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Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 4, pp. 1261 - 1266
Signaling through the Rho family of small GTPases has been intensely investigated for its crucial roles in a wide variety of human diseases. Although RhoA and... 
Molecules | Growth cones | Cell motility | Phosphorylation | Neurons | Fluorescence | Fibroblasts | Swiss 3T3 cells | Pseudopodia | Research universities | ACTIVATION | protein trafficking | cytoskeleton | PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | VESICLE TRAFFICKING | Cdc42 inhibitor | NEURONAL DEVELOPMENT | RAC | computer-assisted virtual screening | FILOPODIA | CDC42 GTPASES | protein-protein interaction | REGULATORS | ACTIN CYTOSKELETON | RHO-GTPASES | User-Computer Interface | Golgi Apparatus - drug effects | Humans | Swiss 3T3 Cells | Molecular Sequence Data | Golgi Apparatus - physiology | Cell Movement - physiology | Neurons - ultrastructure | cdc42 GTP-Binding Protein - antagonists & inhibitors | Adaptor Proteins, Vesicular Transport - chemistry | Drug Evaluation, Preclinical | Neurons - drug effects | Binding Sites | Wound Healing - drug effects | Amino Acid Sequence | Cell Survival - drug effects | Adaptor Proteins, Vesicular Transport - physiology | Protein Interaction Domains and Motifs - drug effects | Adaptor Proteins, Vesicular Transport - antagonists & inhibitors | Cells, Cultured | Models, Molecular | cdc42 GTP-Binding Protein - physiology | Sequence Homology, Amino Acid | Cell Movement - drug effects | Animals | Signal Transduction - drug effects | cdc42 GTP-Binding Protein - genetics | cdc42 GTP-Binding Protein - chemistry | Mice | Cell interaction | Motility | Physiological aspects | Research | Health aspects | Cells | Golgi apparatus | protein–protein interaction | Biological Sciences
Journal Article
Journal Article
Journal Article
Journal Article
Molecular cancer therapeutics, ISSN 1538-8514, 2017, Volume 16, Issue 5, pp. molcanther.0442.2016 - 818
The Rho GTPases Rac (Ras-related C3 botulinum toxin substrate) and Cdc42 (cell division control protein 42 homolog) regulate cell functions governing cancer... 
P21-ACTIVATED KINASE | EHOP-016 | CELLS | ACTIVATION | ACTIN | ONCOLOGY | RAC | STAT3 | PAK | HUMAN BREAST-CANCER | SMALL-MOLECULE INHIBITOR | Cell Survival - drug effects | Pyrimidines - administration & dosage | Humans | Carbazoles - administration & dosage | Breast Neoplasms - drug therapy | Neovascularization, Pathologic - pathology | Cell Movement - drug effects | Neoplasm Metastasis | Animals | Breast Neoplasms - genetics | Signal Transduction - drug effects | Breast Neoplasms - pathology | Neovascularization, Pathologic - drug therapy | cdc42 GTP-Binding Protein - genetics | cdc42 GTP-Binding Protein - antagonists & inhibitors | rac1 GTP-Binding Protein - antagonists & inhibitors | Cell Line, Tumor | Female | Neovascularization, Pathologic - genetics | Antineoplastic Agents - pharmacology | Cell Proliferation - drug effects | Mice | rac1 GTP-Binding Protein - genetics | Cdc42 protein | Mesenchyme | Epithelial cells | Downstream effects | Homology | AKT protein | Malignancy | Metastasis | Kinases | Cell surface | Metastases | Cell adhesion & migration | Angiogenesis | Actin | Polarity | Mammary gland | Incubation | Stat3 protein | Cell division | p21-activated kinase | MAP kinase | Breast cancer | Botulinum toxin | Substrates | Signaling | Detachment | Inhibitors | Cell migration | Cancer | Tumors | Apoptosis | anoikis | breast cancer | Rac | Cdc42 inhibitor | Cdc42
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2009, Volume 325, Issue 5936, pp. 83 - 87
Type IV pili mediate the initial interaction of many bacterial pathogens with their host cells. In Neisseria meningitidis, the causative agent of cerebrospinal... 
