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Circulation Research, ISSN 0009-7330, 10/2006, Volume 99, Issue 8, pp. 853 - 860
We describe extracellular interactions between fibronectin (Fn) and vascular endothelial growth factor (VEGF) that influence integrin-growth factor receptor... 
Signal transduction | Endothelial cell differentiation | Endothelial cell growth | Vascular endothelial growth factor | Endothelial cells | Fibronectin | Integrins | Vascular endothelial growth factor receptors | MIGRATION | endothelial cell growth | endothelial cells | ACTIVATION | CARDIAC & CARDIOVASCULAR SYSTEMS | ANGIOGENESIS | signal transduction | FACTOR RECEPTORS | endothelial cell differentiation | PEPTIDE | ADHESION | integrins | vascular endothelial growth factor receptors | fibronectin | vascular endothelial growth factor | PERIPHERAL VASCULAR DISEASE | HEMATOLOGY | TUMOR-GROWTH | SMOOTH-MUSCLE CELLS | BETA INTEGRIN | EMBRYOID BODIES | Binding, Competitive | Recombinant Proteins - metabolism | Heparin - metabolism | Cell Proliferation | Humans | Cells, Cultured | Extracellular Matrix Proteins - physiology | Vascular Endothelial Growth Factor A - metabolism | Protein Isoforms - isolation & purification | Cell Movement - physiology | Fibronectins - metabolism | Drug Synergism | Peptides - metabolism | Protein Isoforms - metabolism | Endothelial Cells - cytology | Fibronectins - physiology | Signal Transduction - physiology | Fibronectins - genetics | Binding Sites | Fibronectins - isolation & purification | Vascular Endothelial Growth Factor A - physiology | Endothelial Cells - physiology | Protein Isoforms - genetics | Protein Structure, Tertiary - physiology | Index Medicus
Journal Article
Biochemistry, ISSN 0006-2960, 08/2017, Volume 56, Issue 30, pp. 3877 - 3880
The second extracellular loop (ECL2) of the G protein-coupled receptor (GPCR) family is important for ligand interaction and drug discovery. ECL2 of the family... 
COMPLEX | ACTIVATION | GENE-RELATED PEPTIDE | PROTEIN-COUPLED RECEPTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | Protein Multimerization | Cercopithecus aethiops | Peptide Fragments - pharmacology | Receptor Activity-Modifying Protein 1 - chemistry | Calcitonin Gene-Related Peptide - chemistry | Receptors, Calcitonin Gene-Related Peptide - metabolism | Calcitonin Receptor-Like Protein - agonists | Miotics - pharmacology | Receptors, Calcitonin Gene-Related Peptide - chemistry | Miotics - metabolism | Receptors, Calcitonin Gene-Related Peptide - agonists | Protein Interaction Domains and Motifs | Calcitonin Gene-Related Peptide - metabolism | Binding Sites | Peptide Fragments - genetics | Binding, Competitive | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Calcitonin Gene-Related Peptide - pharmacology | Miotics - chemistry | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Receptor Activity-Modifying Protein 1 - metabolism | Recombinant Proteins - chemistry | Calcitonin Gene-Related Peptide - genetics | Receptor Activity-Modifying Protein 1 - genetics | Recombinant Proteins - pharmacology | Calcitonin Receptor-Like Protein - metabolism | Protein Interaction Mapping | Point Mutation | Peptide Fragments - chemistry | Animals | Signal Transduction - drug effects | Calcitonin Receptor-Like Protein - genetics | Ligands | Protein Conformation | Receptors, Calcitonin Gene-Related Peptide - genetics | Structural Homology, Protein | Kinetics | COS Cells | Amino Acid Substitution | Usage | Research | Antibiosis | Antimetabolites | Calcitonin | Index Medicus
Journal Article
Arteriosclerosis, Thrombosis, and Vascular Biology, ISSN 1079-5642, 04/2017, Volume 37, Issue 4, pp. 694 - 706
OBJECTIVE—Increasing evidence suggests that contractile dysfunction in smooth muscle cells (SMCs) plays a critical role in aortic biomechanical dysfunction and... 
