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1. Full Text TspanC8 tetraspanins and a disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: Evidence for distinct binding mechanisms for different TspanC8 proteins
by Noy, Peter J and Yang, Jing and Reyat, Jasmeet S and Matthews, Alexandra L and Charlton, Alice E and Furmston, Joanna and Rogers, David A and Ed Rainger, G and Tomlinson, Michael G
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
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2. Full Text Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease
by Marcello, Elena and Saraceno, Claudia and Musardo, Stefano and Vara, Hugo and De La Fuente, Alerie Guzman and Pelucchi, Silvia and Di Marino, Daniele and Borroni, Barbara and Tramontano, Anna and Pérez-Otaño, Isabel and Padovani, Alessandro and Giustetto, Maurizio and Gardoni, Fabrizio and Di Luca, Monica
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
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3. Full Text Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage In trans
by Janes, Peter W and Saha, Nayanendu and Barton, William A and Kolev, Momchil V and Wimmer-Kleikamp, Sabine H and Nievergall, Eva and Blobel, Carl P and Himanen, Juha-Pekka and Lackmann, Martin and Nikolov, Dimitar B
Cell, ISSN 0092-8674, 2005, Volume 123, Issue 2, pp. 291 - 304
The Eph family of receptor tyrosine kinases and their ephrin ligands are mediators of cell-cell communication. Cleavage of ephrin-A2 by the ADAM10 membrane... 
CONTACT | DISINTEGRIN | ROLES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | REPULSION | ALPHA-CONVERTING-ENZYME | CELL-ADHESION | ENDOCYTOSIS | PROTEASE | CELL BIOLOGY | Ephrin-A2 - metabolism | Ephrin-A3 - metabolism | Ephrin-A5 - metabolism | Humans | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Phylogeny | Receptor, EphA3 - metabolism | RNA Interference | Disulfides - chemistry | Amyloid Precursor Protein Secretases | Conserved Sequence | Membrane Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Green Fluorescent Proteins - metabolism | Protein Structure, Secondary | ADAM Proteins - chemistry | Membrane Proteins - genetics | ADAM10 Protein | Models, Molecular | Cysteine - chemistry | Blotting, Western | Precipitin Tests | Protein Folding | Ephrin-A3 - chemistry | Hydrolysis | Sequence Homology, Amino Acid | Microscopy, Confocal | ADAM Proteins - metabolism | Ephrin-A5 - chemistry | Membrane Proteins - chemistry | Mutagenesis | Cell Line, Tumor | Ligands | ADAM Proteins - genetics | RNA, Small Interfering - metabolism | Genetic research | Cysteine proteinases | Research | Proteolysis | Tyrosine | Phosphotransferases | Switches | Index Medicus
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4. Full Text A new paradigm for enzymatic control of α-cleavage and β-cleavage of the prion protein
by McDonald, Alex J and Dibble, Jessie P and Evans, Eric G. B and Millhauser, Glenn L
Journal of Biological Chemistry, ISSN 0021-9258, 01/2014, Volume 289, Issue 2, pp. 803 - 813
The cellular form of the prion protein (PrPC) is found in both full-length and several different cleaved forms in vivo. Although the precise functions of the... 
AMINO-TERMINUS | OXIDATIVE STRESS | DOMAIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | TERMINAL FRAGMENT | COPPER-BINDING | SCRAPIE PRION | ZINC | BRAIN | ADAM17 Protein | Amyloid Precursor Protein Secretases - genetics | Reactive Oxygen Species - metabolism | Zinc - metabolism | Humans | Zinc - chemistry | PrPC Proteins - chemistry | Copper - chemistry | Proteolysis | Mass Spectrometry | Copper - metabolism | Chromatography, Liquid | Membrane Proteins - metabolism | PrPC Proteins - metabolism | PrPC Proteins - genetics | Peptide Fragments - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Oxidation-Reduction | Membrane Proteins - genetics | ADAM10 Protein | Models, Molecular | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Peptide Fragments - chemistry | Animals | Mice | ADAM Proteins - genetics | Index Medicus | Protein Structure and Folding | ADAM | Prion Protein Proteolysis | Neurodegeneration | Enzyme | Prions | Metalloproteinase | Alzheimer Disease | Copper | Zinc
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5. Full Text Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10
by Caescu, Cristina I and Jeschke, Grace R and Turk, Benjamin E
Biochemical Journal, ISSN 0264-6021, 11/2009, Volume 424, Issue 1, pp. 79 - 88
The metalloproteinases TACE [turnout necrosis factor alpha-conventing enzyme; also known as ADAM17 (a disintegrin and metalloproteinase 17)] and ADAM10 are the... 
