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Nature, ISSN 0028-0836, 03/2010, Volume 464, Issue 7287, pp. 431 - 435
Activating mutations in KRAS and BRAF are found in more than 30% of all human tumours and 40% of melanoma, respectively, thus targeting this pathway could have... 
SELECTIVE INHIBITOR | POTENT | EFFICACY | MECHANISM | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | KINASE | C-RAF | B-RAF | MUTATIONS | PROTEINS | Neoplasms - metabolism | ras Proteins - genetics | Proto-Oncogene Proteins p21(ras) | Diphenylamine - pharmacology | raf Kinases - antagonists & inhibitors | Humans | Protein Multimerization | ras Proteins - metabolism | Protein Transport - drug effects | Extracellular Signal-Regulated MAP Kinases - metabolism | raf Kinases - metabolism | Diphenylamine - analogs & derivatives | Mitogen-Activated Protein Kinase Kinases - metabolism | Adenosine Triphosphate - metabolism | Indoles - pharmacology | Benzamides - pharmacology | Cell Membrane - metabolism | raf Kinases - genetics | Cell Membrane - drug effects | Proto-Oncogene Proteins B-raf - metabolism | Proto-Oncogene Proteins B-raf - chemistry | Pyrazoles - pharmacology | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Indenes - pharmacology | raf Kinases - chemistry | Proto-Oncogene Proteins c-raf - genetics | Mitogen-Activated Protein Kinase Kinases - antagonists & inhibitors | Neoplasms - enzymology | Proto-Oncogene Proteins - genetics | Enzyme Activation - drug effects | Sulfonamides - pharmacology | Proto-Oncogene Proteins c-raf - metabolism | Neoplasms - drug therapy | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Xenograft Model Antitumor Assays | Animals | MAP Kinase Signaling System - drug effects | Protein Kinase Inhibitors - therapeutic use | Proto-Oncogene Proteins B-raf - genetics | Proto-Oncogene Proteins c-raf - deficiency | Cell Proliferation - drug effects | Mice | Protein Kinase Inhibitors - pharmacology | Neoplasms - pathology | Ras genes | Growth | Physiological aspects | Cellular signal transduction | Genetic aspects | Research | Mitogen-activated protein kinases | Competition | Clinical trials | Enzymes | Kinases | Proteins | Cellular | Inhibitors | Pathways | Tumours | Signalling | Dimerization
Journal Article
International Immunopharmacology, ISSN 1567-5769, 11/2013, Volume 17, Issue 3, pp. 638 - 650
Neutrophils play a critical role in the host defense against bacterial and fungal infections, but their inappropriate activation also contributes to tissue... 
Signaling | Receptors | Inflammation | Kinases | Neutrophils | ACTIVATED PROTEIN-KINASE | COLONY-STIMULATING FACTOR | LEUKOCYTE ADHESION DEFICIENCY | IMMUNOLOGY | SRC-FAMILY KINASES | HUMAN POLYMORPHONUCLEAR LEUKOCYTES | HIGH-AFFINITY RECEPTOR | TUMOR-NECROSIS-FACTOR | TOLL-LIKE RECEPTORS | PHARMACOLOGY & PHARMACY | BETA-GAMMA-SUBUNITS | NF-KAPPA-B | Signal Transduction - immunology | Animals | Receptors, Cell Surface - immunology | Humans | Neutrophils - immunology | Selectins - immunology | Mycoses | Lectins | Fc receptors | Integrins | FcR, Fc-receptor | GPI, glycosylphosphatidylinositol anchor | CLEC, C-type lectin | OSCAR, osteoclast-associated receptor | PKB, protein kinase B | DAG, diacyl-glycerol | Tyk2, tyrosine protein kinase 2 | VCAM-1, vascular cell adhesion molecule 1 | ICAM-1, intercellular adhesion molecule 1 | FADD, Fas-associated protein with death domain | IκB, inhibitor of NF-κB | GM-CSF, granulocyte | MyD88, myeloid differentiation protein 88 | TNF, tumor necrosis factor | LTβ, lymphotoxin β | TRADD, TNFR1-associated death domain protein | Abl, Abelson leukemia proto-oncogene | SLP-76, SH2 domain-containing leukocyte protein of 76 kDa | CALDAG-GEFI, calcium and DAG-regulated guanine nucleotide exchange factor I | IL, interleukin | Src, Rous sarcoma virus proto-oncogene | IRF, IFN regulatory factor | RIG, retinoic acid-inducible gene | PLC, phospholipase C | TCR, T-cell receptor | IKK, IκB kinase | ITAM, immunoreceptor tyrosine-based activation motif | CARD, caspase activation and recruitment domain | IP3, inositol-tris-phosphate | CHO, Chinese hamster ovary cells | MKK, MAP kinase kinase | fMLP, formly-Met-Leu-Phe | TRAF, TNF receptor-associated factor | MIP, macrophage inflammatory protein | Rac, Ras-related C3 botulinum toxin substrate | monocyte colony-stimulating