosphatase 2C | Threonine - metabolism | Serine - metabolism | Protein Subunits - metabolism
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2003, Volume 278, Issue 51, pp. 51484 - 51493
Regulation of vascular smooth muscle cell contractile state is critical for the maintenance of blood vessel tone. Abnormal vascular smooth muscle cell...
CA2+ SENSITIZATION | LIGHT-CHAIN PHOSPHATASE | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | FILAMENTOUS ACTIN | PUTATIVE TARGET | SMOOTH-MUSCLE CONTRACTION | CORONARY-ARTERY SPASM | SERINE/THREONINE KINASE | NEOINTIMAL FORMATION | SUBUNIT | Protein Structure, Tertiary | Amino Acid Sequence | Actin Cytoskeleton - metabolism | Humans | Cells, Cultured | rhoA GTP-Binding Protein - metabolism | GTPase-Activating Proteins - chemistry | GTPase-Activating Proteins - metabolism | Muscle, Smooth, Vascular - cytology | Protein Subunits - metabolism | Two-Hybrid System Techniques | Sequence Alignment | Muscle Contraction | Myosin-Light-Chain Phosphatase - metabolism | Myosin-Light-Chain Phosphatase - chemistry | Protein Binding | GTP-Binding Proteins | Binding Sites
CA2+ SENSITIZATION | LIGHT-CHAIN PHOSPHATASE | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | FILAMENTOUS ACTIN | PUTATIVE TARGET | SMOOTH-MUSCLE CONTRACTION | CORONARY-ARTERY SPASM | SERINE/THREONINE KINASE | NEOINTIMAL FORMATION | SUBUNIT | Protein Structure, Tertiary | Amino Acid Sequence | Actin Cytoskeleton - metabolism | Humans | Cells, Cultured | rhoA GTP-Binding Protein - metabolism | GTPase-Activating Proteins - chemistry | GTPase-Activating Proteins - metabolism | Muscle, Smooth, Vascular - cytology | Protein Subunits - metabolism | Two-Hybrid System Techniques | Sequence Alignment | Muscle Contraction | Myosin-Light-Chain Phosphatase - metabolism | Myosin-Light-Chain Phosphatase - chemistry | Protein Binding | GTP-Binding Proteins | Binding Sites
Journal Article
Virology, ISSN 0042-6822, 2007, Volume 366, Issue 1, pp. 126 - 136
Abstract T4 polynucleotide kinase/phosphatase (Pnkp) exemplifies a family of bifunctional enzymes with 5′-kinase and 3′ phosphatase activities that function in...
Infectious Disease | Polynucleotide 3′ phosphatase | End-healing | RNA repair | ACTIVE-SITE | polynucleotide 3 ' phosphatase | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | PHOSPHATASE FCP1 | end-healing | MUTATIONAL ANALYSIS | T4 POLYNUCLEOTIDE KINASE | VIROLOGY | DEOXYRIBONUCLEIC ACID | RNA REPAIR ENZYME | C-TERMINAL DOMAIN | RIBONUCLEIC ACID | Recombinant Proteins - metabolism | Amino Acid Sequence | Polynucleotide 5'-Hydroxyl-Kinase - metabolism | Phosphoric Monoester Hydrolases - genetics | Polynucleotide 5'-Hydroxyl-Kinase - chemistry | Viral Proteins - chemistry | Open Reading Frames | Crystallization | Models, Molecular | Molecular Sequence Data | Mutation, Missense | Viral Proteins - metabolism | Polymerase Chain Reaction | Protein Structure, Quaternary | Bacteriophage T4 - enzymology | Protein Conformation | Kinetics | Polynucleotide 5'-Hydroxyl-Kinase - genetics | Phosphoric Monoester Hydrolases - metabolism | Binding Sites | Amino Acid Substitution | Phosphoric Monoester Hydrolases - chemistry | Glycerol kinase | Analysis | Esterases | CATALYSIS | GLUTAMINE | CRYSTAL STRUCTURE | IONS | national synchrotron light source | FUNCTIONS | NUCLEIC ACIDS | REPAIR | METALS | ENZYMES | MUTATIONS | PHOSPHATASES | ASPARAGINE | SULFATES | STABILIZATION | MATERIALS SCIENCE | DIMERS | PROBES | MERCURY ALLOYS | ALANINES | INTERFACES | ARGININE | PHOSPHOTRANSFERASES | THREONINE | AMIDES | polynucleotide 3′ phosphatase