Caspase 1 | Glyburide | Inflammasomes | Contractile proteins | Proteolysis | Aortic aneurysm | OXIDATIVE STRESS | ACTIVATION | glyburide | inflammasomes | FOCUS | INJURY | caspase 1 | DELETION | aortic aneurysm | PERIPHERAL VASCULAR DISEASE | MICE | MUTATIONS | ISCHEMIA-REPERFUSION | HEMATOLOGY | proteolysis | contractile proteins | Aneurysm, Dissecting - genetics | Aortic Aneurysm, Abdominal - prevention & control | Inflammasomes - metabolism | Humans | Middle Aged | Caspase 1 - metabolism | Male | Mice, 129 Strain | Aorta, Abdominal - drug effects | Aneurysm, Dissecting - physiopathology | Glyburide - pharmacology | Inflammasomes - antagonists & inhibitors | Myocytes, Smooth Muscle - drug effects | Aneurysm, Dissecting - prevention & control | Disease Models, Animal | Muscle, Smooth, Vascular - drug effects | Genetic Predisposition to Disease | Myocytes, Smooth Muscle - enzymology | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Vasoconstriction - drug effects | Aortic Aneurysm, Thoracic - physiopathology | Mice, Knockout | Aorta, Thoracic - enzymology | Biomechanical Phenomena | Phenotype | Aortic Aneurysm, Abdominal - enzymology | Aortic Aneurysm, Abdominal - physiopathology | Caspase 1 - deficiency | Muscle, Smooth, Vascular - enzymology | Aortic Aneurysm, Thoracic - genetics | Aortic Aneurysm, Thoracic - prevention & control | Myocytes, Smooth Muscle - pathology | Muscle, Smooth, Vascular - physiopathology | NLR Family, Pyrin Domain-Containing 3 Protein - genetics | Aneurysm, Dissecting - enzymology | Muscle Proteins - metabolism | Female | Aorta, Abdominal - pathology | Aorta, Thoracic - drug effects | Angiotensin II | Aorta, Abdominal - physiopathology | Aorta, Thoracic - pathology | Aortic Aneurysm, Thoracic - enzymology | Mice, Inbred C57BL | Cells, Cultured | Aortic Aneurysm, Abdominal - genetics | Aorta, Thoracic - physiopathology | Aorta, Abdominal - enzymology | Inflammasomes - genetics | NLR Family, Pyrin Domain-Containing 3 Protein - deficiency | Muscle, Smooth, Vascular - pathology | Animals | Caspase 1 - genetics | Aged | Index Medicus | aneurysm | cardiovascular diseases | contractility | vessels
Journal Article
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 01/2017, Volume 56, Issue 1, pp. 297 - 301
The strikingly different reactivity of a series of homo‐ and heterodinuclear [(M III )(μ‐O) 2 (M III )′] 2+ (M=Ni; M′=Fe, Co, Ni and M=M′=Co) complexes with... 
metal–oxo complexes | nucleophilic oxidant | heterobimetallic complex | dioxygen activation | NIH shift | CORE | BIS(MU-OXO) COMPLEXES | OXO | HYDROXYLATION | STRUCTURAL-CHARACTERIZATION | COPPER | metal-oxo complexes | CHEMISTRY, MULTIDISCIPLINARY | LIGANDS | TEMPERATURE | METAL | Oxidation | Nickel | Reactivity | Hydroxylation | Coordination compounds | Index Medicus | Heterobimetallic Complex | Metal-Oxo | Dioxygen activation | NIH-Shift
Journal Article
The Plant Cell, ISSN 1040-4651, 11/2009, Volume 21, Issue 11, pp. 3700 - 3713
Journal Article
International Journal of Cancer, ISSN 0020-7136, 12/2014, Volume 135, Issue 11, pp. 2547 - 2557
Discoidin domain receptors (DDRs) are unusual receptor tyrosine kinases (RTKs) that are activated by fibrillar collagens instead of soluble growth factors.... 