Peptide library | Tumour necrosis factor | Metalloproteinase | Disintegrin | Enzyme specificity | Ectodomain shedding | CONVERTING-ENZYME TACE | FACTOR-RECEPTOR | enzyme specificity | L-SELECTIN | ectodomain shedding | metalloproteinase | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE | NECROSIS-FACTOR-ALPHA | MATRIX METALLOPROTEINASES | STRUCTURAL REQUIREMENTS | GROWTH-FACTOR-ALPHA | peptide library | MEMBRANE-PROXIMAL CLEAVAGE | disintegrin | tumour necrosis factor | GAMMA-SECRETASE | ADAM17 Protein | Recombinant Proteins - metabolism | Amyloid Precursor Protein Secretases - genetics | Cell Line | Protein Binding - genetics | ADAM Proteins - chemistry | Membrane Proteins - genetics | Humans | Catalytic Domain - genetics | Tumor Necrosis Factors - metabolism | ADAM10 Protein | Recombinant Proteins - chemistry | Substrate Specificity | Recombinant Proteins - genetics | Binding Sites - genetics | Amyloid Precursor Protein Secretases - chemistry | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Membrane Proteins - chemistry | Mutagenesis | Membrane Proteins - metabolism | ADAM Proteins - genetics | Index Medicus
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6. Full Text Inside-out regulation of ectodomain cleavage of cluster-of-differentiation-44 (CD44) and of neuregulin-1 requires substrate dimerization
by Hartmann, Monika and Parra, Liseth M and Ruschel, Anne and Lindner, Christina and Morrison, Helen and Herrlich, Andreas and Herrlich, Peter
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
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7. Full Text Endoproteolytic processing of the mammalian prion glycoprotein family
by Mays, Charles E and Coomaraswamy, Janaky and Watts, Joel C and Yang, Jing and Ko, Kerry W.S and Strome, Bob and Mercer, Robert C.C and Wohlgemuth, Serene L and Schmitt-Ulms, Gerold and Westaway, David
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
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8. Full Text Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10
by Wei Deng and Sungyun Cho and Pin-Chuan Su and Bryan W. Berger and Renhao Li
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
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9. Full Text LC-MS based cleavage site profiling of the proteases ADAM10 and ADAM17 using proteome-derived peptide libraries
by Tucher, Joanna and Linke, Dennis and Koudelka, Tomas and Cassidy, Liam and Tredup, Claudia and Wichert, Rielana and Pietrzik, Claus and Becker-Pauly, Christoph and Tholey, Andreas
Journal of Proteome Research, ISSN 1535-3893, 04/2014, Volume 13, Issue 4, pp. 2205 - 2214
A Disintegrin and Metalloproteinase 10 (ADAM10) and ADAM17 catalyze ectodomain shedding of a number of cell surface proteins important for embryonic... 
ADAM17 | MALDI MS | peptide library | cleavage site specificity | ADAM10 | ESI MS | TMT | PICS | Q-PICS | DISINTEGRIN-METALLOPROTEASE | ACTIVE-SITE | MS/MS ANALYSIS | PRODOMAIN | BIOCHEMICAL RESEARCH METHODS | TACE | RECEPTOR | ALPHA-CONVERTING-ENZYME | DATABASE | INHIBITORS | SELECTIVITY | ADAM17 Protein | Peptide Fragments - metabolism | ADAM Proteins - chemistry | Humans | ADAM10 Protein | Amyloid Precursor Protein Secretases - analysis | Peptide Library | Proteome - analysis | Proteome - chemistry | Amyloid Precursor Protein Secretases - chemistry | Membrane Proteins - analysis | Peptide Fragments - analysis | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Peptide Fragments - chemistry | Animals | Membrane Proteins - chemistry | ADAM Proteins - analysis | Mass Spectrometry | Chromatography, Liquid | Membrane Proteins - metabolism | Mice | Proteomics - methods | Proteome - metabolism | Index Medicus
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10. Full Text Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 Mitogen-activated Protein Kinase (MAPK)
by Thorp, Edward and Vaisar, Tomas and Subramanian, Manikandan and Mautner, Lauren and Blobel, Carl and Tabas, Ira
Journal of Biological Chemistry, ISSN 0021-9258, 09/2011, Volume 286, Issue 38, pp. 33335 - 33344
Mer tyrosine kinase (MerTK) is an integral membrane protein that is preferentially expressed by phagocytic cells, where it promotes efferocytosis and inhibits... 
