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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
Journal Article
Cold Spring Harbor Perspectives in Biology, ISSN 2157-1422, 10/2012, Volume 2, Issue 10, pp. a006296 - a006296
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2008, Volume 283, Issue 51, pp. 35507 - 35516
The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced... 
ALPHA-SECRETASE | RAGE RECEPTOR | MATRIX METALLOPROTEINASES | CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID PRECURSOR PROTEIN | BLOOD-BRAIN-BARRIER | SPLICE VARIANTS | MULTILIGAND RECEPTOR | EXPRESSION | SOLUBLE RECEPTOR | Amyloid Precursor Protein Secretases - genetics | RNA, Small Interfering - genetics | Tetradecanoylphorbol Acetate - pharmacology | Humans | Cell Membrane - genetics | Protease Inhibitors - pharmacology | Matrix Metalloproteinase 9 - metabolism | Carcinogens - pharmacology | Protein Isoforms - metabolism | Cell Membrane - metabolism | Diabetes Complications - genetics | Membrane Proteins - metabolism | Hydroxamic Acids - pharmacology | Receptor for Advanced Glycation End Products | Ionophores - pharmacology | Cell Line | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Alternative Splicing - genetics | Diabetes Complications - metabolism | ADAM10 Protein | Protein Structure, Tertiary - genetics | Calcimycin - pharmacology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Alternative Splicing - drug effects | Membrane Proteins - antagonists & inhibitors | Alzheimer Disease - metabolism | Matrix Metalloproteinase Inhibitors | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Alzheimer Disease - genetics | Receptors, Immunologic - genetics | Receptors, Immunologic - metabolism | Protein Isoforms - genetics | Index Medicus
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 06/2014, Volume 448, Issue 3, pp. 308 - 314
ADAM10, overexpressed in tongue squamous cell carcinoma (TSCC), has been well documented for its role in tumor progression and metastasis. In the present... 
ADAM10 | MicroRNA | Tongue squamous cell carcinoma | ERBB4 | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE | HISTONE-DEACETYLASE-7 | TRANSLATION | CLEAVAGE | BIOPHYSICS | ERBB4/HER4 | TARGETS | EXPRESSION | CARCINOMA | RECEPTOR TYROSINE KINASE | Paired Box Transcription Factors - genetics | Amyloid Precursor Protein Secretases - genetics | RNA, Small Interfering - genetics | Receptor, Epidermal Growth Factor - genetics | Cell Proliferation | Carcinoma, Squamous Cell - genetics | Carcinoma, Squamous Cell - metabolism | Carcinoma, Squamous Cell - pathology | Humans | Neoplasm Invasiveness - prevention & control | Gene Expression Regulation, Neoplastic | MicroRNAs - metabolism | RNA, Neoplasm - metabolism | Cell Movement - genetics | Neoplasm Invasiveness - pathology | Base Sequence | Membrane Proteins - metabolism | Eye Proteins - genetics | 3' Untranslated Regions | Genes, Tumor Suppressor | Tongue Neoplasms - metabolism | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Tongue Neoplasms - genetics | ADAM10 Protein | Repressor Proteins - genetics | PAX6 Transcription Factor | Tongue Neoplasms - pathology | Homeodomain Proteins - genetics | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - antagonists & inhibitors | Cell Line, Tumor | RNA, Neoplasm - genetics | MicroRNAs - genetics | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Neoplasm Invasiveness - genetics | Receptor, ErbB-4
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 | Biological Sciences
Journal Article
FASEB Journal, ISSN 0892-6638, 2014, Volume 28, Issue 2, pp. 978 - 997
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 27, pp. 23967 - 23974
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2017, Volume 292, Issue 15, pp. 6339 - 6351
We previously showed that the cell adhesion molecule Nectin-4 is overexpressed in ovarian cancer tumors, and its cleaved extracellular domain can be detected... 
BREAST-CANCER | CARCINOMA ASCITES SPHEROIDS | METALLOPROTEASE-17 ADAM17 | L-SELECTIN | GROWTH-FACTOR-RECEPTOR | LYSOPHOSPHATIDIC ACID | PERITONEAL MESOTHELIAL CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NECROSIS-FACTOR-ALPHA | TNF-ALPHA | CONVERTING-ENZYME | Amyloid Precursor Protein Secretases - genetics | Cell Adhesion Molecules - genetics | ADAM10 Protein - genetics | Humans | Ovarian Neoplasms - pathology | ADAM10 Protein - metabolism | Extracellular Signal-Regulated MAP Kinases - metabolism | RNA, Messenger - metabolism | Extracellular Signal-Regulated MAP Kinases - genetics | RNA, Neoplasm - metabolism | Proto-Oncogene Proteins c-akt - genetics | ADAM17 Protein - metabolism | Ovarian Neoplasms - genetics | Neoplasm Metastasis | MAP Kinase Signaling System - genetics | Protein Domains | Female | Membrane Proteins - metabolism | Ovarian Neoplasms - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Membrane Proteins - genetics | Proto-Oncogene Proteins c-jun - genetics | RNA, Messenger - genetics | Cell Adhesion Molecules - metabolism | ADAM17 Protein - genetics | Amyloid Precursor Protein Secretases - metabolism | Proto-Oncogene Proteins c-jun - metabolism | Cell Line, Tumor | RNA, Neoplasm - genetics | Nectin-4 | ADAM | ADAM17 | ovarian cancer | cell migration | ADAM10 | cancer biology | biomarker | Cell Biology
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 | Cell Biology
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 04/2010, Volume 30, Issue 14, pp. 4833 - 4844
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 11/2015, Volume 112, Issue 46, pp. 14337 - 14342
Journal Article
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 10/2012, Volume 199, Issue 3, pp. 481 - 496
Journal Article