Porcine Submaxillary Mucin Forms Disulfide-linked Multimers through Its Amino-terminal D-domains
Open Access
- 1 June 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (23) , 14442-14449
- https://doi.org/10.1074/jbc.273.23.14442
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The Complete cDNA Sequence and Structural Polymorphism of the Polypeptide Chain of Porcine Submaxillary MucinPublished by Elsevier ,1997
- Genomic Organization of the 3′ Region of the Human Mucin GeneMUC5BJournal of Biological Chemistry, 1997
- The Carboxyl-terminal Sequence of the Human Secretory Mucin, MUC6Journal of Biological Chemistry, 1997
- Determination of the Site-specific O-Glycosylation Pattern of the Porcine Submaxillary Mucin Tandem Repeat GlycopeptideJournal of Biological Chemistry, 1997
- Characterization of a Mucin cDNA Clone Isolated from HT-29 Mucus-secreting Cells.Published by Elsevier ,1995
- Norrie disease is caused by mutations in an extracellular protein resembling C–terminal globular domain of mucinsNature Genetics, 1992
- von Willebrand factor.Published by Elsevier ,1991
- Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids.The Journal of cell biology, 1991
- Cloning and cDNA sequence of a bovine submaxillary gland mucin-like protein containing two distinct domains.Proceedings of the National Academy of Sciences, 1990
- An integumentary mucin (FIM-B.1) from Xenopus laevis homologous with the von Willebrand factorBiochemistry, 1990