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Cancer Cell, ISSN 1535-6108, 02/2013, Volume 23, Issue 2, pp. 171 - 185
We report a paracrine effect whereby endothelial cells (ECs) promote the cancer stem cell (CSC) phenotype of human colorectal cancer (CRC) cells. We showed... 
COLON-CANCER | METASTASIS | ONCOLOGY | NOTCH | NICHE | SELF-RENEWAL | RECEPTOR | GROWTH-FACTOR | TUMOR ANGIOGENESIS | DIFFERENTIATION | ANGIOCRINE FACTORS | CELL BIOLOGY | ADAM17 Protein | RNA, Small Interfering - genetics | Immunoprecipitation | Receptors, Notch - metabolism | Colorectal Neoplasms - genetics | Humans | Calcium-Binding Proteins - antagonists & inhibitors | Culture Media, Conditioned - pharmacology | Drug Resistance, Neoplasm | Immunoblotting | Peptide Fragments - pharmacology | Intercellular Signaling Peptides and Proteins - metabolism | Neoplastic Stem Cells - metabolism | Serrate-Jagged Proteins | Neoplastic Stem Cells - pathology | Antineoplastic Agents - pharmacology | Membrane Proteins - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Tumor Cells, Cultured | Liver Neoplasms - secondary | Colorectal Neoplasms - metabolism | Jagged-1 Protein | Biomarkers - metabolism | Calcium-Binding Proteins - metabolism | ADAM Proteins - antagonists & inhibitors | Liver Neoplasms - genetics | Signal Transduction | Endothelial Cells - metabolism | Membrane Proteins - genetics | Intercellular Signaling Peptides and Proteins - genetics | Cell Communication | Xenograft Model Antitumor Assays | ADAM Proteins - metabolism | Phenotype | Animals | Membrane Proteins - antagonists & inhibitors | Mice, Nude | Liver Neoplasms - metabolism | Mice | ADAM Proteins - genetics | Colorectal Neoplasms - pathology | Endothelial Cells - pathology | Calcium-Binding Proteins - genetics | Genetic aspects | Colorectal cancer | Stem cells | Endothelium | Index Medicus
Journal Article
Nature Cell Biology, ISSN 1465-7392, 02/2009, Volume 11, Issue 2, pp. 162 - 171
EpCAM was found to be overexpressed on epithelial progenitors, carcinomas and cancer-initiating cells. The role of EpCAM in proliferation, and its association... 
BREAST-CANCER | TARGET | STEM-CELLS | ADHESION MOLECULE | DEPENDENT GAMMA-SECRETASE | EP-CAM | COLORECTAL-CANCER | C-MYC | CELL-PROLIFERATION | BETA-CATENIN | CELL BIOLOGY | ADAM17 Protein | NIH 3T3 Cells | Cell Adhesion Molecules - genetics | Colonic Neoplasms - genetics | Cell Proliferation | Active Transport, Cell Nucleus - physiology | Homeodomain Proteins - metabolism | Humans | Lymphoid Enhancer-Binding Factor 1 - genetics | Male | Presenilin-2 - metabolism | Cell Membrane - genetics | Colonic Neoplasms - metabolism | Epithelial Cell Adhesion Molecule | Cell Nucleus - metabolism | Cell Transformation, Neoplastic - genetics | Muscle Proteins - metabolism | Antigens, Neoplasm - metabolism | Cell Membrane - metabolism | Protein Structure, Tertiary | Antigens, Neoplasm - genetics | Transcription Factors - genetics | Cell Adhesion Molecules - metabolism | Cell Transformation, Neoplastic - metabolism | Lymphoid Enhancer-Binding Factor 1 - metabolism | beta Catenin - metabolism | Homeodomain Proteins - genetics | beta Catenin - genetics | Muscle Proteins - genetics | Transcription Factors - metabolism | ADAM Proteins - metabolism | Animals | Cell Nucleus - genetics | Mitosis - physiology | Carcinoma - genetics | LIM-Homeodomain Proteins | Signal Transduction - physiology | Mice | Carcinoma - metabolism | Tumor antigens | Physiological aspects | Genetic aspects | Research | Health aspects | Cell adhesion molecules | Membrane proteins | Index Medicus
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 3/2004, Volume 164, Issue 5, pp. 769 - 779
All ligands of the epidermal growth factor receptor (EGFR), which has important roles in development and disease, are released from the membrane by proteases.... 
