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Title
N-Glycosylation Regulates ADAM8 Processing and Activation
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 48, Pages 33676-33688
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2014-10-22
DOI
10.1074/jbc.m114.594242
References
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Related references
Note: Only part of the references are listed.- Glycosylation of a disintegrin and metalloprotease 17 affects its activity and inhibition
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- Secreted and Membrane-Bound Isoforms of Protease ADAM9 Have Opposing Effects on Breast Cancer Cell Migration
- (2010) J. L. Fry et al. CANCER RESEARCH
- Tumor Necrosis Factor- (TNF- ) Regulates Shedding of TNF- Receptor 1 by the Metalloprotease-Disintegrin ADAM8: Evidence for a Protease-Regulated Feedback Loop in Neuroprotection
- (2010) J. W. Bartsch et al. JOURNAL OF NEUROSCIENCE
- Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer
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- ADAM-8 isolated from human osteoarthritic chondrocytes cleaves fibronectin at Ala271
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- Overexpression of DPAGT1 Leads to Aberrant N-Glycosylation of E-Cadherin and Cellular Discohesion in Oral Cancer
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- ADAM8/MS2/CD156, an Emerging Drug Target in the Treatment of Inflammatory and Invasive Pathologies
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- Structural Characterization of the Ectodomain of a Disintegrin and Metalloproteinase-22 (ADAM22), a Neural Adhesion Receptor Instead of Metalloproteinase
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- Increased serum ADAM8 concentration in patients with drug-induced eosinophilic pneumonia-ADAM8 expression depends on a the allergen route of entry
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- Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme
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