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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
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 | Index Medicus | Cellular Biology | Original
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 | Index Medicus
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 | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, pp. E11827 - E11836
beta-Catenin signaling controls the development and maintenance of the blood-brain barrier (BBB) and the blood-retina barrier (BRB), but the division of labor... 
Vascular endothelial cells | β-catenin signaling | Central nervous system | Mouse genetics | VASCULAR DEVELOPMENT | FZD4 | MULTIDISCIPLINARY SCIENCES | mouse genetics | TSPAN12 | beta-catenin signaling | central nervous system | PROTEIN-COUPLED RECEPTOR | vascular endothelial cells | MUTATIONS | LIGAND | FAMILIAL EXUDATIVE VITREORETINOPATHY | CNS ANGIOGENESIS | RECK | GPR124 | Blood-Brain Barrier - cytology | Blood-Retinal Barrier - cytology | Nerve Tissue Proteins - deficiency | Tetraspanins - physiology | Wnt Proteins - deficiency | Blood-Retinal Barrier - growth & development | Wnt Proteins - genetics | Tetraspanins - deficiency | Blood-Brain Barrier - physiology | Blood-Brain Barrier - growth & development | beta Catenin - physiology | Cell Culture Techniques | Eye Proteins - genetics | Tetraspanins - genetics | Frizzled Receptors - deficiency | Nerve Tissue Proteins - physiology | Blood-Retinal Barrier - physiology | Signal Transduction | Proto-Oncogene Proteins - genetics | Frizzled Receptors - physiology | Proto-Oncogene Proteins - deficiency | Nerve Tissue Proteins - genetics | Mice, Knockout | Animals | Frizzled Receptors - genetics | Models, Biological | Proto-Oncogene Proteins - physiology | Eye Proteins - physiology | Mice | Wnt Proteins - physiology | Models, Neurological | Physiological aspects | Retina | Blood-brain barrier | Wnt proteins | Cerebellum | Brain | Phenotypes | Redundancy | Nervous system | Maintenance | Signalling systems | Blood | Endothelial cells | β-catenin | Heterogeneity | Receptors | Rodents | Barriers | Genetic analysis | Ligands | Vascular endothelial growth factor | Division of labor | Index Medicus | Biological Sciences | PNAS Plus
Journal Article
Oncology Reports, ISSN 1021-335X, 4/2015, Volume 33, Issue 4, pp. 1965 - 1975
Given its tumor-specific expression, including liver cancer, OY-TES-1 is a potential molecular marker for the diagnosis and immunotherapy of liver cancers.... 
OY-TES-1 | RNAi | bioinformatics | oligonucleotide microarray | CD9 | NANOG | liver cancer | Liver cancer | Bioinformatics | Oligonucleotide microarray | PROTEIN | CELL-CYCLE ARREST | PROLIFERATION | IDENTIFICATION | LUNG-CANCER | OVEREXPRESSION | ONCOLOGY | CANCER/TESTIS ANTIGENS | PROSTATE-CANCER | TETRASPANIN CD9 | GENE-EXPRESSION | Cyclin D2 - genetics | Oligonucleotide Array Sequence Analysis | Humans | Neoplasm Proteins - physiology | Gene Expression Regulation, Neoplastic | Transcriptome | Databases, Genetic | RNA, Messenger - biosynthesis | Carcinoma, Hepatocellular - genetics | Cell Division | Cyclin D2 - physiology | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Liver Neoplasms - pathology | RNA, Bacterial | Neoplasm Proteins - genetics | Carrier Proteins - physiology | Protein Structure, Tertiary | Homeodomain Proteins - biosynthesis | Nanog Homeobox Protein | Liver Neoplasms - genetics | Neoplasm Proteins - biosynthesis | Computational Biology | Neoplasm Proteins - chemistry | Cell Cycle Proteins - biosynthesis | Tetraspanin-29 - physiology | Cell Adhesion | Homeodomain Proteins - genetics | Amino Acid Motifs | Protein Interaction Mapping | Carrier Proteins - genetics | RNA, Neoplasm - biosynthesis | Carcinoma, Hepatocellular - pathology | Cyclin D2 - biosynthesis | Homeodomain Proteins - physiology | Cell Cycle Proteins - physiology | Tetraspanin-29 - genetics | Apoptosis | Cell Movement | Tetraspanin-29 - biosynthesis | Genetic markers | Oncology, Experimental | Genetic research | Development and progression | Genetic aspects | Research | Properties | Cancer | Antigens | Ontology | Cyclin-dependent kinases | Genomes | Gene expression | Kinases | Studies | Proteins | Online data bases | Cell growth | Annotations | Immunotherapy | Collagen | Cell cycle | Tumor necrosis factor-TNF | Index Medicus
Journal Article
Genes and Development, ISSN 0890-9369, 11/2013, Volume 27, Issue 21, pp. 2305 - 2319
Norrin is a cysteine-rich growth factor that is required for angiogenesis in the eye, ear, brain, and female reproductive organs. It functions as an atypical... 
Frizzled 4 | Wnt/β-catenin signaling | Cystine knot growth factor | Norrin structure | Low-density lipoprotein receptor-related protein 5/6 | Tetraspanin 12 | WNT SIGNALING PATHWAY | DOMAIN | PROTEIN | tetraspanin 12 | RETINAL VASCULAR DEVELOPMENT | DEVELOPMENTAL BIOLOGY | Wnt/beta-catenin signaling | CELL BIOLOGY | MOLECULAR RECOGNITION | GROWTH-FACTORS | DISEASE | VITREORETINOPATHY | GENETICS & HEREDITY | low-density lipoprotein receptor-related protein 5/6 | COUPLED SECRETIN RECEPTOR | OLIGOMERIZATION | cystine knot growth factor | Humans | Low Density Lipoprotein Receptor-Related Protein-5 - chemistry | Eye Proteins - chemistry | Crystallography, X-Ray | Transforming Growth Factor beta - chemistry | Low Density Lipoprotein Receptor-Related Protein-6 - chemistry | Nerve Tissue Proteins - chemistry | Frizzled Receptors - chemistry | HEK293 Cells | Maltose-Binding Proteins - chemistry | Eye Proteins - genetics | Protein Stability | Tetraspanins - metabolism | Binding Sites | Dimerization | Protein Structure, Tertiary | Signal Transduction | Frizzled Receptors - metabolism | Models, Molecular | Maltose-Binding Proteins - metabolism | Nerve Tissue Proteins - genetics | beta Catenin - metabolism | Nerve Tissue Proteins - metabolism | Low Density Lipoprotein Receptor-Related Protein-6 - metabolism | Animals | Eye Proteins - metabolism | Low Density Lipoprotein Receptor-Related Protein-5 - metabolism | Protein Binding | Mice | COS Cells | Index Medicus | low-density lipoprotein receptor-related protein 5 | 6 | β-catenin signaling | Research Paper | Wnt
Journal Article
FEBS Journal, ISSN 1742-464X, 01/2013, Volume 280, Issue 1, pp. 127 - 138
Journal Article
Journal Article