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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
2004, ISBN 9780306479922, x· 235
Book
Science, ISSN 0036-8075, 1/2009, Volume 323, Issue 5911, pp. 269 - 272
The Vibrio parahaemolyticus type III effector VopS is implicated in cell rounding and the collapse of the actin cytoskeleton by inhibiting Rho guanosine... 
Proteins | Phosphates | Enzymes | HeLa cells | Amino acids | Ions | Mass spectroscopy | Reports | Infections | Biochemistry | Post translational modification | ACTIVATION | PROTEIN | PARAHAEMOLYTICUS | MULTIDISCIPLINARY SCIENCES | III SECRETION SYSTEM | Phosphorylation | Threonine - chemistry | rho GTP-Binding Proteins - antagonists & inhibitors | Humans | Bacterial Proteins - chemistry | Molecular Sequence Data | rac GTP-Binding Proteins - metabolism | Vibrio parahaemolyticus - metabolism | cdc42 GTP-Binding Protein - metabolism | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | rac GTP-Binding Proteins - antagonists & inhibitors | Cell Shape | cdc42 GTP-Binding Protein - antagonists & inhibitors | rho GTP-Binding Proteins - chemistry | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | Signal Transduction | Adenosine Monophosphate - metabolism | Bacterial Proteins - genetics | Mutant Proteins - metabolism | Vibrio parahaemolyticus - pathogenicity | Amino Acid Motifs | Mutant Proteins - chemistry | rho GTP-Binding Proteins - metabolism | rac GTP-Binding Proteins - chemistry | Bacterial Proteins - metabolism | cdc42 GTP-Binding Protein - chemistry | Protein Processing, Post-Translational | HeLa Cells | Genetic aspects | Chemical properties | Guanosine triphosphatase | Vibrio | Signal transduction | Eukaryotes | Cellular biology | Molecular biology | Binding sites | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 28, pp. 25065 - 25075
Cerebral cavernous malformations (CCMs) are alterations in brain capillary architecture that can result in neurological deficits, seizures, or stroke. We... 
CEREBRAL CAVERNOUS MALFORMATIONS | STRIATIN FAMILY | PHOSPHATASE 2A | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | VASCULAR INTEGRITY | KINASE | RHO GTPASES | CELL-GROWTH | SACCHAROMYCES-CEREVISIAE | GENOME-SCALE | Protein Phosphatase 2 - chemistry | Humans | Multiprotein Complexes - genetics | Proto-Oncogene Proteins - chemistry | Structure-Activity Relationship | Multiprotein Complexes - metabolism | Nerve Tissue Proteins - chemistry | HEK293 Cells | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Golgi Apparatus - chemistry | Protein-Serine-Threonine Kinases - metabolism | Calmodulin-Binding Proteins - genetics | Proto-Oncogene Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | Nerve Tissue Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Nerve Tissue Proteins - metabolism | Multiprotein Complexes - chemistry | Animals | Membrane Proteins - chemistry | Protein Phosphatase 2 - metabolism | Golgi Apparatus - metabolism | Mice | Protein-Serine-Threonine Kinases - chemistry | HeLa Cells | Golgi Apparatus - genetics | Index Medicus | MST4 | Striatin | Signal Transduction | Mass Spectrometry (MS) | Golgi | PP2A | Serine Threonine Protein Phosphatase | Serine Threonine Protein Kinase | Cerebral Cavernous Malformations | Protein-Protein Interactions
Journal Article
Nature Cell Biology, ISSN 1465-7392, 01/2015, Volume 17, Issue 1, pp. 68 - 80
The contractile actomyosin cytoskeleton and its connection to the plasma membrane are critical for control of cell shape and migration. We identify three... 
