The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases
Open accessAbstract
H3G I Y6Glucosidase activities which remove glucose residues from GlcZMangGlcNAcz and GlclManyGlcNAcz oligosaccharides were obtained in soluble form from Saccharomyces cerevisiae X-2180 without detergent.These two enzyme activities were clearly separated from the GlcsMangGlcNAcz oligosaccharide glucosidase which was shown previously to remove the terminal glucose residue from GlcsMan9GlcNAcz oligosaccharide (Kilker,
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“GII inhibitors include the pyranose sugar analogues 1-deoxynojirimycin, N-5-carboxypentyl-dNM, and castanospermine, all iminosugars [218,376,377].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [377]
Citations
Cites
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
Schmidt, D. D., Frommer, W., Junge, B., M�ller, L., Wingender, W., Truscheit, E., & Sch�fer, D. (1977) · Die Naturwissenschaften · doi:10.1007/bf00483561 · Cited by 467
Li, E., Tabas, I., & Kornfeld, S. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34435-6 · Cited by 421
Structure and synthesis of nojirimycin
Inouye, S., Tsuruoka, T., Itô, T., & NIIDA, T. (1968) · Tetrahedron · doi:10.1016/0040-4020(68)88115-3 · Cited by 379
The role of lipid intermediates in the glycosylation of proteins in the eucaryotic cell
Parodi, A. J., & Leloir, L. F. (1979) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(79)90006-6 · Cited by 378
Swainsonine: an inhibitor of glycoprotein processing.
Elbein, A. D., Solf, R., Dorling, P. R., & Vosbeck, K. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7393 · Cited by 255
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
Glucosidase-Inhibitoren aus Bazillen
Schmidt, D. D., Frommer, W., M�ller, L., & Truscheit, E. (1979) · Die Naturwissenschaften · doi:10.1007/bf00368825 · Cited by 163
“Nojirimycin” as a Potent Inhibitor of Glucosidase
NIWA, T., Inouye, S., Tsuruoka, T., Koaze, Y., & NIIDA, T. (1970) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1970.10859713 · Cited by 162
The plurality of long chain isoprenoid alcohols (polyprenols) from natural sources
Dunphy, P. J., Kerr, J. D., Pennock, J. F., Whittle, K. J., & Feeney, J. (1967) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(67)90329-7 · Cited by 162
Cited by
Sorted by citations
INHIBITORS OF THE BIOSYNTHESIS AND PROCESSING OF N-LINKED OLIGOSACCHARIDE CHAINS
Elbein, A. D. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.002433 · Cited by 1,126
Natural products to drugs: natural product-derived compounds in clinical trials
Butler, M. S. (2008) · Natural Product Reports · doi:10.1039/b514294f · Cited by 1,086
Natural products: An evolving role in future drug discovery
Mishra, B. B., & Tiwari, V. K. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.07.057 · Cited by 887
Glycoprotein biosynthesis in yeast
Herscovics, A. A., & Orlean, P. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.6.8472892 · Cited by 518
Self-citationN-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis.
Platt, F. M., Neises, G. R., Dwek, R. A., & Butters, T. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37202-2 · Cited by 455
Protein glycosylation in yeast
Tanner, W., & Lehle, L. (1987) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(87)90006-2 · Cited by 336
Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I.
