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European Journal of Biochemistry|July 21, 2000
Recombinant glycodelin carrying the same type of glycan structures as contraceptive glycodelin-A can be produced in human kidney 293 cells but not in chinese hamster ovary cellsI M Van den Nieuwenhof, H Koistinen, R L Easton, et al.
Glycobiology|July 11, 2001
In vivo glycosylation of mucin tandem repeatsH S Silverman, S Parry, M Sutton-Smith, et al.
FEMS Microbiology Letters|April 21, 2001
The failure of different strains of Yersinia pestis to produce lipopolysaccharide O-antigen under different growth conditions is due to mutations in the O-antigen gene clusterJ L Prior, J Parkhill, P G Hitchen, et al.
Archives of Biochemistry and Biophysics|July 1, 1983
Fucose containing oligosaccharides from human milk. I. Separation and identification of new constituentsH Egge, A Dell, H Von Nicolai
The Journal of Biological Chemistry|April 25, 1984
Structure of fetal lactosaminoglycan. The carbohydrate moiety of Band 3 isolated from human umbilical cord erythrocytesM Fukuda, A Dell, M N Fukuda
Biochemical and Biophysical Research Communications|July 16, 1985
An HPLC/push-pull perfusion technique for investigating peptide metabolismA V Singh, H R Morris
The Journal of Biological Chemistry|May 25, 1987
Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase IIM N Fukuda, A Dell, P Scartezzini
The Journal of Biological Chemistry|April 5, 1987
Biosynthesis of the mycobacterial O-methylglucose lipopolysaccharide. Characterization of putative intermediates in the initiation, elongation, and termination reactionsK Kamisango, A Dell, C E Ballou
The Journal of Biological Chemistry|September 5, 1987
Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNAH Sasaki, B Bothner, A Dell, et al.
Biochemistry|November 15, 1988
Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometryH Sasaki, N Ochi, A Dell, et al.
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