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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 Clinical Investigation, ISSN 0021-9738, 06/2013, Volume 123, Issue 6, pp. 2523 - 2538
A disintegrin and metalloproteinase 10 (ADAM10), a disintegrin and metalloproteinase that resides in the postsynaptic densities (PSDs) of excitatory synapses,... 
ALPHA-SECRETASE | DENDRITIC SPINES | MEDICINE, RESEARCH & EXPERIMENTAL | GLUTAMATE RECEPTORS | IDENTIFIES VARIANTS | AMPA RECEPTORS | LONG-TERM DEPRESSION | A-BETA | CELL-SURFACE | AMYLOID PRECURSOR PROTEIN | GENOME-WIDE ASSOCIATION | Amyloid Precursor Protein Secretases - genetics | Humans | Cercopithecus aethiops | Molecular Sequence Data | Fatty Acid-Binding Proteins - metabolism | Alzheimer Disease - pathology | Endocytosis | Amyloid beta-Protein Precursor - metabolism | Hippocampus - enzymology | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Amino Acid Sequence | ADAM Proteins - chemistry | Membrane Proteins - genetics | ADAM10 Protein | Models, Molecular | Synapses - enzymology | Alzheimer Disease - enzymology | Amyloid Precursor Protein Secretases - chemistry | Long-Term Synaptic Depression | Amino Acid Motifs | Protein Interaction Mapping | Protein Transport | Cell Membrane - enzymology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Membrane Proteins - chemistry | Neuronal Plasticity | Long-Term Potentiation | Protein Binding | Fatty Acid-Binding Proteins - chemistry | Mice | ADAM Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | COS Cells | Neuroplasticity | Physiological aspects | Development and progression | Genetic aspects | Research | Metalloenzymes | Alzheimer's disease | Proteins | Software | Alzheimers disease | Experiments | Index Medicus | Abridged Index Medicus | Cell Membrane | Fatty Acid-Binding Proteins | Life Sciences | Neuroscience | Amyloid Precursor Protein Secretases | Cognitive science | Biochemistry, Molecular Biology | ADAM Proteins | Alzheimer Disease | Membrane Proteins | Adaptor Proteins, Signal Transducing | Hippocampus | Synapses | Amyloid beta-Protein Precursor
Journal Article
Cell, ISSN 0092-8674, 2005, Volume 123, Issue 2, pp. 291 - 304
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2015, Volume 290, Issue 28, pp. 17041 - 17054
Ectodomain shedding of transmembrane precursor proteins generates numerous life-essential molecules, such as epidermal growth factor receptor ligands. This... 
CARCINOMA-CELLS | GROWTH-FACTOR RECEPTOR | BREAST-CANCER CELLS | SIGNALING PATHWAYS | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSMEMBRANE DOMAIN | ALPHA-CONVERTING-ENZYME | NECROSIS-FACTOR-ALPHA | EGF RECEPTOR | LIGAND RELEASE | ADAM17 Protein | Amyloid Precursor Protein Secretases - genetics | NIH 3T3 Cells | Humans | Protein Multimerization | Substrate Specificity | Hyaluronan Receptors - chemistry | Neuregulin-1 - chemistry | Recombinant Fusion Proteins - metabolism | Neuregulin-1 - genetics | Cattle | Proteolysis | HEK293 Cells | Hyaluronan Receptors - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Protein Structure, Tertiary | Mutagenesis, Site-Directed | ADAM Proteins - chemistry | Membrane Proteins - genetics | Cells, Cultured | ADAM10 Protein | Rats | Recombinant Fusion Proteins - chemistry | Amyloid Precursor Protein Secretases - chemistry | Hyaluronan Receptors - genetics | Mice, Knockout | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Membrane Proteins - chemistry | Models, Biological | Neuregulin-1 - metabolism | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Mice | ADAM Proteins - genetics | Index Medicus | ADAM | actin | ADAM17 | Signal Transduction | adhesion molecule | angiotensin | neuregulin | ADAM10 | ezrin | metalloprotease
Journal Article
FEBS Journal, ISSN 1742-464X, 2014, Volume 281, Issue 3, pp. 862 - 876
Cellular prion protein (PrPC) misfolds to form infectivity-associated scrapie prion protein and generates C-terminal fragments C1 and C2 in healthy and... 