Infectious Disease | Polynucleotide 3′ phosphatase | End-healing | RNA repair | ACTIVE-SITE | polynucleotide 3 ' phosphatase | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | PHOSPHATASE FCP1 | end-healing | MUTATIONAL ANALYSIS | T4 POLYNUCLEOTIDE KINASE | VIROLOGY | DEOXYRIBONUCLEIC ACID | RNA REPAIR ENZYME | C-TERMINAL DOMAIN | RIBONUCLEIC ACID | Recombinant Proteins - metabolism | Amino Acid Sequence | Polynucleotide 5'-Hydroxyl-Kinase - metabolism | Phosphoric Monoester Hydrolases - genetics | Polynucleotide 5'-Hydroxyl-Kinase - chemistry | Viral Proteins - chemistry | Open Reading Frames | Crystallization | Models, Molecular | Molecular Sequence Data | Mutation, Missense | Viral Proteins - metabolism | Polymerase Chain Reaction | Protein Structure, Quaternary | Bacteriophage T4 - enzymology | Protein Conformation | Kinetics | Polynucleotide 5'-Hydroxyl-Kinase - genetics | Phosphoric Monoester Hydrolases - metabolism | Binding Sites | Amino Acid Substitution | Phosphoric Monoester Hydrolases - chemistry | Glycerol kinase | Analysis | Esterases | CATALYSIS | GLUTAMINE | CRYSTAL STRUCTURE | IONS | national synchrotron light source | FUNCTIONS | NUCLEIC ACIDS | REPAIR | METALS | ENZYMES | MUTATIONS | PHOSPHATASES | ASPARAGINE | SULFATES | STABILIZATION | MATERIALS SCIENCE | DIMERS | PROBES | MERCURY ALLOYS | ALANINES | INTERFACES | ARGININE | PHOSPHOTRANSFERASES | THREONINE | AMIDES | polynucleotide 3′ phosphatase
Journal Article
International Journal of Biochemistry and Cell Biology, ISSN 1357-2725, 2008, Volume 40, Issue 11, pp. 2358 - 2362
Protein phosphatase 5 (PP5) is a unique member of the PPP family of serine/threonine phosphatases based on the presence of tetratricopeptide repeat (TPR)...
Steroid receptor | HSP90 | Chaperone | Glucocorticoid receptor | Phosphoprotein | Protein phosphatase 5 (PP5, Ppp5) | Phosphatase | Tetratricopeptide repeat protein | MAPK | glucocorticoid receptor | phosphoprotein | ACID | SERINE/THREONINE PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | IDENTIFICATION | steroid receptor | HEAT-SHOCK-PROTEIN | NEGATIVE REGULATOR | CELL BIOLOGY | protein phosphatase 5 (PP5, Ppp5) | tetratricopeptide repeat protein | chaperone | PP5 | phosphatase | TETRATRICOPEPTIDE REPEAT DOMAIN | BINDING | EXPRESSION | Protein Structure, Tertiary | Animals | Phosphoprotein Phosphatases - genetics | Isoenzymes - genetics | Isoenzymes - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Nuclear Proteins - metabolism | Receptors, Glucocorticoid - metabolism | Nuclear Proteins - genetics | Ppp5 | Protein phosphatase 5
Steroid receptor | HSP90 | Chaperone | Glucocorticoid receptor | Phosphoprotein | Protein phosphatase 5 (PP5, Ppp5) | Phosphatase | Tetratricopeptide repeat protein | MAPK | glucocorticoid receptor | phosphoprotein | ACID | SERINE/THREONINE PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | IDENTIFICATION | steroid receptor | HEAT-SHOCK-PROTEIN | NEGATIVE REGULATOR | CELL BIOLOGY | protein phosphatase 5 (PP5, Ppp5) | tetratricopeptide repeat protein | chaperone | PP5 | phosphatase | TETRATRICOPEPTIDE REPEAT DOMAIN | BINDING | EXPRESSION | Protein Structure, Tertiary | Animals | Phosphoprotein Phosphatases - genetics | Isoenzymes - genetics | Isoenzymes - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Nuclear Proteins - metabolism | Receptors, Glucocorticoid - metabolism | Nuclear Proteins - genetics | Ppp5 | Protein phosphatase 5
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2014, Volume 289, Issue 40, pp. 27677 - 27691
Background: In Alzheimer brain, I-2(PP2A) is translocated from the neuronal nucleus to the cytoplasm and promotes abnormal hyperphosphorylation of Tau....