Elbein, A. D., Tropea, J. E., Mitchell, M., & Kaushal, G. P. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55439-9 · Cited by 332
Glycosidases of the asparagine-linked oligosaccharide processing pathway
Moremen, K. W., Trimble, R. B., & Herscovics, A. A. (1994) · Glycobiology · doi:10.1093/glycob/4.2.113 · Cited by 331
Self-citationBallou, C. E. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85038-p · Cited by 298
Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides
Fuhrmann, U., Bause, E., Legler, G., & Ploegh, H. L. (1984) · Nature · doi:10.1038/307755a0 · Cited by 298
Protein Localization and Membrane Traffic in Yeast
Schekman, R. W. (1985) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.01.110185.000555 · Cited by 259
Pan, Y., Hori, H., Saul, R., Sanford, B. A., Molyneux, R. J., & Elbein, A. D. (1983) · Biochemistry · doi:10.1021/bi00285a038 · Cited by 257
Lodish, H. F., & Kong, N. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.98.5.1720 · Cited by 239
Inhibitors of oligosaccharide processing
Fuhrmann, U., Bause, E., & Ploegh, H. L. (1985) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(85)90095-8 · Cited by 213
Cell wall integrity modulates RHO1 activity via the exchange factor ROM2
Bickle, M., Delley, P., Schmidt, A., & Hall, M. N. (1998) · EMBO Journal · doi:10.1093/emboj/17.8.2235 · Cited by 198
Glycosidase inhibition by plant alkaloids which are structural analogues of monosaccharides
Evans, S. V., Fellows, L. E., Shing, T. K. M., & Fleet, G. W. J. (1985) · Phytochemistry · doi:10.1016/s0031-9422(00)83099-x · Cited by 184
Inhibitors of the Biosynthesis and Processing of N-Linked Oligosaccharide
Elbein, A. D., & Heath, E. C. (1984) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238409102805 · Cited by 183
Golgi endo-alpha-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme.
Lubas, W. A., & Spiro, R. G. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61422-x · Cited by 180
Platt, F. M., Neises, G. R., Karlsson, G. B., Dwek, R. A., & Butters, T. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47132-3 · Cited by 176
Protein N-Glycosylation: Molecular Genetics and Functional Significance
Kukuruzinska, M. A., & Lennon, K. (1998) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411980090040301 · Cited by 174
Effects of the imino sugar N-butyldeoxynojirimycin on the N-glycosylation of recombinant gp120.
Karlsson, G. B., Butters, T. D., Dwek, R. A., & Platt, F. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54189-2 · Cited by 173
Fischer, P. B., Collin, M., Karlsson, G. B., James, W., Butters, T. D., Davis, S. J., Gordon, S., Dwek, R. A., & Platt, F. M. (1995) · Journal of Virology · doi:10.1128/jvi.69.9.5791-5797.1995 · Cited by 155
Lubas, W. A., & Spiro, R. G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69024-6 · Cited by 151
Mora-Montes, H. M., Bates, S., Netea, M. G., Díaz-Jiménez, D. F., López-Romero, E., Zinker, S., Ponce‐Noyola, P., Kullberg, B. J., Brown, A. J. P., Odds, F. C., et al. (2007) · Eukaryotic Cell · doi:10.1128/ec.00350-07 · Cited by 149
Slieker, L. J., Martensen, T. M., & Lane, M. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66858-9 · Cited by 145
Hilkens, J., & Buijs, F. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68911-2 · Cited by 140
Processing glycosidases of Saccharomyces cerevisiae
Herscovics, A. A. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(98)00129-9 · Cited by 137
Self-citationLe, A., Ferrell, G. A., Dishon, D. S., Le, Q., & Sifers, R. N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48397-4 · Cited by 125
The effect of 1-deoxymannojirimycin on rat liver α-mannosidases
Bischoff, J. E., & Kornfeld, R. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80371-x · Cited by 125
Gross, V., Andus, T., Tran-Thi, T. A., Schwarz, R. Τ., Decker, K., & Heinrich, P. C. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44157-3 · Cited by 122
Bernotas, R. C., & Ganem, B. (1985) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)98412-0 · Cited by 121
Fischer, P. B., Karlsson, G. B., Butters, T. D., Dwek, R. A., & Platt, F. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.10.7143-7152.1996 · Cited by 115
Camirand, A., Heysen, A., Grondin, B., & Herscovics, A. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98594-7 · Cited by 114
Self-citationEarly steps in processing of yeast glycoproteins.
Esmon, B., Esmon, P. C., & Schekman, R. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90967-1 · Cited by 112
Studies on the adaptation of influenza viruses to MDCK cells.
