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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
American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 06/2009, Volume 296, Issue 6, pp. 1258 - 1270
Myostatin is a negative regulator of skeletal muscle size, previously shown to inhibit muscle cell differentiation. Myostatin requires both Smad2 and Smad3... 
MAFbx | Mammalian target of rapamycin complex signaling | MuRF1 | S6 kinase | Smad signaling | Human skeletal muscle cells | Transducer of regulated Ca | responsive element-binding protein activity | MuRF-1 | Atrogin | Transforming growth factor-β-like molecules | IGF-I | PHYSIOLOGY | ATROPHY | RAPID DISUSE | human skeletal muscle cells | transforming growth factor-beta-like molecules | SKELETAL-MUSCLE HYPERTROPHY | FOXO TRANSCRIPTION FACTORS | UBIQUITIN LIGASES | transducer of regulated Ca2+-responsive element-binding protein activity | CELL BIOLOGY | atrogin | PATHWAY | GROWTH | GENE-EXPRESSION | mammalian target of rapamycin complex signaling | CONDITIONAL ACTIVATION | Activin Receptors, Type I - antagonists & inhibitors | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Humans | Smad3 Protein - metabolism | Muscle Fibers, Skeletal - drug effects | Tripartite Motif Proteins | Smad3 Protein - genetics | Transfection | RNA Interference | Myoblasts, Skeletal - pathology | Smad2 Protein - genetics | Muscle Proteins - metabolism | Dioxoles - pharmacology | Regulatory-Associated Protein of mTOR | Benzamides - pharmacology | Myostatin - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Rapamycin-Insensitive Companion of mTOR Protein | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Signal Transduction | Cell Size - drug effects | Cells, Cultured | Smad2 Protein - metabolism | Ubiquitin-Protein Ligases - metabolism | Organ Size | Activin Receptors, Type I - metabolism | Myoblasts, Skeletal - enzymology | SKP Cullin F-Box Protein Ligases - metabolism | Mice, SCID | Myostatin - antagonists & inhibitors | Adaptor Proteins, Signal Transducing | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Cell Differentiation - drug effects | Follistatin - pharmacology | Muscle Fibers, Skeletal - pathology | Creatine Kinase - metabolism | Mice | Protein Kinase Inhibitors - pharmacology | TOR Serine-Threonine Kinases | Myoblasts, Skeletal - drug effects | Insulin-Like Growth Factor I - metabolism | Muscle Fibers, Skeletal - enzymology | RNA, Small Interfering - metabolism | Abdominal surgery | Musculoskeletal system | Signal transduction | Cell growth | Kinases | Gene expression | Cells | Index Medicus
Journal Article
Science, ISSN 0036-8075, 12/2010, Volume 330, Issue 6009, pp. 1390 - 1393
Although the proteins BAX and BAK are required for initiation of apoptosis at the mitochondria, how BAX and BAK are activated remains unsettled. We provide in... 
T lymphocytes | Mitochondria | Cytokines | Thymocytes | Neurons | Cell death | REPORTS | Cytochromes | Mice | Potassium | Apoptosis | NEURONAL APOPTOSIS | CYTOCHROME-C | MITOCHONDRIAL APOPTOSIS | MECHANISM | MULTIDISCIPLINARY SCIENCES | BH3 DOMAINS | RELEASE | JNK PATHWAY | PROTEINS | BCL-2 FAMILY-MEMBERS | MEMBRANE PERMEABILIZATION | BH3 Interacting Domain Death Agonist Protein - deficiency | T-Lymphocytes - physiology | bcl-2-Associated X Protein - chemistry | Protein Multimerization | Stress, Physiological | bcl-2 Homologous Antagonist-Killer Protein - genetics | BH3 Interacting Domain Death Agonist Protein - genetics | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Membrane Proteins - deficiency | Caspases - metabolism | Bcl-2-Like Protein 11 | Apoptosis Regulatory Proteins - deficiency | Tumor Suppressor Proteins - deficiency | Tumor Suppressor Proteins - genetics | Neurons - physiology | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | bcl-2-Associated X Protein - genetics | Proto-Oncogene Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Permeability | Proto-Oncogene Proteins - deficiency | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Models, Biological | Cerebellum - cytology | Intracellular Membranes - metabolism | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Protein research | Genetic aspects | Mitochondrial DNA | Biochemical genetics | Research | Properties | Methods | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 11/2009, Volume 36, Issue 3, pp. 487 - 499
While activation of BAX/BAK by BH3-only molecules (BH3s) is essential for mitochondrial apoptosis, the underlying mechanisms remain unsettled. Here we... 
CELLCYCLE | CYTOCHROME-C | PROAPOPTOTIC BAX | OLIGOMERIZES BAK | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOPLASMIC-RETICULUM | SUBCELLULAR LOCATION | PROTEINS | BCL-2 FAMILY-MEMBERS | BH3 DOMAIN | CELL-DEATH | MEMBRANE PERMEABILIZATION | CELL BIOLOGY | bcl-2-Associated X Protein - chemistry | Immunoprecipitation | Apoptosis - drug effects | Protein Multimerization | bcl-2 Homologous Antagonist-Killer Protein - genetics | Immunoblotting | BH3 Interacting Domain Death Agonist Protein - genetics | Green Fluorescent Proteins - genetics | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Bcl-2-Like Protein 11 | Protein Binding - drug effects | Tumor Suppressor Proteins - genetics | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | bcl-2-Associated X Protein - genetics | Fibroblasts - metabolism | Proto-Oncogene Proteins - metabolism | Green Fluorescent Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Etoposide - pharmacology | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Models, Biological | Tunicamycin - pharmacology | Fibroblasts - drug effects | Thapsigargin - pharmacology | Fibroblasts - cytology | Mice | Mutation | Microscopy, Fluorescence | Staurosporine - pharmacology | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Monomers | Apoptosis | Oligomers | Index Medicus
Journal Article
The Plant Cell, ISSN 1040-4651, 5/2007, Volume 19, Issue 5, pp. 1617 - 1634
Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal and environmental cues, including auxin, blue... 