MATRIX | BORDER CELLS | INVASION | COMPLEX | IN-VIVO | PROTEIN PHOSPHATASE 2A | POLARIZATION | MYOSIN PHOSPHATASE | MICROARRAY DATA | DROSOPHILA | CELL BIOLOGY | Phosphorylation | Autoantigens - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Autoantigens - genetics | Cell Movement - genetics | Neoplasm Metastasis | RNA Interference | rho-Associated Kinases - metabolism | Apoptosis Regulatory Proteins - genetics | Cytoskeletal Proteins - metabolism | Female | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Calmodulin-Binding Proteins - genetics | Actin Cytoskeleton - metabolism | Signal Transduction | Membrane Proteins - genetics | Computational Biology | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - metabolism | Actomyosin - metabolism | Protein-Serine-Threonine Kinases - biosynthesis | Carrier Proteins - genetics | Protein Phosphatase 1 - metabolism | Animals | Breast Neoplasms - genetics | Carrier Proteins - metabolism | Breast Neoplasms - pathology | Protein Phosphatase 2 - metabolism | Cell Line, Tumor | RNA, Small Interfering | Drosophila melanogaster | Metastasis | Muscle proteins | Health aspects | Phosphotransferases | Analysis | Cancer cells | Index Medicus | Cytoskeletal Proteins | Medical and Health Sciences | Medicin och hälsovetenskap | Protein-Serine-Threonine Kinases | Breast Neoplasms | Klinisk medicin | Calmodulin-Binding Proteins | Journal Article | rho-Associated Kinases | Proto-Oncogene Proteins | Protein Phosphatase 2 | Protein Phosphatase 1 | Carrier Proteins | Phosphoprotein Phosphatases | Actin Cytoskeleton | Actomyosin | Autoantigens | Membrane Proteins | Clinical Medicine | Apoptosis Regulatory Proteins | Microfilament Proteins | Research Support, Non-U.S. Gov't | Cancer and Oncology | Cell Movement | Cancer och onkologi
Journal Article
Cell Death and Differentiation, ISSN 1350-9047, 01/2014, Volume 21, Issue 1, pp. 79 - 91
The immunogenic demise of cancer cells can be induced by various chemotherapeutics, such as anthracyclines and oxaliplatin, and provokes an immune response... 
quinacrine | apoptosis | U2OS cells | caspases | endoplasmic reticulum stress | Beclin 1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | RELEASE | AUTOPHAGY | CLEAVAGE | CHEMOTHERAPY | CELL BIOLOGY | CALRETICULIN EXPOSURE | PANNEXIN 1 | ASSAYS | FIND-ME SIGNAL | Connexins - antagonists & inhibitors | RNA-Binding Proteins - genetics | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cell Death - immunology | rho-Associated Kinases - antagonists & inhibitors | Antineoplastic Agents - toxicity | DNA-Binding Proteins - metabolism | Lysosomes - metabolism | Lysosomal-Associated Membrane Protein 1 - genetics | Myosin Type II - metabolism | RNA Interference | rho-Associated Kinases - metabolism | Adenosine Triphosphate - metabolism | HMGB1 Protein - metabolism | Cell Membrane - metabolism | Cell Death - drug effects | RNA-Binding Proteins - antagonists & inhibitors | Nerve Tissue Proteins - antagonists & inhibitors | DNA-Binding Proteins - antagonists & inhibitors | Connexins - genetics | rho-Associated Kinases - genetics | Lysosomal-Associated Membrane Protein 1 - antagonists & inhibitors | Microtubule-Associated Proteins - antagonists & inhibitors | DNA-Binding Proteins - genetics | Nerve Tissue Proteins - genetics | Connexins - metabolism | Nerve Tissue Proteins - metabolism | Animals | Autophagy-Related Protein 5 | Cell Line, Tumor | Lysosomal-Associated Membrane Protein 1 - metabolism | Mice | RNA-Binding Proteins - metabolism | RNA, Small Interfering - metabolism | Index Medicus | Original Paper
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2016, Volume 291, Issue 9, pp. 4323 - 4333
Invadosomes are actin-rich membrane protrusions that degrade the extracellular matrix to drive tumor cell invasion. Key players in invadosome formation are... 