ROTT, R., Orlich, M., Klenk, H., Wang, M. L., Skehel, J. J., & Wiley, D. C. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02299.x · Cited by 107
Burke, B. E., Matlin, K. S., Bause, E., Legler, G., Peyriéras, N., & Ploegh, H. L. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01845.x · Cited by 107
Australine, a pyrrolizidine alkaloid that inhibits amyloglucosidase and glycoprotein processing
Tropea, J. E., Molyneux, R. J., Kaushal, G. P., Pan, Y., Mitchell, M., & Elbein, A. D. (1989) · Biochemistry · doi:10.1021/bi00431a010 · Cited by 106
Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells
Sasak, V., Ordovás, J. M., Elbein, A. D., & Berninger, R. W. (1985) · Biochemical Journal · doi:10.1042/bj2320759 · Cited by 105
Lodish, H. F., Kong, N., Hirani, S., & RASMUSSEN, J. E. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.2.221 · Cited by 105
The effect of deoxymannojirimycin on the processing of the influenza viral glycoproteins
Elbein, A. D., Legler, G., Tlusty, A., McDowell, W., & Schwarz, R. Τ. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90232-7 · Cited by 105
Pal, R., Hoke, G., & Sarngadharan, M. G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.9.3384 · Cited by 104
ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg
Grubenmann, C. E. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.19.2331 · Cited by 103
Prepro-alpha-factor has a cleavable signal sequence.
Waters, M. G., Evans, E. A., & Blobel, G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68773-3 · Cited by 102
Jelinek-Kelly, S., Akiyama, T., Saunier, B., Tkacz, J. S., & Herscovics, A. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89546-1 · Cited by 102
Self-citationPurification and properties of glucosidase I from mung bean seedlings
Szumiło, T., Kaushal, G. P., & Elbein, A. D. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90583-7 · Cited by 101
Chiasson, J., & Naditch‐Brûlé, L. (2001) · Diabetes Care · doi:10.2337/diacare.24.6.989 · Cited by 100
Isolation of a homogeneous glucosidase II from pig kidney microsomes
BRADA, D., & DUBACH, U. C. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08169.x · Cited by 97
Trugnan, G., Rousset, M., Chantret, I., Barbat, A., & Zweibaum, A. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.5.1199 · Cited by 97
Inhibitors of trimming: new tools in glycoprotein research
Schwarz, R. Τ., & DATEMA, R. (1984) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(84)90046-x · Cited by 93
Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9
Roth, J., & Zuber, C. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-016-1513-9 · Cited by 92
Fischer, P. B., Karlsson, G. B., Dwek, R. A., & Platt, F. M. (1996) · Journal of Virology · doi:10.1128/jvi.70.10.7153-7160.1996 · Cited by 86
Asano, N., Nishida, M., Kato, A., Kizu, H., Matsui, K., Shimada, Y., Itoh, T., Baba, M., Watson, A. A., Nash, R. J., et al. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm970836l · Cited by 86
Jelinek-Kelly, S., & Herscovics, A. A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68102-5 · Cited by 86
Self-citationMaras, M., Bruyn, A. D., Schraml, J., Herdewijn, P. A., Claeyssens, M., Fiers, W. C., & Contreras, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00617.x · Cited by 85
Inhibition of glycoprotein processing by L-fructose and L-xylulose
Muniruzzaman, S., Pan, Y., Zeng, Y., Atkins, B. D., Izumori, K., & Elbein, A. D. (1996) · Glycobiology · doi:10.1093/glycob/6.8.795 · Cited by 85
Inhibitors of protein glycosylation and glycoprotein processing in viral systems
DATEMA, R., Olofsson, S., & Romero, P. (1987) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(87)90066-0 · Cited by 85
Lemansky, P., Gieselmann, V., Hasilík, A., & FIGURA, K. V. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90939-7 · Cited by 84
