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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
The Journal of Physiology, ISSN 0022-3751, 08/2018, Volume 596, Issue 16, pp. 3637 - 3653
Journal Article
Journal Article
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2009, Volume 106, Issue 38, pp. 16233 - 16238
Carbonic anhydrase (CA) IX is a plasma membrane-associated member of the α-CA enzyme family, which is involved in solid tumor acidification. It is a marker of... 
Enzymes | Molecules | Active sites | Memory interference | Crystals | Cell adhesion | Hypoxia | Dimers | Crystal structure | Tumors | CA-IX | ISOZYMES | PROTEIN-TYROSINE-PHOSPHATASES | MULTIDISCIPLINARY SCIENCES | RESOLUTION | INTRACELLULAR PH | EXTRACELLULAR DOMAIN | E-CADHERIN | PROTON-TRANSFER | HYPOXIA | REFINED STRUCTURE | Protons | Carbon Dioxide - chemistry | Carbonic Anhydrases - genetics | Humans | Protein Multimerization | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Carbonic Anhydrases - chemistry | Antigens, Neoplasm - chemistry | Carbonic Anhydrases - metabolism | Disulfides - chemistry | Enzyme Inhibitors - chemistry | Drug Design | Water - chemistry | Antigens, Neoplasm - metabolism | Bicarbonates - chemistry | Carbonic Anhydrase IX | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Antigens, Neoplasm - genetics | Catalytic Domain | Carbon Dioxide - metabolism | Enzyme Inhibitors - metabolism | Crystallization | Enzyme Inhibitors - pharmacology | Water - metabolism | Models, Molecular | Neoplasms - enzymology | Recombinant Proteins - chemistry | Neoplasms - drug therapy | Sequence Homology, Amino Acid | Bicarbonates - metabolism | Protein Conformation | Kinetics | Neoplasms - pathology | Hydrogen-Ion Concentration | Structure | Proteins | Membranes | Molecular structure | Chemical compounds | Cell adhesion & migration | Index Medicus | Biological Sciences
Journal Article
Journal Article