Receptors, Lysophosphatidic Acid - metabolism | Lysophospholipids - metabolism | Receptors, G-Protein-Coupled - metabolism | Humans | Extracellular Matrix - metabolism | Melanoma - enzymology | Podosomes - enzymology | Neoplasm Proteins - antagonists & inhibitors | Receptors, Lysophosphatidic Acid - agonists | Receptors, Lysophosphatidic Acid - genetics | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - genetics | Endothelins - metabolism | Neoplasm Proteins - metabolism | Time-Lapse Imaging | Podosomes - metabolism | RNA Interference | cdc42 GTP-Binding Protein - antagonists & inhibitors | Fluorescence Resonance Energy Transfer | Receptors, Lysophosphatidic Acid - antagonists & inhibitors | Neoplasm Proteins - genetics | Biomarkers - metabolism | Melanoma - metabolism | Recombinant Proteins - metabolism | rac1 GTP-Binding Protein - agonists | rhoA GTP-Binding Protein - antagonists & inhibitors | Recombinant Proteins - genetics | Melanoma - pathology | cdc42 GTP-Binding Protein - agonists | Hydrolysis | Podosomes - pathology | Microscopy, Confocal | Neoplasm Proteins - agonists | cdc42 GTP-Binding Protein - genetics | Receptors, G-Protein-Coupled - antagonists & inhibitors | rac1 GTP-Binding Protein - antagonists & inhibitors | Cell Line, Tumor | Luminescent Proteins - genetics | Receptors, G-Protein-Coupled - genetics | Extracellular Matrix - pathology | Microscopy, Fluorescence | rac1 GTP-Binding Protein - metabolism | Luminescent Proteins - metabolism | rac1 GTP-Binding Protein - genetics | Index Medicus | CDC42 | invadopodia | biosensor | fluorescence resonance energy transfer (FRET) | calcium intracellular release | G protein-coupled receptor (GPCR) | Rho (Rho GTPase) | phosphatidylinositide 3-kinase (PI 3-kinase) | imaging | Rac (Rac GTPase) | Cell Biology
Journal Article
Journal Article
2005, Proteins and cell regulation, ISBN 978140203461X, Volume 3., xiii, 296
Humans contain more than 20 Rho type GTPases. This volume not only presents a detailed phylogenetic analysis of Rho proteins, but also discusses the possible... 
Rho GTPases | G proteins | Life Sciences | Biochemistry, general | Cancer Research | Molecular Medicine | Proteomics | Cell Biology
Book
Biochemical Journal, ISSN 0264-6021, 04/2017, Volume 474, Issue 7, pp. 1259 - 1272
Active, GTP-bound small GTPases need to be attached to membranes by post-translational lipid modifications in order to process and propagate information in... 
MYRISTOYLATED ARF1 | REGULATOR | GUANINE-NUCLEOTIDE-EXCHANGE | STRUCTURAL BASIS | EFFICIENT ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | RAB7 GTPASE | RHO-GTPASES | PROTEINS | BINDING | FAMILY | Humans | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | GTPase-Activating Proteins - metabolism | Histidine - metabolism | rhoA GTP-Binding Protein - genetics | DNA-Binding Proteins - metabolism | Protein Isoforms - metabolism | Guanine Nucleotide Exchange Factors - metabolism | ADP-Ribosylation Factor 1 - metabolism | Phosphatidylinositols - metabolism | ADP-Ribosylation Factor 1 - genetics | Legionella pneumophila - chemistry | Phosphatidylinositols - genetics | Recombinant Proteins - metabolism | Gene Expression | Guanine Nucleotide Exchange Factors - genetics | rho GTP-Binding Proteins - genetics | Oligopeptides - genetics | Bacterial Proteins - genetics | Histidine - genetics | Membranes, Artificial | Recombinant Proteins - genetics | Oligopeptides - metabolism | DNA-Binding Proteins - genetics | cdc42 GTP-Binding Protein - genetics | rho GTP-Binding Proteins - metabolism | Protein Binding | Bacterial Proteins - metabolism | Enzyme Activation | GTPase-Activating Proteins - genetics | rac1 GTP-Binding Protein - metabolism | Protein Isoforms - genetics | rac1 GTP-Binding Protein - genetics | Index Medicus
Journal Article
Genes and Development, ISSN 0890-9369, 01/2003, Volume 17, Issue 2, pp. 295 - 309
Wnt/Frizzled (Fz) signaling controls cell polarity/movements during vertebrate gastrulation via incompletely defined mechanisms. We demonstrated previously... 
