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Cancer Cell, ISSN 1535-6108, 2010, Volume 17, Issue 6, pp. 547 - 559
In mice, Lkb1 deletion and activation of Kras G12D results in lung tumors with a high penetrance of lymph node and distant metastases. We analyzed these... 
CELLCYCLE | SIGNALING | INACTIVATION | SUPPRESSOR | SIGNATURES | ONCOLOGY | SRC | ADENOCARCINOMA | SENSITIVITY | MUTATIONS | LKB1/STK11 | EXPRESSION | TUMORIGENESIS | CELL BIOLOGY | Lung Neoplasms - drug therapy | Protein-Serine-Threonine Kinases - deficiency | Protein-Tyrosine Kinases - metabolism | Proto-Oncogene Proteins p21(ras) - genetics | Genomics | Humans | Lung Neoplasms - metabolism | Gene Expression Profiling | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Cell Movement - genetics | Phosphorylation - genetics | RNA Interference | Gene Expression Regulation, Neoplastic - genetics | MAP Kinase Kinase 1 - antagonists & inhibitors | Carcinoma, Non-Small-Cell Lung - metabolism | Signal Transduction - genetics | Enzyme Inhibitors - therapeutic use | Focal Adhesion Protein-Tyrosine Kinases - antagonists & inhibitors | Focal Adhesion Protein-Tyrosine Kinases - genetics | Focal Adhesions - genetics | Signal Transduction - drug effects | Mice, Nude | Cell Line, Tumor | Mice | TOR Serine-Threonine Kinases | src-Family Kinases - genetics | Protein-Tyrosine Kinases - antagonists & inhibitors | ras Proteins - genetics | Lung Neoplasms - pathology | Cell Transdifferentiation - genetics | Protein-Tyrosine Kinases - genetics | Neoplasm Metastasis - drug therapy | Mice, Mutant Strains | Protein-Serine-Threonine Kinases - antagonists & inhibitors | src-Family Kinases - metabolism | Female | Drug Therapy, Combination | Lung Neoplasms - genetics | Cell Adhesion - genetics | Carcinoma, Non-Small-Cell Lung - genetics | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | src-Family Kinases - antagonists & inhibitors | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Up-Regulation - genetics | Xenograft Model Antitumor Assays | Neoplasm Metastasis - genetics | Animals | MAP Kinase Kinase 2 - antagonists & inhibitors | Protein Kinase Inhibitors - therapeutic use | Focal Adhesions - metabolism | Proteomics | Protein Kinase Inhibitors - pharmacology | Oncology, Experimental | Analysis | Lung cancer | Development and progression | Metastasis | Research | Cancer
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... 
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
The Journal of cell biology, ISSN 1540-8140, 2008, Volume 181, Issue 3, pp. 497 - 510
.... We next screened for ULK binding proteins and identified the focal adhesion kinase family interacting protein of 200 kD (FIP200... 
Yeasts | Starvation | NIH 3T3 cells | Microscopy | Neurons | Cell lines | Antibodies | Cultured cells | Focal adhesions | Gene expression regulation | COMPLEX | MOLECULAR MACHINERY | FOCAL ADHESION | GENE | C-ELEGANS | AXONAL ELONGATION | HUMAN BREAST-CANCER | SACCHAROMYCES-CEREVISIAE | SERINE/THREONINE KINASE | SELF-DIGESTION | CELL BIOLOGY | Protein Kinases - metabolism | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Fibroblasts - physiology | Microtubule-Associated Proteins - metabolism | Protein-Tyrosine Kinases - metabolism | Humans | Autophagy - physiology | Recombinant Fusion Proteins - metabolism | Autophagy-Related Protein-1 Homolog | Intracellular Membranes - ultrastructure | Protein-Tyrosine Kinases - genetics | Protein-Serine-Threonine Kinases - metabolism | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Phagosomes - metabolism | Protein-Serine-Threonine Kinases - genetics | Fungal Proteins - genetics | Mice, Knockout | Focal Adhesion Protein-Tyrosine Kinases - genetics | Animals | Autophagy-Related Protein 5 | Recombinant Fusion Proteins - genetics | Fibroblasts - cytology | Mice | TOR Serine-Threonine Kinases | Intracellular Membranes - metabolism | Fungal Proteins - metabolism | Allelomorphism | Muridae | Physiological aspects | Cell physiology | Research | Properties | Binding proteins | Identification and classification | Phosphotransferases
Journal Article
Journal of Endocrinology, ISSN 0022-0795, 04/2005, Volume 185, Issue 1, pp. 19 - 33
Journal Article
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2013, Volume 8, Issue 7, p. e71531
CD45 is a protein tyrosine phosphatase expressed on all cells of hematopoietic origin that is known to regulate Src family kinases... 
CYTOKINE PRODUCTION | COLONY-STIMULATING FACTOR | B-CELL | CD4(+)CD8(+) THYMOCYTES | NEGATIVE REGULATION | MULTIDISCIPLINARY SCIENCES | ENDOTHELIAL-CELL APOPTOSIS | SRC-FAMILY KINASES | INTEGRIN-MEDIATED ADHESION | T-CELLS | FOCAL ADHESIONS | Paxillin - metabolism | Calpain - metabolism | Leukocyte Common Antigens - metabolism | Cell Shape - genetics | Cell Movement - genetics | Proteolysis - drug effects | Focal Adhesion Kinase 2 - metabolism | src-Family Kinases - metabolism | Time-Lapse Imaging - methods | Phosphorylation - drug effects | Focal Adhesion Kinase 1 - metabolism | Cell Adhesion - genetics | Mice, Inbred C57BL | Cells, Cultured | Macrophages - cytology | Blotting, Western | Mice, Knockout | Leupeptins - pharmacology | Microscopy, Confocal | Macrophages - metabolism | Animals | Cysteine Proteinase Inhibitors - pharmacology | Cytoskeleton - metabolism | Leukocyte Common Antigens - genetics | Mice | Proteins | Tyrosine | Phosphatases | Phenols | Calpain | Macrophages | Phosphotransferases | Phosphorylation | Motility | Cytology | Proline | Kinases | Phosphatase | Cell spreading | CD45 antigen | Cell morphology | Defects | Cell adhesion & migration | Degradation | Immunology | Rodents | Bone marrow | Localization | Protein-tyrosine kinase | Src protein | Adhesion | Hemopoiesis | Virology | Studies | Molecular modelling | Cytoskeleton | Focal adhesion kinase | Paxillin | Cell migration | Protein-tyrosine-phosphatase
Journal Article
Nature cell biology, ISSN 1476-4679, 2004, Volume 6, Issue 2, pp. 154 - 161
Journal Article