TUMOR-NECROSIS-FACTOR | EXPRESSION ANALYSIS | SOLUBLE FORM | BIOCHEMISTRY & MOLECULAR BIOLOGY | APOPTOTIC CELLS | ALPHA-CONVERTING-ENZYME | TNF-ALPHA | NF-KAPPA-B | POTENTIAL ROLE | ARREST-SPECIFIC GENE | CUTTING EDGE | ADAM17 Protein | Solubility - drug effects | Sequence Deletion | Reactive Oxygen Species - metabolism | Proline - metabolism | Molecular Sequence Data | Adaptor Proteins, Vesicular Transport - metabolism | NADP - deficiency | Protein Processing, Post-Translational - drug effects | Mass Spectrometry | c-Mer Tyrosine Kinase | p38 Mitogen-Activated Protein Kinases - metabolism | NADP - metabolism | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | ADAM Proteins - chemistry | Mice, Inbred C57BL | Receptor Protein-Tyrosine Kinases - metabolism | Toll-Like Receptor 4 - metabolism | Protein Kinase C-delta - metabolism | ADAM Proteins - metabolism | Animals | Signal Transduction - drug effects | Lipopolysaccharides - pharmacology | Mice | Myeloid Differentiation Factor 88 - metabolism | Index Medicus | Shedding | ADAM ADAMTS | PKCdelta | ROS | TACE | Efferocytosis | Macrophages | MerTK | Phagocytosis | Cell Biology | Lipopolysaccharide (LPS)
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11. Full Text Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx
by Horiuchi, Keisuke and Le Gall, Sylvain and Schulte, Marc and Yamaguchi, Takafumi and Reiss, Karina and Murphy, Gillian and Toyama, Yoshiaki and Hartmann, Dieter and Saftig, Paul and Blobel, Carl P
Molecular Biology of the Cell, ISSN 1059-1524, 01/2007, Volume 18, Issue 1, pp. 176 - 188
Signaling via the epidermal growth factor receptor (EGFR), which has critical roles in development and diseases such as cancer, is regulated by proteolytic... 
CANCER-CELLS | PROTEIN | TUMOR PROGRESSION | HB-EGF | ECTODOMAIN | TACE | CELL-SURFACE | ALPHA-CONVERTING-ENZYME | PROTGF-ALPHA | POTENTIAL ROLE | CELL BIOLOGY | ADAM17 Protein | Tetradecanoylphorbol Acetate - pharmacology | Calcium - metabolism | Glycoproteins - metabolism | Cercopithecus aethiops | Epiregulin | Amphiregulin | Recombinant Fusion Proteins - metabolism | Intercellular Signaling Peptides and Proteins - metabolism | Membrane Proteins - deficiency | Receptor, Epidermal Growth Factor - metabolism | EGF Family of Proteins | Transforming Growth Factor alpha - metabolism | Ionophores - pharmacology | ADAM Proteins - chemistry | ADAM Proteins - deficiency | ADAM10 Protein | Epidermal Growth Factor - metabolism | Amyloid Precursor Protein Secretases - chemistry | Heparin-binding EGF-like Growth Factor | ADAM Proteins - metabolism | Animals | Substrate Specificity - drug effects | Betacellulin | Membrane Proteins - chemistry | Amyloid Precursor Protein Secretases - deficiency | Ligands | Mice | COS Cells | Calmodulin - antagonists & inhibitors | Protein Structure, Tertiary - drug effects | Index Medicus
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12. Full Text Secreted Frizzled-related protein 3 (sFRP3)-mediated suppression of interleukin-6 receptor release by A disintegrin and metalloprotease 17 (ADAM17) is abrogated in the osteoarthritis-associated rare double variant of sFRP3
by Oldefest, Mirja and Öft, Stefan Düsterh and Desel, Christine and Thysen, Sarah and Fink, Christine and Rabe, Ö and Lories, Rik and Ötzinger, Joachim Gr and Lorenzen, Inken
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
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13. Full Text Secretion-Positive LGI1 Mutations Linked to Lateral Temporal Epilepsy Impair Binding to ADAM22 and ADAM23 Receptors
by Dazzo, Emanuela and Leonardi, Emanuela and Belluzzi, Elisa and Malacrida, Sandro and Vitiello, Libero and Greggio, Elisa and Tosatto, Silvio C. E and Nobile, Carlo
PLoS Genetics, ISSN 1553-7390, 10/2016, Volume 12, Issue 10, pp. e1006376 - e1006376
Autosomal dominant lateral temporal epilepsy (ADTLE) is a focal epilepsy syndrome caused by mutations in the LGI1 gene, which encodes a secreted protein. Most... 
ENCODES | LOW PENETRANCE | LIMBIC ENCEPHALITIS | PROTEIN | LGI1/EPITEMPIN GENE | LOBE EPILEPSY | FAMILIES | GENETICS & HEREDITY | LEUCINE-RICH REPEAT | AUTOSOMAL-DOMINANT | DOMINANT PARTIAL EPILEPSY | Epilepsy, Frontal Lobe - genetics | ADAM Proteins - chemistry | Humans | Cercopithecus aethiops | Cell Membrane - genetics | Mutation, Missense | Nerve Tissue Proteins - genetics | Epilepsy, Frontal Lobe - pathology | Protein Folding | Sleep Wake Disorders - genetics | Nerve Tissue Proteins - metabolism | Proteins - genetics | ADAM Proteins - metabolism | Nerve Tissue Proteins - chemistry | Animals | Protein Interaction Maps - genetics | Proteins - secretion | Sleep Wake Disorders - pathology | Amino Acid Substitution - genetics | Protein Conformation | Cell Membrane - metabolism | Proteins - chemistry | ADAM Proteins - genetics | COS Cells | Genetic aspects | Gene mutations | Health aspects | Epilepsy | Binding sites (Biochemistry) | Proteins | Neurosciences | Sodium | Protein folding | Funding | Genes | Colleges & universities | Biology | Mutation | Index Medicus
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