Rho | Vertebrates | Gastrulation | Frizzled | Wnt | Rac | HUMAN NEUTROPHILS | TISSUE POLARITY | PLANAR CELL POLARITY | DEVELOPMENTAL BIOLOGY | MAMMALIAN-CELLS | vertebrates | DROSOPHILA EYE | XENOPUS-LAEVIS | CONVERGENT EXTENSION MOVEMENTS | MAMMARY ONCOGENE | GENETICS & HEREDITY | ACTIN CYTOSKELETON | gastrulation | Xenopus - genetics | Humans | rac GTP-Binding Proteins - metabolism | Wnt Proteins | Phosphoproteins - metabolism | Xenopus - embryology | Cell Movement - genetics | Cell Movement - physiology | RNA - genetics | rac GTP-Binding Proteins - genetics | JNK Mitogen-Activated Protein Kinases | Drosophila - embryology | Dishevelled Proteins | Drosophila - genetics | RNA - metabolism | Frizzled Receptors | Proto-Oncogene Proteins - metabolism | Cell Line | Drosophila Proteins | Signal Transduction | rho GTP-Binding Proteins - genetics | Zebrafish Proteins | Proto-Oncogene Proteins - genetics | Gastrula - cytology | Phosphoproteins - genetics | Xenopus Proteins | Proteins - genetics | Cell Polarity - genetics | Adaptor Proteins, Signal Transducing | Animals | Proteins - metabolism | Xenopus - metabolism | Models, Biological | rho GTP-Binding Proteins - metabolism | Cell Polarity - physiology | Gastrula - metabolism | Drosophila - metabolism | Mitogen-Activated Protein Kinases - metabolism | Morphogenesis | Analysis | Genetic research | Physiological aspects | Genetic aspects | Genetic regulation | Cells | rac protein | Wnt protein | Frizzled protein | Dishevelled protein | Index Medicus | Research Paper
Journal Article
Journal Article
The New England Journal of Medicine, ISSN 0028-4793, 12/2011, Volume 365, Issue 25, pp. 2377 - 2388
The authors report that INF2 mutations are present in patients with focal segmental glomerulosclerosis (FSGS) associated with Charcot–Marie–Tooth neuropathy.... 
GLOMERULOSCLEROSIS | MEDICINE, GENERAL & INTERNAL | MYELIN | PROTEIN | NEUROPATHY | EPITHELIAL-CELLS | GENE | RHO | MEDIATED TRANSPORT | FORMIN | NEPHROPATHY | Humans | Middle Aged | Proteolipids - metabolism | Actins - metabolism | Male | Charcot-Marie-Tooth Disease - genetics | Young Adult | Kidney - metabolism | Glomerulosclerosis, Focal Segmental - etiology | Myelin and Lymphocyte-Associated Proteolipid Proteins | Adult | Female | Membrane Transport Proteins - metabolism | Microfilament Proteins - metabolism | Child | Microfilament Proteins - genetics | Charcot-Marie-Tooth Disease - complications | Schwann Cells - metabolism | Phenotype | Animals | Adolescent | Age of Onset | Heterozygote | Mice | Mutation | Myelin Proteins - metabolism | Glomerulonephritis | Gene mutations | Charcot-Marie-Tooth disease | Causes of | Genetic aspects | Research | Myelin proteins | Cdc42 protein | Disease | Exons | Genes | Amino acids | Nervous system | Neuropathy | Guanine nucleotide-binding protein | Proteins | Myelin P0 protein | Localization | Peripheral myelin protein 22 | Deoxyribonucleic acid--DNA | Kidneys | Schwann cells | Polymerization | Myelination | Genotyping | Biopsy | Glomerulus | Cytoskeleton | Genetic testing | Cytoplasm | Guanosinetriphosphatase | Index Medicus | Abridged Index Medicus | Schwann Cells | Genomics | Kidney | Charcot-Marie-Tooth Disease | Life Sciences | Proteolipids | Biochemistry, Molecular Biology | Actins | Microfilament Proteins | Membrane Transport Proteins | Myelin Proteins | Glomerulosclerosis, Focal Segmental
Journal Article
Journal Article