Role of the Juxtamembrane Domains of the Transforming Growth Factor-α Precursor and the β-Amyloid Precursor Protein in Regulated Ectodomain Shedding
Open Access
- 1 July 1997
- journal article
- Published by Elsevier BV
- Vol. 272 (27), 17160-17165
- https://doi.org/10.1074/jbc.272.27.17160
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Diverse Cell Surface Protein Ectodomains Are Shed by a System Sensitive to Metalloprotease InhibitorsPublished by Elsevier BV ,1996
- Length of the Linking Domain of Human pro-Tumor Necrosis Factor Determines the Cleavage ProcessingBiochemistry, 1996
- Mutational analysis of the membrane-proximal cleavage site of L-selectin: relaxed sequence specificity surrounding the cleavage site.The Journal of Experimental Medicine, 1995
- Transforming growth factor-alpha and beta-amyloid precursor protein share a secretory mechanism.The Journal of cell biology, 1995
- Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processingNature, 1994
- Circulating adhesion molecules in diseaseImmunology Today, 1993
- The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGFα into soluble growth factorCell, 1992
- Membrane proteins with soluble counterparts: role of proteolysis in the release of transmembrane proteinsBiochemistry, 1991
- Evidence that β-Amyloid Protein in Alzheimer's Disease Is Not Derived by Normal ProcessingScience, 1990
- Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta.The Journal of cell biology, 1989