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Biochemical Journal, ISSN 0264-6021, 12/2007, Volume 408, Issue 3, pp. 297 - 315
The specificities of 65 compounds reported to be relatively specific inhibitors of protein kinases have been profiled against a panel of 70-80 protein kinases.... 
Drug discovery | Kinase profiling | Protein kinase | Anti-cancer drugs | Inhibitor specificity | RHO-ASSOCIATED KINASE | TUMOR PROGRESSION | FAMILY-MEMBERS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-PROLIFERATION | protein kinase | P38 MAP KINASE | CYCLIN-DEPENDENT KINASES | RECEPTOR TYROSINE KINASES | drug discovery | kinase profiling | SB 203580 | anti-cancer drugs | ISOFORMS IN-VITRO | P90 RSK | inhibitor specificity | Amino Acid Sequence | Cell Line | Phosphorylation | Recombinant Proteins - antagonists & inhibitors | Animals | Mitogen-Activated Protein Kinases - antagonists & inhibitors | Humans | Drug Design | Protein Kinase Inhibitors - pharmacology | Enzyme Activation | Mitogen-Activated Protein Kinases - metabolism | Spodoptera | Index Medicus | Yes1, Yamaguchi sarcoma viral oncogene homologue 1 | CSK, C-terminal Src kinase | Lck, lymphocyte cell-specific protein-tyrosine kinase | EGF, epidermal growth factor | FGF-R, fibroblast-growth-factor receptor | PAK, p21-activated protein kinase | PDK, 3-phosphoinositide-dependent protein kinase | PI3K, phosphatidylinositol (phosphoinositide) 3-kinase | NEK, NIMA (never in mitosis in Aspergillus nidulans)-related kinase | RSK, p90 ribosomal S6 kinase | HEK-293 cells, human embryonic kidney-293 cells | VEGF, vascular endothelial growth factor (vasoendothelial growth factor) | EF2K, elongation-factor-2 kinase | CK, casein kinase | PTEN, phosphatase and tensin homologue deleted on chromosome 10 | ERK, extracellular-signal-regulated kinase | ATM, ataxia telangiectasia mutated | SRPK, serine-arginine protein kinase | IL-1, interleukin 1 | MNK, MAPK-integrating protein kinase | ROCK, Rho-dependent protein kinase | CaMKK, CaMK kinase | GST, glutathione transferase | MKK1, MAPK kinase-1 (also called MEK1, MAPK or ERK kinase 1) | GAK, cyclin G-associated kinase | FMK, fluoromethylketone | MST, mammalian homologue Ste20-like kinase | PKA, cAMP-dependent protein kinase | FKBP, FK506-binding protein | PPAR, peroxisome-proliferator-activated receptor | IKK, inhibitory κB kinase | PH, pleckstrin homology | MBP, myelin basic protein | AICAR, aminoimidazole-4-carboxamide-1-β-D-ribofuranoside | MAPKAP-K, MAPK-activated protein kinase | Sf21, Spodoptera frugiperda (fall armyworm) 21 | MARK, microtubule-affinity-regulating kinase | PIM, provirus integration site for Moloney murine leukaemia virus | LPS, lipopolysaccharide | MSK, mitogen- and stress-activated protein kinase | MAPK, mitogen-activated protein kinase | MELK, maternal embryonic leucine-zipper kinase | His6, hexahistidine | CAK, cyclin-dependent kinase-activating kinase | Eph-A2, Ephrin A2 receptor | PLK, polo-like kinase | ATF2, activating transcription factor 2 | PKD, protein kinase D | Src, sarcoma kinase | AMPK, AMP-activated protein kinase | MMS, methyl methanesulfonate | CHK, checkpoint kinase | JNK, c-Jun N-terminal kinase | TORC1, mTOR (mammalian target of rapamycin)–raptor (regulatory associated protein of mTOR) complex | BRSK, brain-specific kinase | RIP2, receptor-interacting protein 2 | IGF-1, insulin-like growth factor-1 | S6K1, S6 kinase 1 | DYRK, dual-specificity tyrosine-phosphorylated and -regulated kinase | HIPK, homeodomain-interacting protein kinase | ZMP, aminoimidazole-4-carboxamide-1-β-D-ribofuranoside monophosphate | PRAK, p38-regulated activated kinase | PKC, protein kinase C | Src-I1, Src inhibitor 1 | TANK, TRAF (tumour-necrosis-factor-receptor-associated factor)-family-member-associated nuclear factor κB activator | NFAT, nuclear factor for activated T-cells | PHK, phosphorylase kinase | GSK3, glycogen synthase kinase 3 | PKB, protein kinase B (also called Akt) | CaMK, calmodulin-dependent kinase | CDK, cyclin-dependent protein kinase | NDRG, N-myc downstream-regulated gene | SmMLCK, smooth-muscle myosin light-chain kinase | TBK1, TANK-binding kinase 1 | PRK, protein kinase C-related kinase | SGK, serum- and glucocorticoid-induced kinase
Journal Article
Cell, ISSN 0092-8674, 2008, Volume 133, Issue 6, pp. 963 - 977
Journal Article
Nature Neuroscience, ISSN 1097-6256, 07/2003, Volume 6, Issue 7, pp. 708 - 716
Neurexins are a large family of proteins that act as neuronal cell-surface receptors. The function and localization of the various neurexins, however, have not... 