Doppel | ADAM | Shadoo | Prion protein | Endoproteolysis | ALPHA-CLEAVAGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ADAM10 | HUMAN DOPPEL | GENE | CELLULAR PRION | SHADOO PROTEINS | endoproteolysis | MICE | KNOCKOUT | EXPRESSION | prion protein | N-TERMINAL REGION | Testis - metabolism | Prions - genetics | Glycoproteins - metabolism | Brain - enzymology | Male | Recombinant Fusion Proteins - metabolism | PrPC Proteins - chemistry | Brain - metabolism | Nerve Tissue Proteins - chemistry | Proteolysis | Testis - enzymology | Neurons - metabolism | PrPC Proteins - metabolism | Glycoproteins - chemistry | PrPC Proteins - genetics | Peptide Fragments - genetics | Glycoproteins - genetics | Protein Structure, Tertiary | Cell Line | Endopeptidases - metabolism | Prions - metabolism | Rabbits | Peptide Fragments - metabolism | Mice, Transgenic | Mutant Proteins - metabolism | Glycosylation | Prions - chemistry | Recombinant Fusion Proteins - chemistry | Nerve Tissue Proteins - genetics | GPI-Linked Proteins - metabolism | Nerve Tissue Proteins - metabolism | Peptide Fragments - chemistry | Animals | GPI-Linked Proteins - chemistry | Mutant Proteins - chemistry | Neurons - enzymology | Mice | Protein Processing, Post-Translational | GPI-Linked Proteins - genetics | Gene mutations | Proteases | Prions | Glycoproteins | Cellular biology | Molecular biology | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 45, pp. 15987 - 15992
Intrinsically disordered protein regions are widely distributed in the cytoplasmic domains of many transmembrane receptors. The cytoplasmic domain of a... 
Proteins | Phosphorylation | Receptors | Micelles | Teeth | Fluorescence | Cell membranes | Dimers | Physiological regulation | Dimerization | Intrinsic disorder | ADAM10 | FRET | Membrane protein dimerization | L-SELECTIN | ACTIVATION | PHOSPHORYLATION | JUXTAMEMBRANE | TRYPSIN DIGESTION | MULTIDISCIPLINARY SCIENCES | TRANSMEMBRANE | INTERFACE | membrane protein dimerization | PROTEINS | ASSOCIATION | CONVERTING-ENZYME | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amyloid Precursor Protein Secretases - genetics | ADAM Proteins - chemistry | Membrane Proteins - genetics | Humans | ADAM10 Protein | Recombinant Proteins - chemistry | Cell Membrane - genetics | Recombinant Proteins - genetics | Escherichia coli - chemistry | Amyloid Precursor Protein Secretases - chemistry | Cell Membrane - chemistry | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Protein Multimerization - physiology | Escherichia coli - metabolism | Signal Transduction - physiology | Cell Membrane - metabolism | Membrane Proteins - metabolism | ADAM Proteins - genetics | Biological research | Physiological aspects | Research | Structure | Molecular biology | Cytoplasm | Membrane proteins | Biology, Experimental | Membranes | Cells | Index Medicus | Biological Sciences
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2011, Volume 286, Issue 38, pp. 33335 - 33344
Journal Article
Molecular Biology of the Cell, ISSN 1059-1524, 01/2007, Volume 18, Issue 1, pp. 176 - 188
Journal Article
Biochemical Journal, ISSN 0264-6021, 06/2015, Volume 468, Issue 3, pp. 507 - 518
To avoid malformation and disease, tissue development and homoeostasis are co-ordinated precisely in time and space. Secreted Frizzled-related protein 3... 
A disintegrin and metalloprotease 17 (ADAM17) | SNPs (single nucleotide polymorphisms) | Frizzled-related protein gene (FRZB) | Metalloprotease | Secreted Frizzled-related proteins (sFRPs) | Osteoarthritis | Interleukin-6 receptor (IL-6R) | Ectodomain shedding | DOMAIN | ectodomain shedding | CANCER CELLS | osteoarthritis | BIOCHEMISTRY & MOLECULAR BIOLOGY | secreted Frizzled-related proteins (sFRPs) | WNT ANTAGONIST | NECROSIS-FACTOR-ALPHA | interleukin-6 receptor (IL-6R) | INHIBITION | FRZB | SOLUBLE INTERLEUKIN-6 | HIP OSTEOARTHRITIS | metalloprotease | CONVERTING-ENZYME | SPEMANN ORGANIZER | ADAM17 Protein | Osteoarthritis, Hip - metabolism | Receptors, Interleukin-6 - chemistry | Up-Regulation | Humans | Proteins - secretion | HEK293 Cells | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Chondrocytes - secretion | Peptide Fragments - genetics | Chondrocytes - metabolism | Recombinant Proteins - metabolism | Genetic Predisposition to Disease | Peptide Fragments - metabolism | Mutagenesis, Site-Directed | ADAM Proteins - chemistry | Receptors, Interleukin-6 - genetics | Down-Regulation | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Osteoarthritis, Hip - genetics | Proteins - genetics | ADAM Proteins - metabolism | Peptide Fragments - chemistry | Proteins - metabolism | Mutant Proteins - chemistry | Cell Line, Tumor | Proteins - chemistry | ADAM Proteins - genetics | Amino Acid Substitution | Receptors, Interleukin-6 - metabolism | Index Medicus
Journal Article
Journal Article