EGF receptor | Growth factor signaling | EGF receptor ligands | ADAMs | Ectodomain shedding | CELLS | ectodomain shedding | HB-EGF | TACE | PROTEIN-COUPLED RECEPTORS | ALPHA-CONVERTING-ENZYME | growth factor signaling | MICE LACKING | FAMILY | CELL BIOLOGY | EPIDERMAL-GROWTH-FACTOR | TGF-ALPHA | METALLOPROTEASE-DISINTEGRIN | ADAM17 Protein | Metalloendopeptidases - genetics | Phenylalanine - analogs & derivatives | Glycoproteins - metabolism | Metalloendopeptidases - metabolism | Thiophenes - metabolism | Epiregulin | Amphiregulin | Disintegrins - genetics | ADAM12 Protein | Intercellular Signaling Peptides and Proteins - metabolism | Receptor, Epidermal Growth Factor - metabolism | EGF Family of Proteins | Embryo, Mammalian - anatomy & histology | Aspartic Acid Endopeptidases | Amyloid Precursor Protein Secretases | Muscle Proteins - metabolism | Membrane Proteins - metabolism | Transforming Growth Factor alpha - metabolism | Fibroblasts - metabolism | Tetradecanoylphorbol Acetate - metabolism | Protein Structure, Tertiary | Endopeptidases - metabolism | Phenylalanine - metabolism | Disintegrins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Epidermal Growth Factor - metabolism | Genotype | Protease Inhibitors - metabolism | ADAM Proteins | Mice, Knockout | Muscle Proteins - genetics | Heparin-binding EGF-like Growth Factor | Animals | Endopeptidases - genetics | Betacellulin | Ligands | Fibroblasts - cytology | Mice | Cytology | Research | Proteins | Enzymes | Cellular biology | Rodents | Index Medicus | EGF receptor; EGF receptor ligands; ADAMs; ectodomain shedding; growth factor signaling
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2010, Volume 107, Issue 30, pp. 13473 - 13478
Staphylococcus aureus α-hemolysin (Hla), a potent cytotoxin, plays an important role in the pathogenesis of staphylococcal diseases, including those caused by... 
Receptors | Epithelial cells | Cell lines | Erythrocytes | Small interfering RNA | Cytotoxicity | Toxins | Cell membranes | Focal adhesions | Staphylococcus aureus | Cellular receptor | Pore-forming cytotoxin | CELLS | INFECTIONS | TYROSINE PHOSPHORYLATION | PROTECTION | pore-forming cytotoxin | TOXIN | MULTIDISCIPLINARY SCIENCES | P130(CAS) | MURINE MODEL | ERYTHROCYTES | PORE | BINDING | cellular receptor | Amyloid Precursor Protein Secretases - genetics | Epithelial Cells - metabolism | Hemolysin Proteins - pharmacology | Staphylococcus aureus - physiology | Hemolysin Proteins - genetics | Humans | Focal Adhesions | Molecular Sequence Data | Immunoblotting | RNA Interference | Membrane Proteins - metabolism | Staphylococcus aureus - metabolism | Staphylococcus aureus - genetics | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Rabbits | Membrane Proteins - genetics | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | ADAM10 Protein | Epithelial Cells - pathology | Host-Pathogen Interactions | Integrin beta1 - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Bacterial Proteins - pharmacology | Animals | Epithelial Cells - microbiology | Erythrocytes - metabolism | Cell Line, Tumor | Protein Binding | Bacterial Proteins - metabolism | Mutation | ADAM Proteins - genetics | Integrin beta1 - genetics | Hemolysin Proteins - metabolism | Index Medicus | Biological Sciences
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3145 - 3157
A disintegrin and metalloprotease 10 (ADAM10) is a ubiquitously expressed transmembrane metalloprotease that cleaves the extracellular regions from its... 
ACTIVATION | ANGIOGENESIS | endothelial cell | INTEGRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | CELL-SURFACE | shedding | cell surface enzyme | ADAM | ADHESION | MICRODOMAINS | TspanC8 | N-cadherin | tetraspanin | platelet | COMPONENT | metalloprotease | GPVI | DOMAINS | EXPRESSION | Endothelium, Vascular - cytology | Amyloid Precursor Protein Secretases - genetics | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Tetraspanins - chemistry | Substrate Specificity | Recombinant Fusion Proteins - metabolism | Blood Platelets - cytology | Proteolysis | Human Umbilical Vein Endothelial Cells - cytology | Surface Properties | Cell Membrane - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Tetraspanins - genetics | Tetraspanins - metabolism | Peptide Fragments - genetics | Tetraspanin-29 - chemistry | Cell Line | Peptide Fragments - metabolism | ADAM Proteins - chemistry | Membrane Proteins - genetics | Cells, Cultured | ADAM10 Protein | Recombinant Fusion Proteins - chemistry | Amyloid Precursor Protein Secretases - chemistry | Protein Transport | Cell Membrane - enzymology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Peptide Fragments - chemistry | Animals | Membrane Proteins - chemistry | Blood Platelets - metabolism | Endothelium, Vascular - metabolism | Mice | Protein Processing, Post-Translational | Enzyme Activation | ADAM Proteins - genetics | Tetraspanin-29 - metabolism | Tetraspanin-29 - genetics | Index Medicus | Cell Biology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2011, Volume 286, Issue 38, pp. 33335 - 33344
Journal Article
Nature Neuroscience, ISSN 1097-6256, 05/2012, Volume 15, Issue 5, pp. 713 - 721
The Huntington's disease gene product, huntingtin, is indispensable for neural tube formation, but its role is obscure. We studied neurulation in htt-null... 
