A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein-processing enzyme

Detection of Sugars on Paper Chromatograms

Trevelyan, W. E., PROCTER, D. P., & HARRISON, J. S. (1950) · Nature · doi:10.1038/166444b0 · Cited by 3,836 · see citing works

Synthesis and Processing of Asparagine-Linked Oligosaccharides

Hubbard, S. C., & Ivatt, R. J. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.003011 · Cited by 1,382 · see citing works

The biochemistry of glycoproteins and proteoglycans

Summers, D. F. (1980) · Cell · doi:10.1016/0092-8674(80)90572-3 · Cited by 639 · see citing works

The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant.

Kornfeld, K., Reitman, M. L., & Kornfeld, R. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69037-x · Cited by 565 · see citing works

Primary Structure of Glycoprotein Glycans Basis for the Molecular Biology of Glycoproteins

Montreuil, J. (1980) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(08)60021-9 · Cited by 557 · see citing works

Structural determinants of concanavalin A specificity for oligosaccharides

Baenziger, J., & Fiete, D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30236-3 · Cited by 462 · see citing works

Fractionation of Glycopeptides by Affinity Column Chromatography on Concanavalin A-Sepharose1

OGATA, S.-I., Muramatsu, T., & Kobata, A. (1975) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a130956 · Cited by 422 · see citing works

The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein

Li, E., Tabas, I., & Kornfeld, S. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34435-6 · Cited by 421 · see citing works

[90] α-Mannosidase, β-N-acetylhexosaminidase, and β-galactosidase from jack bean meal

Li, Y., & Li, S. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(72)28094-6 · Cited by 405 · see citing works

The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex oligosaccharide units of the vesicular stomatitis virus G protein

Kornfeld, S. A., Li, E., & Tabas, I. A. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34436-8 · Cited by 333 · see citing works

The structural basis of the different affinities of two types of acidic N‐glycosidic glycopeptides for concanavalin a—sepharose

Krusius, T., Finne, J., & Rauvala, H. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80911-8 · Cited by 273 · see citing works

The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannose.

Chapman, A. E., Fujimoto, K., & Kornfeld, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85510-2 · Cited by 230 · see citing works

Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides.

Grinna, L. S., & Robbins, P. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86771-6 · Cited by 224 · see citing works

Deficient uridine diphosphate-N-acetylglucosamine:glycoprotein N-acetylglucosaminyltransferase activity in a clone of Chinese hamster ovary cells with altered surface glycoproteins

Gottlieb, C., Baenziger, J., & Kornfeld, S. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41514-7 · Cited by 224 · see citing works

Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase activity.

Stanley, P., Narasimhan, S., Siminovitch, L., & Schachter, H. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3323 · Cited by 222 · see citing works

The Role of Polyprenol-Bound Saccharides as Intermediates in Glycoprotein Synthesis in Liver

Parodi, A. J., Behrens, N. H., Leloir, L. F., et al. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.11.3268 · Cited by 155 · see citing works

Substrate specificities of rat liver microsomal glucosidases which process glycoproteins.

Grinna, L. S., & Robbins, P. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85881-7 · Cited by 152 · see citing works

Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides

Michael, J. M., & Kornfeld, S. A. (1980) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(80)90278-7 · Cited by 106 · see citing works

Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains.

Elting, J. J., Chen, W. W., & Lennarz, W. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85894-5 · Cited by 103 · see citing works

Endo-β-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: Purification and properties of the two enzymes with different specificities from Clostridium perfringens

Ito, S., Muramatsu, T., & Kobata, A. (1975) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(75)90009-0 · Cited by 99 · see citing works

Ricin resistance in baby hamster kidney cells

Meager, A., UNGKITCHANUKIT, A., NAIRN, R., & Hughes, R. C. (1975) · Nature · doi:10.1038/257137a0 · Cited by 97 · see citing works

Processing of carbohydrate units of glycoproteins. Characterization of a thyroid glucosidase.

Spiro, R. G., Spiro, M. J., & Bhoyroo, V. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35997-0 · Cited by 87 · see citing works

Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2.

Kilker, R., Saunier, B., Tkacz, J. S., & Herscovics, A. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69402-0 · Cited by 86 · see citing works

The initial stages of processing of protein-bound oligosaccharides in vitro.

Turco, S. J., & Robbins, P. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30048-0 · Cited by 76 · see citing works

Enzymatic basis for a lectin-resistant phenotype: increase in a fucosyltransferase in mouse melanoma cells.