factor | PIP3, phosphatidylinositol-3-phosphate | VLA-4, very late antigen 4 (α4β1 integrin) | PAF, platelet activating factor | STAT, signal transducer and activator of transcription | TAK, TGFβ-activated kinase 1 | Mac-1, macrophage antigen 1 (αMβ2 integrin) | FcRγ, Fc-receptor γ-chain | Asc, apoptosis-associated speck-like protein containing a CARD | cIAP, cellular inhibitor of apoptosis | BCR, B-cell receptor | Fgr, Gardner–Rasheed feline sarcoma proto-oncogene | VASP, vasodilator-stimulated phosphoprotein | Hck, hematopoietic cell kinase | TGFβ, transforming growth factor β | Rap, Ras-related protein | SHP-1, SH2 domain-containing protein tyrosine phosphatase 1 | Syk, spleen tyrosine kinase | GPCR, G protein-coupled receptor | G-CSF, granulocyte colony-stimulating factor | TREM, triggering receptor expressed on myeloid cells | DISC, death-inducing signaling complex | MDL-1, myeloid DAP12-associating lectin 1 | C3G, Crk SH3 domain-binding guanine nucleotide exchange factor (RapGEF1) | NF-κB, nuclear factor κB | ERM, ezrin-radixin-moesin | Epac1, exchange protein activated by cyclic AMP 1 | LTB4, leukotriene B4 | Mcl, macrophage C-type lectin | SAP130, Sin3A-associated protein of 130 kDa | SH2, Src-homology 2 domain | MAP kinase, mitogen-activated protein kinase | PSGL-1, P-selectin glycoprotein ligand | PI3K, phoshoinositide-3-kinase | ADAP, adhesion and degranulation promoting adapter protein (Fyb, SLAP-130) | NLRP3, NOD-like receptor family, pyrin domain containing 3 | MDA5, melanoma differentiation-associated protein 5 | TLR, Toll-like receptor | GRK, GPCR kinase | LAD, leukocyte adhesion deficiency | MAPKAP-kinase, MAP kinase-associated protein kinase | ZAP-70, ζ-chain-associated protein of 70 kDa | TRAIL, TNF-related apoptosis-inducing ligand | JNK, c-Jun N-terminal kinase | LFA-1, lymphocyte function-associated receptor 1 (αLβ2 integrin) | ROS, reactive oxygen species | RIP3, receptor-interacting serine-threonine protein kinase 3 | DAP12, DNAX activating protein 12 | IFN, interferon | PIR, paired immunoglobulin-like receptor | PKC, protein kinase C | PAK, p21-activated kinase | ESL-1, E-selectin ligand 1 | GAP, GTPase activating protein | ERK, extracellular signal-regulated kinase | SOCS, suppressor of cytokine signaling | JAK, Janus kinase | RANK, receptor activator of NF-κB | IRAK, IL-1 receptor-associated kinase | NOD, nucleotide-binding oligomerization domain containing protein | CEACAM3, carcinoembryonic antigen-related cell adhesion molecule 3 (CD66b)
Journal Article
Annual Review of Pharmacology and Toxicology, ISSN 0362-1642, 2014, Volume 54, Issue 1, pp. 435 - 456
Protein-protein interactions (PPIs) are critical regulatory events in physiology and pathology, and they represent an important target space for... 
Allosteric inhibitors | Interfacial binders | Orthosteric inhibitors | Small-molecule inhibitors | Protein-protein interactions | PPIs | interfacial binders | PYRUVATE-KINASE M2 | DRUG DISCOVERY | protein-protein interactions | AGGRESSIVE CARCINOMA | SIGNAL-TRANSDUCTION | STRUCTURAL BASIS | IN-VIVO | NUCLEOTIDE EXCHANGE FACTOR | CANCER METABOLISM | PHARMACOLOGY & PHARMACY | allosteric inhibitors | BREFELDIN-A | TOXICOLOGY | orthosteric inhibitors | B-RAF | small-molecule inhibitors | SOS1 Protein - antagonists & inhibitors | ras Proteins - genetics | Humans | ras Proteins - metabolism | Molecular Targeted Therapy | Proto-Oncogene Proteins c-akt - genetics | Carrier Proteins - agonists | SOS1 Protein - genetics | Membrane Proteins - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Proto-Oncogene Proteins B-raf - metabolism | Protein Interaction Domains and Motifs - drug effects | Membrane Proteins - genetics | SOS1 Protein - metabolism | ras Proteins - antagonists & inhibitors | Models, Molecular | Thyroid Hormones - agonists | Thyroid Hormones - genetics | Membrane Proteins - agonists | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Carrier Proteins - genetics | Carrier Proteins - metabolism | Proto-Oncogene Proteins B-raf - genetics | Thyroid Hormones - metabolism | Protein Binding | Proto-Oncogene Proteins c-akt - antagonists & inhibitors | Proteins | Protein binding
Journal Article
Nature, ISSN 0028-0836, 06/2009, Volume 459, Issue 7248, pp. 852 - 856
Cells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1... 
