A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces
- 1 January 1997
- journal article
- Published by Elsevier in Molecular and Biochemical Parasitology
- Vol. 84 (1) , 33-48
- https://doi.org/10.1016/s0166-6851(96)02780-6
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Posttranslational Regulation of a Leishmania HEXXH Metalloprotease (gp63)Published by Elsevier ,1996
- An investigation into the significance of the N-linked oligosaccharides of Leishmania gp63Molecular and Biochemical Parasitology, 1994
- N-Glycosylation in trypanosomatid protozoaGlycobiology, 1993
- A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulumBiochemistry, 1991
- Lipophosphoglycan expression and virulence in Ricin-resistant variants of Leishmania majorMolecular and Biochemical Parasitology, 1990
- Leishmania gp63 molecule implicated in cellular adhesion lacks an Arg-Gly-Asp sequenceMolecular and Biochemical Parasitology, 1990
- Role of macrophage complement and lectin-like receptors in binding Leishmania parasites to host macrophagesImmunology Letters, 1985
- Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase FBiochemistry, 1985
- Glycoprotein assembly in LeishmaniamexicanaBiochemical and Biophysical Research Communications, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970