Finne, J., Burger, M. M., & Prieels, J. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.92.2.277 · Cited by 74 · see citing works

Effect of glucosylation of lipid intermediates on oligosaccharide transfer in solubilized microsomes from Saccharomyces cerevisiae.

Trimble, R. B., Byrd, J. C., & Maley, F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70218-x · Cited by 72 · see citing works

Isolation and characterization of two mouse L cell lines resistant to the toxic lectin ricin

Gottlieb, C., & Kornfeld, S. A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)56999-x · Cited by 71 · see citing works

Addition of Glucose to Dolichyl Diphosphate Oligosaccharide and Transfer to Protein

Staneloni, R. J., Ugalde, R. A., & Leloir, L. F. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04498.x · Cited by 71 · see citing works

Microsomal Glucosidases of Rat Liver. Partial Purification and Inhibition by Disaccharides

Ugalde, R. A., Staneloni, R. J., & Leloir, L. F. (2005) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06144.x · Cited by 68 · see citing works

Mouse lymphoma cell lines resistant to pea lectin are defective in fucose metabolism

Reitman, M. L., Trowbridge, I. S., & Kornfeld, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43477-1 · Cited by 59 · see citing works

Transfer of glucose to oligosaccharide-lipid intermediates by thyroid microsomal enzymes and its relationship to the N-glycosylation of proteins.

Murphy, L. A., & Spiro, R. G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68988-x · Cited by 58 · see citing works

Expression of Thy‐1 glycoprotein on lectin‐resistant lymphoma cell lines

Trowbridge, I. S., Hyman, R., Ferson, T., & Mazauskas, C. (1978) · European Journal of Immunology · doi:10.1002/eji.1830081009 · Cited by 50 · see citing works

Lectin-resistant cell surface variants of eukaryotic cells

Briles, E. B., & Kornfeld, S. A. (1978) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(78)94561-9 · Cited by 33 · see citing works

The substrate specificity of neutral α-glucosidase from rabbit muscle

Carter, J., & Smith, E. E. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(73)80011-6 · Cited by 15 · see citing works

Biological roles of glycans

Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635 · see citing works

Mutations in GANAB , Encoding the Glucosidase IIα Subunit, Cause Autosomal-Dominant Polycystic Kidney and Liver Disease

Porath, B., Gainullin, V. G., Cornec-Le Gall, E., Dillinger, E. K., Heyer, C. M., Hopp, K., Edwards, M. E., Madsen, C. D., Mauritz, S. R., Banks, C. J., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.05.004 · Cited by 475 · see citing works

Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetylesterase

Varki, A., Hooshmand, F., Diaz, S., Varki, N. M., & Hedrick, S. M. (1991) · Cell · doi:10.1016/0092-8674(91)90408-q · Cited by 134 · see citing works

Persistence of glucose residues on core oligosaccharides prevents association of TCR alpha and TCR beta proteins with calnexin and results specifically in accelerated degradation of nascent TCR alpha proteins within the endoplasmic reticulum

Kearse, K. P., Williams, D. B., & Singer, A. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06677.x · Cited by 119 · see citing works

GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review

De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20 · see citing works

Interactions of an ovalbumin glycopeptide with concanavalin A

Brewer, C. F. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91597-3 · Cited by 14 · see citing works

Interactions of concanavalin a with a trimannosyl oligosaccharide fragment of complex and high mannose type glycopeptides

Brewer, F., Bhattacharyya, L., Brown, R. D., & Koenig, S. H. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(85)80053-x · Cited by 38 · see citing works

5-O-beta-D-Galactofuranosyl-containing exocellular glycopeptide of Penicillium charlesii. Incorporation of mannose from GPD-D-mannose into glycopeptide.

Gander, J. E., Drewes, L. R., Fang, F., et al. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40539-4 · Cited by 5 · see citing works

Glycopeptide and Oligosaccharide Libraries

Hilaire, P. M. S., & Meldal, M. (1999) · doi:10.1002/9783527613502.ch08 · Cited by 4 · see citing works

Structural Analysis of an Oligosaccharide and Glycopeptide Mixture from Panax Ginseng Root with Inhibition SHP-1 Function

Wang, Y., Gao, Q., Li, G., et al. (2011) · Chemical Research in Chinese Universities · Cited by 1 · see citing works