TARGETED DISRUPTION | ZEBRAFISH | LACKING HUNTINGTIN | EMBRYONIC STEM-CELLS | MUTANT HUNTINGTIN | ADAM10 | MICE | DISEASE GENE HOMOLOG | WILD-TYPE HUNTINGTIN | NEUROSCIENCES | N-CADHERIN CLEAVAGE | Body Patterning - drug effects | Guanylate Kinases - genetics | Amyloid Precursor Protein Secretases - genetics | RNA, Small Interfering - genetics | Wnt1 Protein - genetics | Brain - embryology | PAX2 Transcription Factor - metabolism | Cadherins - metabolism | Apoptosis - drug effects | Embryo, Mammalian | Hedgehog Proteins - metabolism | Apoptosis - genetics | Green Fluorescent Proteins - genetics | Brain - metabolism | NFI Transcription Factors - metabolism | Cadherins - genetics | Tissue Inhibitor of Metalloproteinase-1 - pharmacology | Discs Large Homolog 1 Protein | Membrane Proteins - genetics | Gene Expression Regulation, Developmental - drug effects | PAX2 Transcription Factor - genetics | Cell Adhesion - drug effects | Mutation - genetics | Biological Evolution | Brain - drug effects | Huntingtin Protein | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Analysis of Variance | Membrane Proteins - antagonists & inhibitors | Cell Adhesion - physiology | Embryo, Nonmammalian | Guanylate Kinases - metabolism | Neuroepithelial Cells - physiology | Mice | Zebrafish Proteins - genetics | ADAM Proteins - genetics | Cerebral Ventricles - cytology | Drosophila melanogaster | Neuroepithelial Cells - drug effects | Embryonic Stem Cells - metabolism | Nestin | Immunoprecipitation | Gene Expression Regulation, Developmental - genetics | Wnt1 Protein - metabolism | Zebrafish - embryology | Cell Differentiation - genetics | Transfection | Hedgehog Proteins - genetics | Intermediate Filament Proteins - genetics | Neurons - physiology | Membrane Proteins - metabolism | Cerebral Ventricles - embryology | Neurons - drug effects | Nuclear Proteins - genetics | Hydroxamic Acids - pharmacology | Green Fluorescent Proteins - metabolism | Brain - cytology | ADAM Proteins - antagonists & inhibitors | Animals, Genetically Modified | Zebrafish Proteins - metabolism | Dipeptides - pharmacology | Cells, Cultured | ADAM10 Protein | Morpholines - pharmacology | Nuclear Proteins - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Animals | Dictyostelium | Embryonic Stem Cells - drug effects | Cell Differentiation - drug effects | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Body Patterning - genetics | Huntington's chorea | Physiological aspects | Cadherins | Genetic aspects | Research | Embryonic stem cells | Risk factors | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2006, Volume 313, Issue 5794, pp. 1792 - 1795
Journal Article
Journal Article
International Journal of Cancer, ISSN 0020-7136, 10/2013, Volume 133, Issue 7, pp. 1557 - 1566
The interaction of the MHC class I-related chain molecules A and B (MICA and MICB) with the corresponding natural killer group 2, member D (NKG2D) receptor... 
ADAM10 | ADAM17 | shedding | NKG2D ligands | MICA | MICB | ACTIVATION | CANCER | CUTTING EDGE | RECEPTOR NKG2D | NK CELLS | ONCOLOGY | ENGAGEMENT | SOLUBLE MICA | CYTOTOXICITY | T-CELLS | ADAM17 Protein | Immunologic Surveillance | Neoplasms - metabolism | T-Lymphocyte Subsets - immunology | Amyloid Precursor Protein Secretases - genetics | Prostatic Neoplasms - metabolism | Pancreatic Neoplasms - metabolism | Breast Neoplasms - immunology | Humans | Carcinoma, Pancreatic Ductal - metabolism | Male | Exosomes | Breast Neoplasms - metabolism | Prostatic Neoplasms - immunology | Histocompatibility Antigens Class I - metabolism | NK Cell Lectin-Like Receptor Subfamily K - metabolism | RNA Interference | Killer Cells, Natural - immunology | Female | Membrane Proteins - metabolism | Carcinoma, Pancreatic Ductal - immunology | Tumor Escape - immunology | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Dipeptides - pharmacology | Histocompatibility Antigens Class I - immunology | ADAM10 Protein | Matrix Metalloproteinase Inhibitors - pharmacology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - antagonists & inhibitors | Neoplasms - immunology | Pancreatic Neoplasms - immunology | Cell Line, Tumor | RNA, Small Interfering | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Tetraspanin-29 - metabolism | Cytokines - biosynthesis | T cells | Proteases | Analysis | Enzyme-linked immunosorbent assay | Tumors | Ligands | Immunology | Immune system | Index Medicus | ADAM10 protein
Journal Article
13.