Spore coat is altered inmodB glycosylation mutants ofDictyostelium discoideum
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Monoclonal antibody recognizing gp80, a membrane glycoprotein implicated in intercellular adhesion of Dictyostelium discoideum.
2. Absence of a carbohydrate modification does not affect the level or subcellular localization of three membrane glycoproteins in modB mutants of Dictyostelium discoideum.
3. Post-translational glycosylation of the contact site A protein of Dictyostelium discoideum is important for stability but not for its function in cell adhesion
4. Adhesion mutants of Dictyostelium discoideum lacking the saccharide determinant recognized by two adhesion-blocking monoclonal antibodies
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1. Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion;Journal of Proteome Research;2010-05-21
2. Initiation of Mucin-type O-Glycosylation in Dictyostelium Is Homologous to the Corresponding Step in Animals and Is Important for Spore Coat Function;Journal of Biological Chemistry;2003-12
3. Formation of the outer layer of the Dictyostelium spore coat depends on the inner-layer protein SP85/PsB;Microbiology;2003-02-01
4. Comparative analysis of spore coat Formation, structure, and function in Dictyostelium;International Review of Cytology;2003
5. Dictyostelium discoideum glycoproteins: using a model system for organismic glycobiology;Glycoproteins II;1997
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