FISSION YEAST | WEE1 | PHOSPHORYLATION | NIM1/CDR1 MITOTIC INDUCER | PROTEIN-KINASE | NEGATIVE REGULATION | MULTIDISCIPLINARY SCIENCES | GROWTH | DIVISION PLANE | DUAL-SPECIFICITY KINASE | SCHIZOSACCHAROMYCES-POMBE | Protein Kinases - metabolism | Cell Polarity | Phosphorylation | Mitosis | Protein-Tyrosine Kinases - metabolism | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Protein Transport | Cell Cycle Proteins - antagonists & inhibitors | Schizosaccharomyces - metabolism | Nuclear Proteins - antagonists & inhibitors | ras-GRF1 - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Schizosaccharomyces pombe Proteins - metabolism | Cell Cycle - physiology | G2 Phase | Protein-Serine-Threonine Kinases - metabolism | Schizosaccharomyces - cytology | Fungal Proteins - metabolism | Protein-Tyrosine Kinases - antagonists & inhibitors | Schizosaccharomyces pombe Proteins - antagonists & inhibitors | Arctic research | Cell cycle | Physiological aspects | Cell physiology | Genetic aspects | Research | Protein kinases | Proteins | Cell growth | Kinases | Molecular biology | Monitoring systems | ras-GRF1 | Protein-Serine-Threonine Kinases | Schizosaccharomyces pombe Proteins | Fungal Proteins | Cellular Biology | Nuclear Proteins | Life Sciences | Cell Cycle | Protein Kinases | Protein-Tyrosine Kinases | Cell Cycle Proteins | Schizosaccharomyces
Journal Article
Nature Medicine, ISSN 1078-8956, 08/2012, Volume 18, Issue 8, pp. 1239 - 1247
The inactivation of the p53 tumor suppressor pathway, which often occurs through mutations in TP53 (encoding tumor protein 53) is a common step in human... 
MEDICINE, RESEARCH & EXPERIMENTAL | N-RAS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TUMOR-SUPPRESSOR ACTIVITY | STAPLED P53 | BRAF | MALIGNANT-MELANOMA | P53 PATHWAY | CELL-DEATH | CELL BIOLOGY | BREAST-CANCER | METASTATIC MELANOMA | IN-VIVO | Up-Regulation | Proto-Oncogene Proteins c-mdm2 - genetics | Tumor Suppressor Protein p53 - antagonists & inhibitors | Apoptosis - drug effects | Humans | Neoplasm Proteins - physiology | Gene Expression Regulation, Neoplastic | Recombinant Fusion Proteins - physiology | Skin Neoplasms - chemistry | Male | Melanocytes - metabolism | Neoplasm Proteins - antagonists & inhibitors | Cell Line, Tumor - transplantation | Proto-Oncogene Proteins - biosynthesis | Tumor Suppressor Protein p53 - physiology | Cell-Penetrating Peptides - pharmacology | Nuclear Proteins - biosynthesis | Female | Antineoplastic Agents - pharmacology | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Cell Line, Tumor - metabolism | Melanoma - chemistry | Proto-Oncogene Proteins c-mdm2 - biosynthesis | Proto-Oncogene Proteins - antagonists & inhibitors | Tumor Stem Cell Assay | Membrane Proteins - genetics | Neoplasm Proteins - biosynthesis | Melanoma, Experimental - etiology | Mice, Inbred C57BL | Mice, Transgenic | Proto-Oncogene Proteins - genetics | Melanoma - pathology | Melanoma - secondary | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Xenograft Model Antitumor Assays | Animals | Melanoma, Experimental - genetics | GTP Phosphohydrolases - genetics | Keratinocytes - metabolism | Mice, Nude | Nuclear Proteins - antagonists & inhibitors | Proto-Oncogene Proteins - physiology | Signal Transduction - physiology | Mice | Nuclear Proteins - physiology | Drug Resistance, Neoplasm - physiology | Drug Resistance, Neoplasm - drug effects | Care and treatment | Gene mutations | Melanoma | Diagnosis | Research | Gene expression | Identification and classification | Skin cancer | Proteins | Cell growth | Mutation | Cell cycle
Journal Article
Journal of Clinical Oncology, ISSN 0732-183X, 12/2013, Volume 31, Issue 34, pp. 4333 - 4342
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2008, Volume 379, Issue 4, pp. 787 - 802
Journal Article
2002, Methods in molecular biology, ISBN 089603934X, Volume 189., xi, 267
Small GTPase binding proteins (GTPases) are an ancient group of proteins that play key roles in almost every aspect of cell biology, from cell proliferation to... 
Ras proteins | Guanosine triphosphatase | Laboratory manuals |