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NATURE STRUCTURAL & MOLECULAR BIOLOGY, ISSN 1545-9985, 01/2005, Volume 12, Issue 1, pp. 17 - 25
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 EMBO Journal, ISSN 0261-4189, 03/2012, Volume 31, Issue 6, pp. 1364 - 1378
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2010, Volume 107, Issue 20, pp. 9452 - 9457
Oligogalacturonides (OGs) released from the plant cell wall are active both as damage-associated molecular patterns (DAMPs) for the activation of the plant... 
Pathogens | Leaves | Receptors | Cell walls | Genes | Infections | Plants | Chimeras | Transgenic plants | Plant cells | Damage-associated molecular patterns | Elongation factor tu receptor | Pectin-mediated signaling | Chimeric receptors | Plant immunity | elongation factor tu receptor | ARABIDOPSIS-THALIANA | PROTEIN | BOTRYTIS-CINEREA | MULTIDISCIPLINARY SCIENCES | TRANSMEMBRANE DOMAIN | BACTERIAL FLAGELLIN | PATHOGEN RECOGNITION | INDUCED EXPRESSION | chimeric receptors | IN-VITRO | CELL-WALL | damage-associated molecular patterns | pectin-mediated signaling | plant immunity | DISEASE RESISTANCE | Protein Kinases - metabolism | Protein Structure, Tertiary | Arabidopsis Proteins - genetics | Protein Kinases - genetics | Arabidopsis - drug effects | Arabidopsis - enzymology | Botrytis - chemistry | Membrane Proteins - genetics | Oligosaccharides - metabolism | Mycotoxins - toxicity | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Microscopy, Confocal | Receptors, Pattern Recognition - genetics | Recombinant Fusion Proteins - genetics | Biological Assay | Membrane Proteins - metabolism | Genetic aspects | Research | Arabidopsis | Plant immunology | Chimeras (Organisms) | Enzymes | Molecular structure | Flowers & plants | Kinases | Gene expression | Cells | Index Medicus | oligogalacturonides | Immune response | oligosaccharides | Lethality | Pattern recognition | Biological Sciences
Journal Article
The Plant Journal, ISSN 0960-7412, 12/2014, Volume 80, Issue 5, pp. 809 - 822
Golgi‐resident type– II membrane proteins are asymmetrically distributed across the Golgi stack. The intrinsic features of the protein that determine its... 
glycan processing | icotiana benthamiana | transmembrane domain | glycosyltransferase | protein–protein interaction | membrane protein | type | olgi apparatus | rabidopsis thaliana | Arabidopsis thaliana | Nicotiana benthamiana | protein-protein interaction | N-glycan processing | type-II membrane protein | Golgi apparatus | LIFETIME IMAGING MICROSCOPY | LOCALIZATION | ARABIDOPSIS-THALIANA | MEMBRANE-SPANNING DOMAIN | PLANT SCIENCES | HELA-CELLS | GLYCOSYLTRANSFERASES | KIN RECOGNITION | APPARATUS | GLYCAN PROCESSING ENZYMES | ENDOPLASMIC-RETICULUM EXPORT | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Tobacco - metabolism | Sialyltransferases - genetics | N-Acetylglucosaminyltransferases - genetics | Rats | Cytoplasm - metabolism | Glycosylation | Recombinant Proteins - genetics | Sialyltransferases - metabolism | Genetic Complementation Test | N-Acetylglucosaminyltransferases - metabolism | Arabidopsis - metabolism | Polysaccharides - metabolism | Protein Interaction Maps | Tobacco - cytology | Arabidopsis - genetics | Plant Proteins - genetics | Animals | Plants, Genetically Modified | Polysaccharides - chemistry | Golgi Apparatus - metabolism | Plant Proteins - metabolism | Enzymes | Genetic engineering | Analysis | Protein-protein interactions | Membrane proteins | Proteins | Botany | Index Medicus | Original
Journal Article