Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure
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Amyloidosis in Retinal Neurodegenerative DiseasesCurrent and future implications of basic and translational research on amyloid-β peptide production and removal pathwaysADAM-17: the enzyme that does it all.Microarray analysis on human neuroblastoma cells exposed to aluminum, β(1-42)-amyloid or the β(1-42)-amyloid aluminum complex.An overview of APP processing enzymes and products.Induction of RAGE shedding by activation of G protein-coupled receptors.Structural and mechanistic commonalities of amyloid-β and the prion proteinADAM10 expression and promoter haplotype in Alzheimer's disease.The role of proteases in regulating Eph/ephrin signaling.The role and therapeutic targeting of α-, β- and γ-secretase in Alzheimer's diseaseHarnessing the natural inhibitory domain to control TNFα Converting Enzyme (TACE) activity in vivo.Amyloid-beta immunotherapy: the hope for Alzheimer disease?The Role of Shed PrPc in the Neuropathogenesis of HIV Infection.Regulation of Alpha-Secretase ADAM10 In vitro and In vivo: Genetic, Epigenetic, and Protein-Based Mechanisms.Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs.The role of zinc in Alzheimer's disease.Regulation of ADAM10 by miR-140-5p and potential relevance for Alzheimer's disease.
P2860
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P2860
Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure
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Alpha-secretase activity of th ...... Influences of domain structure
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Alpha-secretase activity of th ...... Influences of domain structure
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Alpha-secretase activity of th ...... Influences of domain structure
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2000-01-01T00:00:00Z