TRANSMEMBRANE LIGANDS | ALPHA-LATROTOXIN RECEPTORS | PROTEIN | ADHESION MOLECULE | EPH RECEPTORS | ACETYLCHOLINESTERASE | PHOSPHORYLATION | SYNAPSE | CELL-ADHESION | NEUROLIGIN-1 | NEUROSCIENCES | Membrane Glycoproteins - metabolism | Humans | RNA Replicase - metabolism | Cell Communication - physiology | Synapses - genetics | PC12 Cells | Viral Proteins - metabolism | Choline O-Acetyltransferase - metabolism | Immunomagnetic Separation - methods | Mutation - physiology | Time Factors | Membrane Proteins - physiology | Binding Sites | Cell Aggregation - genetics | Receptors, AMPA - metabolism | Animals, Newborn | Membrane Proteins - genetics | R-SNARE Proteins | Rats | Recombinant Proteins - chemistry | Blotting, Western | Chickens | Cerebellum - cytology | Choline O-Acetyltransferase - chemistry | Mice | RNA Replicase - immunology | Synaptic Vesicles - metabolism | Viral Proteins - immunology | Structure-Activity Relationship | Cerebellum - physiology | Cell Aggregation - physiology | Kidney | Cell Adhesion Molecules, Neuronal | Nerve Tissue Proteins - chemistry | Transfection - methods | Alanine - genetics | Female | Membrane Proteins - metabolism | Cell Differentiation - physiology | Nerve Tissue Proteins - physiology | Calcium-Binding Proteins | Nerve Tissue Proteins - immunology | Presynaptic Terminals - drug effects | Synapses - physiology | Cells, Cultured | Presynaptic Terminals - physiology | Nerve Tissue Proteins - genetics | Proto-Oncogene Proteins c-myc - metabolism | Nerve Tissue Proteins - metabolism | Hippocampus - metabolism | Animals | Membrane Proteins - chemistry | Synaptotagmins | Pons - metabolism | Structural Homology, Protein | Lipid Bilayers - metabolism | Physiological aspects | Neural transmission | Research | Nerve proteins | Synapses | Index Medicus
Journal Article
Genes and Development, ISSN 0890-9369, 01/1999, Volume 13, Issue 2, pp. 163 - 175
MAP kinases phosphorylate specific groups of substrate proteins. Here we show that the amino acid sequence FXFP is an evolutionarily conserved docking site... 