Calmodulin-dependent Protein Kinase (CaMK) | CATALYTIC SUBUNIT | SET | MICROTUBULES | Serine | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE BRAIN | CELL-PROLIFERATION | AMYLOID PRECURSOR PROTEIN | Alzheimer Disease | NUCLEAR-LOCALIZATION | Threonine Phosphatase (PSP) | Tau Protein (Tau) | PHOSPHORYLATED-TAU | Ca2 | Protein Serine | DOWN-SYNDROME | NEUROFIBRILLARY DEGENERATION | Threonine Protein Kinase | Phosphorylation | Histone Chaperones - genetics | Humans | Protein Phosphatase 2 - genetics | Histone Chaperones - metabolism | tau Proteins - metabolism | Cytoplasm - metabolism | Glycogen Synthase Kinase 3 beta | Transcription Factors - genetics | Glycogen Synthase Kinase 3 - metabolism | Nuclear Localization Signals | Brain - metabolism | Transcription Factors - metabolism | Cell Nucleus - metabolism | tau Proteins - genetics | Glycogen Synthase Kinase 3 - genetics | Alzheimer Disease - metabolism | Protein Phosphatase 2 - metabolism | Cytoplasm - genetics | Alzheimer Disease - genetics | Neurobiology
Calmodulin-dependent Protein Kinase (CaMK) | CATALYTIC SUBUNIT | SET | MICROTUBULES | Serine | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE BRAIN | CELL-PROLIFERATION | AMYLOID PRECURSOR PROTEIN | Alzheimer Disease | NUCLEAR-LOCALIZATION | Threonine Phosphatase (PSP) | Tau Protein (Tau) | PHOSPHORYLATED-TAU | Ca2 | Protein Serine | DOWN-SYNDROME | NEUROFIBRILLARY DEGENERATION | Threonine Protein Kinase | Phosphorylation | Histone Chaperones - genetics | Humans | Protein Phosphatase 2 - genetics | Histone Chaperones - metabolism | tau Proteins - metabolism | Cytoplasm - metabolism | Glycogen Synthase Kinase 3 beta | Transcription Factors - genetics | Glycogen Synthase Kinase 3 - metabolism | Nuclear Localization Signals | Brain - metabolism | Transcription Factors - metabolism | Cell Nucleus - metabolism | tau Proteins - genetics | Glycogen Synthase Kinase 3 - genetics | Alzheimer Disease - metabolism | Protein Phosphatase 2 - metabolism | Cytoplasm - genetics | Alzheimer Disease - genetics | Neurobiology
Journal Article
Science, ISSN 0036-8075, 5/2010, Volume 328, Issue 5981, pp. 1043 - 1046
The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and...
Datasets | Research fellowships | Yeasts | Protein metabolism | Phosphatases | Cellular metabolism | REPORTS | Cell cycle | Research grants | Proteomes | Nitrogen | MITOSIS | SIGNAL | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | TRANSDUCTION | CELL-CYCLE | SACCHAROMYCES-CEREVISIAE | FEEDBACK | PROTEOMICS | Protein Kinases - metabolism | Carbon - metabolism | Nitrogen - metabolism | Phosphorylation | Signal Transduction | Phosphoprotein Phosphatases - metabolism | Cell Cycle Proteins - metabolism | Protein Tyrosine Phosphatases - metabolism | Proteome | Protein Subunits - metabolism | MAP Kinase Signaling System | Protein Interaction Mapping | Saccharomyces cerevisiae - metabolism | Metabolic Networks and Pathways | Models, Biological | Mass Spectrometry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | DNA Damage | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Physiological aspects | Genetic aspects | Research | Yeast fungi | Protein kinases | Proteins | Enzymes | Yeast | Microbiology | Kinases
Datasets | Research fellowships | Yeasts | Protein metabolism | Phosphatases | Cellular metabolism | REPORTS | Cell cycle | Research grants | Proteomes | Nitrogen | MITOSIS | SIGNAL | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | TRANSDUCTION | CELL-CYCLE | SACCHAROMYCES-CEREVISIAE | FEEDBACK | PROTEOMICS | Protein Kinases - metabolism | Carbon - metabolism | Nitrogen - metabolism | Phosphorylation | Signal Transduction | Phosphoprotein Phosphatases - metabolism | Cell Cycle Proteins - metabolism | Protein Tyrosine Phosphatases - metabolism | Proteome | Protein Subunits - metabolism | MAP Kinase Signaling System | Protein Interaction Mapping | Saccharomyces cerevisiae - metabolism | Metabolic Networks and Pathways | Models, Biological | Mass Spectrometry | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | DNA Damage | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Physiological aspects | Genetic aspects | Research | Yeast fungi | Protein kinases | Proteins | Enzymes | Yeast | Microbiology | Kinases
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
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