Proteins | 14-3-3 proteins | Yeasts | Phosphorylation | Plant roots | pH | Cell membranes | Plants | Seedlings | Plant cells | CELLS | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BLUE-LIGHT | PLANT SCIENCES | CELL BIOLOGY | ION FLUXES | PLANT SALT TOLERANCE | C-TERMINAL REGION | CALCIUM | STRESS SIGNAL-TRANSDUCTION | BINDING-SITE | REGULATORY DOMAIN | Protons | Gene Expression Regulation, Enzymologic - drug effects | Arabidopsis - enzymology | Adaptation, Physiological - drug effects | Molecular Sequence Data | DNA, Bacterial | Plant Roots - drug effects | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | RNA Interference | Protein Binding - drug effects | Ethyl Methanesulfonate | Proton-Translocating ATPases - antagonists & inhibitors | Cell Membrane - drug effects | Protein-Serine-Threonine Kinases - metabolism | Membrane Potentials - drug effects | Amino Acid Sequence | Arabidopsis Proteins - genetics | Arabidopsis - drug effects | Plant Roots - metabolism | Arabidopsis - cytology | Protein-Serine-Threonine Kinases - genetics | Down-Regulation - drug effects | Mutation - genetics | Phosphoserine - metabolism | Proton-Translocating ATPases - chemistry | 14-3-3 Proteins - metabolism | Arabidopsis - genetics | Cell Membrane - enzymology | Gene Expression Regulation, Plant - drug effects | Arabidopsis Proteins - chemistry | Calcium Signaling - drug effects | Alleles | Plant Growth Regulators - pharmacology | Arabidopsis Proteins - antagonists & inhibitors | Hydrogen-Ion Concentration | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 11, pp. e15394 - e15394
Autophagy is a highly orchestrated intracellular bulk degradation process that is activated by various environmental stresses. The serine/threonine kinase... 
COMPLEX | ACTIVATED PROTEIN-KINASE | METABOLISM | PHOSPHORYLATION | MACHINERY | BIOLOGY | INHIBITS CELL-GROWTH | INDUCTION | SACCHAROMYCES-CEREVISIAE | ATG13 | DEGENERATION | AMP-Activated Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | Multiprotein Complexes | Immunoblotting | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Protein Subunits - metabolism | Autophagy-Related Protein-1 Homolog | Mechanistic Target of Rapamycin Complex 1 | Transfection | RNA Interference | HEK293 Cells | Regulatory-Associated Protein of mTOR | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Protein Subunits - genetics | Cell Line | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Mice, Knockout | 14-3-3 Proteins - metabolism | Proteins - genetics | Animals | Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Cell Line, Tumor | Protein Binding | Mice | TOR Serine-Threonine Kinases | Mutation | Adaptor Proteins, Signal Transducing - metabolism | AMP-Activated Protein Kinases - genetics | Microscopy, Fluorescence | TOR protein | Yeast | Homology | Kinases | Inactivation | Proteins | Cell growth | Cell cycle | Binding | Biodegradation | Deactivation | Threonine | Pharmacology | Metabolism | Mammals | Environmental stress | Medicine | TSC2 protein | 14-3-3 protein | Insects | Environmental degradation | Protein-serine/threonine kinase | Regulation | Phagocytosis | Cancer | Apoptosis | Index Medicus
Journal Article
Science, ISSN 0036-8075, 2/2007, Volume 315, Issue 5813, pp. 856 - 859
A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only members initiate apoptosis by directly binding to the essential... 
Research fellowships | Protein isoforms | Medical research | Myeloid cells | Antibodies | Cytochromes | Ligands | Reports | Grants | Viability | Apoptosis | RESPONSES | FAMILY-MEMBERS | X-L | MULTIDISCIPLINARY SCIENCES | BIM | HELIX | MITOCHONDRIAL-MEMBRANE | PUMA | DOMAINS | BH3-ONLY PROTEINS | CELL-DEATH | bcl-2-Associated X Protein - chemistry | Humans | BH3 Interacting Domain Death Agonist Protein - genetics | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Tumor Suppressor Proteins - genetics | BH3 Interacting Domain Death Agonist Protein - chemistry | Apoptosis Regulatory Proteins - genetics | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Mice | Mutation | bcl-X Protein - metabolism | Research | Peptides | Analysis | Biochemistry | Cellular biology | Molecular biology | Binding sites | Index Medicus
Journal Article
1990, ISBN 0123774500, xvii, 651
Book
2004, Methods in molecular biology, ISBN 1588291375, Volume 237, xii, 249
G proteins and G protein-coupled receptors are ubiquitously expressed proteins that regulate a wide range of physiological processes and are consequently the... 
Cellular signal transduction | G proteins | Laboratory manuals | Cytology | Cell Biology | Life Sciences
Book