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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 | Cell Biology
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 5/2016, Volume 73, Issue 9, pp. 1895 - 1915
The metalloprotease ADAM10 mediates the shedding of the ectodomain of various cell membrane proteins, including APP, the precursor of the amyloid peptide Aβ,... 
Life Sciences | Biochemistry, general | Life Sciences, general | Microdomain | Membrane compartmentalization | Notch | ADAM10 | Biomedicine general | Cell Biology | Tetraspanin | Ectodomain shedding | ALPHA-SECRETASE | MAJOR CD9 | CD151 | CD81 | INTEGRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEOLYTIC ACTIVATION | COMPLEXES | CELL BIOLOGY | EPIDERMAL-GROWTH-FACTOR | ENDOTHELIAL-CELLS | PROTEINS | Amyloid Precursor Protein Secretases - genetics | Immunoprecipitation | Cadherins - metabolism | Humans | Substrate Specificity | Chromatography, High Pressure Liquid | Membrane Proteins - analysis | Tandem Mass Spectrometry | RNA Interference | ADAM Proteins - analysis | Amyloid beta-Protein Precursor - metabolism | Hyaluronan Receptors - metabolism | Membrane Proteins - metabolism | Tetraspanins - genetics | Tetraspanins - metabolism | Membrane Proteins - genetics | ADAM10 Protein | Amyloid Precursor Protein Secretases - analysis | Receptor, Notch1 - metabolism | Microscopy, Confocal | Tetraspanins - antagonists & inhibitors | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Cell Line, Tumor | ADAM Proteins - genetics | Receptor, Notch1 - genetics | RNA, Small Interfering - metabolism | Peptides | Analysis | Resveratrol | Membrane proteins | Proteins | Cytokines | Mass spectrometry | Endoplasmic reticulum | Cellular Biology | Original
Journal Article
Journal Article
Protein Expression and Purification, ISSN 1046-5928, 07/2017, Volume 135, pp. 8 - 15
The human tetraspanin family of scaffold proteins comprises 33 isoforms. Being integral membrane proteins, they organize a so-called tetraspanin web via... 
Expression screening | Dictyostelium | Protein-protein interaction | Folding | Tetraspanin | Heterologous expression | MAJOR CD9 | CD81 | INTEGRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | HEPATITIS-C-VIRUS | EXTRACELLULAR DOMAIN | STRUCTURAL BASIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MEMBRANE-PROTEIN OVEREXPRESSION | TGF-ALPHA | SUPERFAMILY | ASSOCIATION | Tetraspanin 24 - genetics | Tetraspanin 28 - chemistry | Antibodies - chemistry | Humans | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Flow Cytometry | Protein Isoforms - metabolism | Tetraspanin 24 - chemistry | Protein Isoforms - chemistry | Cloning, Molecular | Tetraspanin 28 - genetics | Transgenes | Tetraspanin-29 - chemistry | Green Fluorescent Proteins - metabolism | Gene Expression | Tetraspanin 24 - metabolism | Recombinant Fusion Proteins - chemistry | Protein Folding | Animals | High-Throughput Screening Assays | Dictyostelium - genetics | Recombinant Fusion Proteins - genetics | Tetraspanin 28 - metabolism | Protein Conformation | Dictyostelium - metabolism | Tetraspanin-29 - metabolism | Tetraspanin-29 - genetics | Protein Isoforms - genetics | Tyrosine | Evaluation | Codon | Viral proteins | Proteases | Fluorescence | Protein-protein interactions | Membrane proteins | Integrins | Aquaporins
Journal Article
JOURNAL OF VIROLOGY, ISSN 0022-538X, 05/2018, Volume 92, Issue 10, pp. e01982 - 17
Hepatitis C virus (HCV) infection causes 500,000 deaths annually, in association with end-stage liver diseases. Investigations of the HCV life cycle have... 