Romero, P., DATEMA, R., & Schwarz, R. Τ. (1983) · Virology · doi:10.1016/0042-6822(83)90133-2 · Cited by 84
Trimble, R. B., & Atkinson, P. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67588-x · Cited by 81
Pique, C., Pham, D., Tursz, T., & Dokhélar, M. (1992) · Journal of Virology · doi:10.1128/jvi.66.2.906-913.1992 · Cited by 82
Microbial β-Glucanases Different from Cellulases
Bielecki, S., & Galas, E. (1991) · Critical Reviews in Biotechnology · doi:10.3109/07388559109038212 · Cited by 77
The role of N-linked oligosaccharides in glycoprotein function
Elbein, A. D. (1991) · Trends in biotechnology · doi:10.1016/0167-7799(91)90117-z · Cited by 76
Schlesinger, S., Malfer, C., & Schlesinger, M. J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42832-8 · Cited by 75
Wikström, L., & Lodish, H. F. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.113.5.997 · Cited by 75
Elbein, A. D., Mitchell, M., Sanford, B. A., Fellows, L. E., & Evans, S. V. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90761-1 · Cited by 74
Geysens, S., Pakula, T., Uusitalo, J. M., Dewerte, I., Penttilä, M. E., & Contreras, R. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.6.2910-2924.2005 · Cited by 73
Roth, J., Ziak, M., & Zuber, C. (2003) · Biochimie · doi:10.1016/s0300-9084(03)00049-x · Cited by 72
Yeo, K. T., Parent, J. B., Yeo, T.-K., & Olden, K. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39537-6 · Cited by 72
[58] Glycosylation inhibitors for n-linked glycoproteins
Elbein, A. D. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)38060-7 · Cited by 72
Arakaki, R. F., HEDO, J. A., COLLIER, E. S., & Görden, P. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60898-1 · Cited by 71
Romero, P., Saunier, B., & Herscovics, A. A. (1985) · Biochemical Journal · doi:10.1042/bj2260733 · Cited by 70
Self-citationBiological activities of cyclophellitol.
Atsumi, S., IINUMA, H., Nosaka, C., & Umezawa, K. (1990) · The Journal of Antibiotics · doi:10.7164/antibiotics.43.1579 · Cited by 69
Formation and Assembly of Alphavirus Glycoproteins
Schlesinger, M. J., & Schlesinger, S. (1986) · Springer eBooks · doi:10.1007/978-1-4757-0785-4_5 · Cited by 68
Castanospermine: a potent inhibitor of sucrase from the human enterocyte‐like cell line Caco‐2
Trugnan, G., Rousset, M., & Zweibaum, A. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80123-5 · Cited by 68
Tan, A. K., van den Broek, L. A. M., van Boeckel, S., Ploegh, H. L., & Bolscher, J. G. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98715-6 · Cited by 67
di Bello, I. C., Dorling, P. R., Fellows, L. E., & WINCHESTER, B. G. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80911-4 · Cited by 65
Dissecting glycoprotein biosynthesis by the use of specific inhibitors
McDowell, W., & Schwarz, R. Τ. (1988) · Biochimie · doi:10.1016/0300-9084(88)90290-8 · Cited by 64
Purification and Properties of a Glycoprotein Processing α-Mannosidase from Mung Bean Seedlings
Szumiło, T., Kaushal, G. P., Hori, H., & Elbein, A. D. (1986) · PLANT PHYSIOLOGY · doi:10.1104/pp.81.2.383 · Cited by 64
[44] Analysis of synthesis, processing, and secretion of proteins expressed in mammalian cells
Dorner, A. J., & Kaufman, R. J. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85046-q · Cited by 63
The yeast CWH41 gene encodes glucosidase I
Romero, P., Dijkgraaf, G. J. P., Shahinian, S., Herscovics, A. A., & Bussey, H. (1997) · Glycobiology · doi:10.1093/glycob/7.7.997 · Cited by 62
Self-citationShahinian, S., Dijkgraaf, G. J. P., Sdicu, A., Thomas, D. Y., Jakob, C. A., Aebi, M., & Bussey, H. (1998) · Genetics · doi:10.1093/genetics/149.2.843 · Cited by 62
Sha, X., Brunner, A. M., Purchio, A. F., & Gentry, L. E. (1989) · Molecular Endocrinology · doi:10.1210/mend-3-7-1090 · Cited by 62
The effects of inhibitors of glucosidase I on the formation of Sindbis virus