ETS transcription factor | MAP kinase | KSR | JNK | ERK | TRANSCRIPTION FACTORS | ACTIVATION DOMAIN | KSR-1 GENE ENCODES | DEVELOPMENTAL BIOLOGY | TERNARY COMPLEX FACTORS | SIGNAL-TRANSDUCTION | OOCYTE MATURATION | HIGH-AFFINITY INTERACTION | GENETICS & HEREDITY | DELTA-DOMAIN | XENOPUS OOCYTES | C-JUN | Conserved Sequence - genetics | Protein Kinases - genetics | Receptors, Eph Family | Transcription Factors - chemistry | MAP Kinase Kinase 4 | Peptides - metabolism | Oocytes - drug effects | Binding Sites | Amino Acid Sequence | Calcium-Calmodulin-Dependent Protein Kinases - genetics | Enzyme Inhibitors - metabolism | Caenorhabditis elegans - genetics | Enzyme Inhibitors - pharmacology | Recombinant Fusion Proteins - chemistry | Receptor Protein-Tyrosine Kinases - metabolism | Recombinant Fusion Proteins - genetics | Mice | Mutation | 3T3 Cells | Caenorhabditis elegans - enzymology | Receptor Protein-Tyrosine Kinases - chemistry | Protein Kinases - metabolism | Phosphorylation | Conserved Sequence - physiology | Molecular Sequence Data | Protein Kinases - chemistry | Substrate Specificity | Proto-Oncogene Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Oocytes - enzymology | Mitogen-Activated Protein Kinase Kinases | JNK Mitogen-Activated Protein Kinases | Proto-Oncogene Proteins c-ets | Proto-Oncogene Proteins - metabolism | Receptor, EphB4 | Caenorhabditis elegans Proteins | Oocytes - growth & development | Xenopus laevis | Proto-Oncogene Proteins - genetics | Transcription Factors - genetics | Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors | Peptides - pharmacology | Transcription Factors - metabolism | Animals | Proteins - metabolism | Receptor Protein-Tyrosine Kinases - genetics | Proteins - chemistry | Mitogen-Activated Protein Kinase 1 | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Evolution | Research | Genetic regulation | Observations | Protein kinases | Protein binding | Index Medicus | Research Paper
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2011, Volume 6, Issue 11, pp. e27072 - e27072
Journal Article
PROTEOMICS, ISSN 1615-9853, 12/2011, Volume 11, Issue 23, pp. 4514 - 4528
Journal Article
by Peifer, Martin and Fernández-Cuesta, Lynnette and Sos, Martin L and George, Julie and Seidel, Danila and Kasper, Lawryn H and Plenker, Dennis and Leenders, Frauke and Sun, Ruping and Zander, Thomas and Menon, Roopika and Koker, Mirjam and Dahmen, Ilona and Müller, Christian and Di Cerbo, Vincenzo and Schildhaus, Hans-Ulrich and Altmüller, Janine and Baessmann, Ingelore and Becker, Christian and De Wilde, Bram and Vandesompele, Jo and Böhm, Diana and Ansén, Sascha and Gabler, Franziska and Wilkening, Ines and Heynck, Stefanie and Heuckmann, Johannes M and Lu, Xin and Carter, Scott L and Cibulskis, Kristian and Banerji, Shantanu and Getz, Gad and Park, Kwon-Sik and Rauh, Daniel and Grütter, Christian and Fischer, Matthias and Pasqualucci, Laura and Wright, Gavin and Wainer, Zoe and Russell, Prudence and Petersen, Iver and Chen, Yuan and Stoelben, Erich and Ludwig, Corinna and Schnabel, Philipp and Hoffmann, Hans and Muley, Thomas and Brockmann, Michael and Engel-Riedel, Walburga and Muscarella, Lucia A and Fazio, Vito M and Groen, Harry and Timens, Wim and Sietsma, Hannie and Thunnissen, Erik and Smit, Egber and Heideman, Daniëlle A. M and Snijders, Peter J. F and Cappuzzo, Federico and Ligorio, Claudia and Damiani, Stefania and Field, John and Solberg, Steinar and Brustugun, Odd Terje and Lund-Iversen, Marius and Sänger, Jörg and Clement, Joachim H and Soltermann, Alex and Moch, Holger and Weder, Walter and Solomon, Benjamin and Soria, Jean-Charles and Validire, Pierre and Besse, Benjamin and Brambilla, Elisabeth and Brambilla, Christian and Lantuejoul, Sylvie and Lorimier, Philippe and Schneider, Peter M and Hallek, Michael and Pao, William and Meyerson, Matthew and Sage, Julien and Shendure, Jay and Schneider, Robert and Büttner, Reinhard and Wolf, Jürgen and Nürnberg, Peter and Perner, Sven and Heukamp, Lukas C and Brindle, Paul K and Haas, Stefan and Thomas, Roman K
Nature Genetics, ISSN 1061-4036, 10/2012, Volume 44, Issue 10, pp. 1104 - 1110
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Journal Article