PROTEIN-KINASE-A | piperazinylbenzenesulfonamide | RNA REPLICATION | INFECTION ASSAY | MAP KINASE | SEROTONIN RECEPTORS | virus-host interaction | TIGHT JUNCTIONS | VIROLOGY | CELL-CULTURE SYSTEMS | tight junction protein | SIGNALING PATHWAY | HUMAN HEPATOCYTES | IN-VIVO | hepatitis C virus | virus entry | protein kinase A | Cyclic AMP-Dependent Protein Kinases - metabolism | Tight Junctions - metabolism | Receptors, G-Protein-Coupled - metabolism | Humans | Protein Transport - drug effects | Sulfonamides - pharmacology | Virus Internalization - drug effects | Piperazines - pharmacology | Receptors, Serotonin - metabolism | Isoquinolines - pharmacology | Claudin-1 - metabolism | Cell Line, Tumor | Hepatocytes - virology | Tetraspanin 28 - metabolism | Hepacivirus - physiology | Protein Kinase Inhibitors - pharmacology | Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors | Hepatocytes/virology | Protein Transport/drug effects | Cyclic AMP-Dependent Protein Kinases/metabolism | Claudin-1/metabolism | Cellular Biology | Life Sciences | Tight Junctions/metabolism | Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors | Isoquinolines/pharmacology | Tetraspanin 28/metabolism | Virus Internalization/drug effects | Pharmaceutical sciences | Hépatology and Gastroenterology | Receptors, Serotonin/metabolism | Piperazines/pharmacology | Pharmacology | Hepacivirus/physiology | Virology | Microbiology and Parasitology | Human health and pathology | Sulfonamides/pharmacology | Infectious diseases | Receptors, G-Protein-Coupled/metabolism | Protein Kinase Inhibitors/pharmacology
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2013, Volume 288, Issue 36, pp. 26323 - 26334
Journal Article
Neuron, ISSN 0896-6273, 03/2012, Volume 73, Issue 6, pp. 1143 - 1158
Mutations in TSPAN7—a member of the tetraspanin protein superfamily—are implicated in some forms of X-linked intellectual disability. Here we show that TSPAN7... 
DENDRITIC SPINES | GLUTAMATE RECEPTORS | MENTAL-RETARDATION | TRANSMEMBRANE 4 SUPERFAMILY | KINASE-C-ALPHA | RECEPTOR TRAFFICKING | PICK1 | ACTIVITY-DEPENDENT REGULATION | HIPPOCAMPAL-NEURONS | NEUROSCIENCES | TETRASPANIN PROTEINS | Disks Large Homolog 4 Protein | Electric Stimulation | Embryo, Mammalian | Humans | Green Fluorescent Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Protein Transport - drug effects | Synapses - genetics | Long-Term Potentiation - drug effects | Time Factors | Tetraspanins - genetics | Excitatory Postsynaptic Potentials - genetics | Receptors, AMPA - metabolism | Dendritic Spines - physiology | Gene Expression Regulation, Developmental - drug effects | Rats | Protein Transport - genetics | Hydrazones - pharmacology | Microscopy, Confocal | Patch-Clamp Techniques | Analysis of Variance | RNA, Small Interfering - metabolism | Immunoprecipitation | Cercopithecus aethiops | Gene Expression Regulation, Developmental - genetics | Excitatory Postsynaptic Potentials - drug effects | Pseudopodia - drug effects | Transfection | Dendritic Spines - drug effects | Neurons - physiology | Membrane Proteins - metabolism | Tetraspanins - metabolism | Green Fluorescent Proteins - metabolism | Synapses - physiology | RNA, Small Interfering - pharmacology | Cells, Cultured | Nuclear Proteins - metabolism | Long-Term Potentiation - genetics | Biophysics | Hippocampus - cytology | Nerve Tissue Proteins - genetics | Integrin beta1 - metabolism | Nerve Tissue Proteins - metabolism | Two-Hybrid System Techniques | Animals | Carrier Proteins - metabolism | Pseudopodia - genetics | Dendritic Spines - genetics | In Vitro Techniques | Neurons | Neurosciences | Proteins | Brain | Brain research | Mutation | Rodents | alpha -Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors | Head | Synaptogenesis | X chromosome | Pseudopodia | Embryos | Mental retardation | Dendritic spines | Development | Glutamatergic transmission | Protein transport | Hippocampus | Synapses
Journal Article