Intercellular junctions | Cell lines | Actins | Small interfering RNA | Bacteria | Cadherins | Reports | Bacterial adhesion | Infections | Blood brain barrier | Endothelial cells | CDC42 | ADHESION | HUMAN EPITHELIAL-CELLS | PATHOGENIC NEISSERIA | TWITCHING MOTILITY | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | BARRIER | PAR3 | RECEPTOR | ADHERENS | Cell Polarity | Brain - microbiology | Cadherins - metabolism | Humans | cdc42 GTP-Binding Protein - metabolism | Intercellular Junctions - microbiology | Phosphoproteins - metabolism | Blood-Brain Barrier - microbiology | Antigens, CD - metabolism | Catenins | Endothelial Cells - microbiology | Endothelium, Vascular - ultrastructure | Brain - blood supply | Protein Kinase C - metabolism | Membrane Proteins - metabolism | Neisseria meningitidis - physiology | Neisseria meningitidis - pathogenicity | Cell Line | Brain - cytology | Endothelial Cells - metabolism | Cell Cycle Proteins - metabolism | Intercellular Junctions - metabolism | Cell Adhesion Molecules - metabolism | Blood-Brain Barrier - metabolism | Endothelium, Vascular - microbiology | Bacterial Adhesion | Endothelium, Vascular - metabolism | Fimbriae, Bacterial - physiology | Adaptor Proteins, Signal Transducing - metabolism | Intercellular Junctions - ultrastructure | Measurement | Polarity (Biology) | Neisseria meningitidis | Properties | Health aspects | Endothelium | Brain | Meningitis | Eukaryotes | Cell adhesion & migration | Fimbriae, Bacterial | Endothelial Cells | Cell Adhesion Molecules | Intercellular Junctions | Membrane Proteins | Life Sciences | Microbiology and Parasitology | Adaptor Proteins, Signal Transducing | Phosphoproteins | cdc42 GTP-Binding Protein | Endothelium, Vascular | Cell Cycle Proteins | Antigens, CD | Protein Kinase C | Blood-Brain Barrier | cytology | meningitis | microbiology | physiology | ultrastructure | blood brain barrier | pathogenicity | blood supply | metabolism
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 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 | 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
Nature cell biology, ISSN 1476-4679, 2018, Volume 20, Issue 9, pp. 1023 - 1031
Endocytosis mediates the cellular uptake of micronutrients and the turnover of plasma membrane proteins. Clathrin-mediated endocytosis is the major uptake... 
CDC42 | DOMAIN | BAR | LINKED MENTAL-RETARDATION | CLATHRIN-INDEPENDENT ENDOCYTOSIS | EGF-RECEPTOR | PATHWAY | LEADING-EDGE | PROTEIN GRAF1 | ACTIN CYTOSKELETON | CELL BIOLOGY | Phosphatidylinositol Phosphates - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | cdc42 GTP-Binding Protein - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | GTPase-Activating Proteins - metabolism | Endocytosis | Time Factors | HEK293 Cells | Minor Histocompatibility Antigens - genetics | Cell Membrane - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Intracellular Signaling Peptides and Proteins - genetics | Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases - metabolism | Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases - genetics | Signal Transduction | Membrane Proteins - genetics | Rats | Carrier Proteins - genetics | Minor Histocompatibility Antigens - metabolism | Animals | Carrier Proteins - metabolism | cdc42 GTP-Binding Protein - genetics | Protein Binding | GTPase-Activating Proteins - genetics | Clathrin | Cell membranes | Research | Analysis | Cdc42 protein | Deactivation | Stimulation | Guanosine triphosphatases | Activation | Membrane proteins | Proteins | Phosphatidylinositol | Micronutrients | Receptors | Guanosine triphosphate | Inositol polyphosphate 5-phosphatase | Dismantling
Journal Article