Schlesinger, S., Koyama, A. H., Malfer, C., Gee, S. L., & Schlesinger, M. J. (1985) · Virus Research · doi:10.1016/0168-1702(85)90244-8 · Cited by 61
Nichols, E. J., Manger, R., Hakomori, S., Herscovics, A. A., & Rohrschneider, L. R. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3467 · Cited by 61
Self-citationA Systematic Review of the Medicinal Potential of Mulberry in Treating Diabetes Mellitus
Wei, H., Liu, S., Liao, Y., Ma, C., Wang, D., Tong, J., Feng, J., Yi, T., & Zhu, L. (2018) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x1850088x · Cited by 60
Fungal cell walls: Their structure, biosynthesis and biotechnological aspects
Farkaš, V. (1990) · Acta Biotechnologica · doi:10.1002/abio.370100303 · Cited by 59
Runge, K. W., & Robbins, P. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66754-7 · Cited by 57
Pourcq, K. D., Tiels, P., Hecke, A. V., Geysens, S., Vervecken, W., & Callewaert, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039976 · Cited by 56
Saxena, S., Shailubhai, K., Dong-Yu, B., & Vijay, I. K. (1987) · Biochemical Journal · doi:10.1042/bj2470563 · Cited by 53
Zamofing, D., Rossier, B. C., & Geering, K. (1988) · The Journal of Membrane Biology · doi:10.1007/bf01871903 · Cited by 53
Ray, M. K., Yang, J., Sundaram, S., & Stanley, P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54427-6 · Cited by 53
Studies on the effect of glycoprotein processing inhibitors on fusion of L6 myoblast cell lines
Spearman, M. A., Jamieson, J., & Wright, J. (1987) · Experimental Cell Research · doi:10.1016/0014-4827(87)90421-6 · Cited by 53
Role of malectin in Glc2Man9GlcNAc2-dependent quality control of α1-antitrypsin
Chen, Y., Hu, D., Yabe, R., Tateno, H., Qin, S.-Y., Matsumoto, N., Hirabayashi, J., & Yamamoto, K. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-03-0201 · Cited by 52
Ballou, L., Gopal, P. K., Krümmel, B., Tammi, M., & Ballou, C. E. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.10.3081 · Cited by 50
1,4-Dideoxy-1,4-imino-d-mannitol inhibits glycoprotein processing and mannosidase
Palamarczyk, G., Mitchell, M., Smith, P. W., Fleet, G. W. J., & Elbein, A. D. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90771-4 · Cited by 50
Bosch, M., Trombetta, S., Engström, U., & Parodi, A. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77843-0 · Cited by 50
Inhibition of processing of plant N-linked oligosaccharides by castanospermine
Hori, H., Pan, Y., Molyneux, R. J., & Elbein, A. D. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90019-5 · Cited by 50
Strous, G. J., van Kerkhof, P., Brok, R. G. P. M., Roth, J., & Brada, D. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61398-5 · Cited by 48
[19] Glycosidase inhibitors in study of glycoconjugates
Kaushal, G. P., & Elbein, A. D. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)30021-6 · Cited by 48
Kamps, C. A., Lin, Y., & Wong, P. K. Y. (1991) · Virology · doi:10.1016/0042-6822(91)90438-h · Cited by 48
Metadata
- Authors
- Saunier, B., Kilker, R. D., Tkacz, J. S., Quaroni, A., & Herscovics, A.
- Affiliations
- Harvard University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-12
- Volume
- 257
- Issue
- 23
- Pages
- 14155-14161
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1515555384
- Cited by
- 283
- References
- 26
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 4 · 2022: 6 · 2021: 1 · 2019: 3 · 2018: 7 · 2017: 1 · 2016: 5 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 2
- FWCI
- 8.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- 1-deoxynojirimycin, glucosidase inhibitors, Saccharomyces cerevisiae, oligosaccharide processing
- MeSH terms
- Glucosamine, Glucosidases, Glycoproteins, Kinetics, Oligosaccharides, Saccharomyces cerevisiae, Sucrase, 1-Deoxynojirimycin
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review