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Processing of epidermal glucosylceramides is required for optimal mammalian cutaneous permeability barrier function.
- W. Holleran, Y. Takagi, G. Menon, G. Legler, K. Feingold, P. Elias
- BiologyThe Journal of clinical investigation
- 1 April 1993
It is demonstrated that glucosylceramide hydrolysis is important in the formation of the epidermal permeability barrier, and suggested that accumulation of glucosyceramides in stratum corneum intercellular membrane domains leads to abnormal barrier function.
The effect of deoxymannojirimycin on the processing of the influenza viral glycoproteins.
Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol.
- R. Datema, P. Romero, G. Legler, R. Schwarz
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 November 1982
The alpha-glucosidase inhibitor bromoconduritol inhibits trimming of the innermost glucose residue from the Glc3Man9GlcNAc2 precursor of high-mannose and complex oligosaccharides, which inhibited the release of infectious fowl plague virus particles from infected chicken-embryo cells.
On the chemical basis of the Lowry protein determination.
The use of inhibitors in the study of glycosidases.
Goat liver beta-mannosidases: molecular properties, inhibition and inactivation of the lysosomal and nonlysosomal forms.
The radical mechanistic differences between the two beta-mannosidases argue against their having the same genetic origin.
The role of N-glycosylation for the plasma clearance of rat liver secretory glycoproteins.
It is concluded that N-glycosylation and processing to complex-type oligosaccharides seems to be of great importance for the circulatory life time of plasma glycoproteins.
The mannosidase inhibitors 1-deoxymannojirimycin and swainsonine have no effect on the biosynthesis and infectivity of Rous sarcoma virus.
Active site directed inhibitors and mechanism of action of glycosidases
- G. Legler
- Biology, ChemistryMolecular and Cellular Biochemistry
- 15 November 1973
In those cases where definite conclusions regarding the mechanism can be drawn, catalysis seems to occur by a carboxylate ion as base and an acid that has been identified as a car boxyl group withβ-glucosidase from Asp.
Study of beta-glucosidase from Helix pomatia by active site-directed inhibitors.
The inhibition studies demonstrate that conduritol epoxides are irreversible inhibitors of beta-glucosidase from the digestive juice of H. pomatia, and that nojirimicin shows tight binding with glucosid enzyme.