discoidin domain receptor 2 | cancer cell proliferation | invasion | dimerization | colony formation | matrix metalloproteinases | intracellular juxtamembrane region | Matrix metalloproteinases | Discoidin domain receptor 2 | Intracellular juxtamembrane region | Colony formation | Cancer cell proliferation | Dimerization | Invasion | PHOSPHORYLATION | TRANSMEMBRANE | COLLAGEN-BINDING | TYROSINE KINASES | NILOTINIB | INHIBITION | ONCOLOGY | IMATINIB | TARGETS | EXPRESSION | EGF RECEPTOR | Neoplasms - metabolism | Phosphorylation | Cell Proliferation | Immunoprecipitation | Cross-Linking Reagents - pharmacology | Humans | Protein Multimerization | Immunoenzyme Techniques | Discoidin Domain Receptors | Flow Cytometry | Cell Membrane - metabolism | Tumor Cells, Cultured | Binding Sites | Protein Structure, Tertiary | Signal Transduction | Receptors, Mitogen - metabolism | Receptor Protein-Tyrosine Kinases - metabolism | Cell Adhesion | Blotting, Western | Disease Progression | Collagen - metabolism | Protein Binding | Neoplasms - pathology | Microscopy, Fluorescence | Cell Movement | Development and progression | Peptides | Memory (Computers) | Analysis | Collagen | Cancer | Medical research | Kinases | Binding | Cell proliferation | Tyrosine | Stomach | Lung | Collagens | Bladder | Activation | Matrix metalloproteinase | Tissues | Domains | Receptors | Metalloproteinase | Inhibition | Receptor mechanisms | Growth factors | Prostate | Index Medicus
Journal Article
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 2006, Volume 362, Issue 4, pp. 861 - 875
Recent advances in functional genomics have helped generate large-scale high-throughput protein interaction data. Such networks, though extremely valuable... 
protein–protein interaction | domain–domain interaction | co-evolution | domain-domain interaction | protein-protein interaction | PHYLOGENETIC PROFILES | COEVOLUTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | INTERACTION MAP | SACCHAROMYCES-CEREVISIAE | INTERACTION NETWORK | CONSERVATION | DATABASE | SEQUENCE | PAIRS | Nucleocytoplasmic Transport Proteins | Protein Structure, Tertiary | Amino Acid Sequence | COP-Coated Vesicles | Reproducibility of Results | GTPase-Activating Proteins | Karyopherins - chemistry | Nuclear Proteins - metabolism | Yeasts - chemistry | Mutation - genetics | Nuclear Proteins - chemistry | Protein Interaction Mapping | Proton-Translocating ATPases - chemistry | Proton-Translocating ATPases - metabolism | Membrane Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | DNA-Directed RNA Polymerases - chemistry | Membrane Proteins - metabolism | DNA-Directed RNA Polymerases - metabolism | Dimerization | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Proteins | RNA | Analysis | Genomics | Crystals | Structure | Adenosine triphosphatase | Index Medicus | MLE, Maximum Likelihood Estimation | PDB, Protein Data Bank | RDFF, Random Decision Forest Framework | RCDP, Relative Co-evolution of Domain Pairs | SLA, Sequence Lengths Assigned | protein—protein interaction | DPEA, Domain Pair Exclusion Analysis | domain—domain interaction
Journal Article
Journal Article
Neuron, ISSN 0896-6273, 01/2018, Volume 97, Issue 2, pp. 299 - 312.e6
Microglia exhibit two modes of motility: they constantly extend and retract their processes to survey the brain, but they also send out targeted processes to... 
THIK-1 | inflammasome | potassium channel | surveillance | microglia | ATP | ramification | interleukin-1β | OUTWARD POTASSIUM CURRENTS | CELLS | ACTIVATION | BRAIN-INJURY | IN-VIVO | MOUSE | RECEPTOR | MICE | NEUROSCIENCES | DAMAGE | Brain | Motility | Surveillance | Cytokines | Neurons | Channel gating | Lasers | Rodents | Immunosurveillance | Inflammation | Membrane potential | Microglia | Index Medicus
Journal Article