Transport to Endoplasmic Reticulum by Signal Peptide, but Not Proteolytic Processing, Is Required for Formation of Conformational Epitopes of Pemphigus Vulgaris Antigen (Dsg3)
- 1 October 1996
- journal article
- Published by Elsevier in Journal of Investigative Dermatology
- Vol. 107 (4), 539-542
- https://doi.org/10.1111/1523-1747.ep12582796
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Pemphigus Vulgaris Antigen (Desmoglein 3) Is Localized in the Lower Epidermis, the Site of Blister Formation in PatientsJournal of Investigative Dermatology, 1996
- Conformational Epitopes of Pemphigus Antigens (Dsg1 and Dsg3) Are Calcium Dependent and Glycosylation IndependentJournal of Investigative Dermatology, 1995
- Antigen-Specific Immunoadsorption of Pathogenic Autoantibodies in Pemphigus FoliaceusJournal of Investigative Dermatology, 1995
- Adhesion Molecules. I: Keratinocyte-Keratinocyte Interactions; Cadherins and PemphigusJournal of Investigative Dermatology, 1995
- Absorption of pathogenic autoantibodies by the extracellular domain of pemphigus vulgaris antigen (Dsg3) produced by baculovirus.Journal of Clinical Investigation, 1994
- Autoantibodies against the amino-terminal cadherin-like binding domain of pemphigus vulgaris antigen are pathogenic.Journal of Clinical Investigation, 1992
- Autoantibodies against a novel epithelial cadherin in pemphigus vulgaris, a disease of cell adhesionCell, 1991
- Proteolytic processing and physiological regulationTrends in Biochemical Sciences, 1989
- Identification of pemphigus vulgaris antigen extracted from normal human epidermis and comparison with pemphigus foliaceus antigen.Journal of Clinical Investigation, 1988
- An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAsNucleic Acids Research, 1987