ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

Brown, D. A., & Rose, J. K. (1992) · Cell · doi:10.1016/0092-8674(92)90189-j · Cited by 2,921

Intracellular Functions of N-Linked Glycans

Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405

Roles of N-Linked Glycans in the Endoplasmic Reticulum

Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037

Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells

Chen, C.-J., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., & Roninson, I. B. (1986) · Cell · doi:10.1016/0092-8674(86)90595-7 · Cited by 1,898

The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus

Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173

Cellular senescence and tumor suppressor gene p16

Rayess, H., Wang, M. B., & Srivatsan, E. S. (2012) · International Journal of Cancer · doi:10.1002/ijc.27316 · Cited by 825

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

Hammond, C., Braakman, I., & Helenius, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.913 · Cited by 841

Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio

Inoue, S., Tanaka, K., Arisaka, F., Kimura, S., Ohtomo, K., & Mizuno, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006897200 · Cited by 784

Role of Glycosylation in Development

Haltiwanger, R. S., & Lowe, J. B. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074043 · Cited by 757

Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum

Hebert, D. N., Foellmer, B., & Helenius, A. (1995) · Cell · doi:10.1016/0092-8674(95)90395-x · Cited by 552

A two-way street: reciprocal regulation of metabolism and signalling

Wellen, K. E., & Thompson, C. B. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3305 · Cited by 528

Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides

Schachter, H. (1986) · Biochemistry and Cell Biology · doi:10.1139/o86-026 · Cited by 526

Sulfonation and molecular action

Strott, C. A. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0040 · Cited by 487

Cellular Metabolic Stress: Considering How Cells Respond to Nutrient Excess

Wellen, K. E., & Thompson, C. B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.004 · Cited by 486

Antibody Glycosylation and Its Impact on the Pharmacokinetics and Pharmacodynamics of Monoclonal Antibodies and Fc-Fusion Proteins

Liu, L. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24444 · Cited by 428

Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160

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Advances in the production of human therapeutic proteins in yeasts and filamentous fungi

Gerngross, T. U. (2004) · Nature Biotechnology · doi:10.1038/nbt1028 · Cited by 409

Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates.

Ioffe, E., & Stanley, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.728 · Cited by 400

Hereditary hemochromatosis: Effects of C282Y and H63D mutations on association with β 2 -microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells

Waheed, A., Parkkila, S., Zhou, X. Y., Tomatsu, S., Tsuchihashi, Z., Feder, J. N., Schatzman, R. C., Britton, R. S., Bacon, B. R., & Sly, W. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12384 · Cited by 380

The hexosamine biosynthetic pathway couples growth factor-induced glutamine uptake to glucose metabolism

Wellen, K. E., Lu, C., Mancuso, A., Lemons, J. M. S., Ryczko, M., Dennis, J. W., Rabinowitz, J. D., Coller, H. A., & Thompson, C. B. (2010) · Genes & Development · doi:10.1101/gad.1985910 · Cited by 377

Loss of intestinal core 1–derived O-glycans causes spontaneous colitis in mice

Fu, J., Wei, B., Wen, T., Johansson, M. E. V., Liu, X., Bradford, E., Thomsson, K. A., McGee, S., Mansour, L., Tong, M., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45538 · Cited by 366

Complex asparagine-linked oligosaccharides are required for morphogenic events during post-implantation development

Metzler, M., Gertz, A., Sarkar, M., Schachter, H., Schrader, J. W., & Marth, J. D. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06480.x · Cited by 339

Iminosugars past, present and future: Medicines for tomorrow

Horne, G., Wilson, F. X., Tinsley, J., Williams, D. H., & Storer, R. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2010.08.017 · Cited by 320

N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

Mitra, N., Sinha, S., Ramya, T. N. C., & Surolia, A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.003 · Cited by 302

39 kDa receptor‐associated protein is an ER resident protein and molecular chaperone for LDL receptor‐related protein.

Bu, G., Geuze, H. J., Strous, G. J., & Schwartz, A. L. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07221.x · Cited by 274

Nicotine upregulates its own receptors through enhanced intracellular maturation

Sallette, J., Pons, S., Devillers-Thiery, A., Soudant, M., Prado de Carvalho, L., Changeux, J.-P., & Corringer, P. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.03.029 · Cited by 261

Isolation of a Mutant Arabidopsis Plant That Lacks N-Acetyl Glucosaminyl Transferase I and Is Unable to Synthesize Golgi-Modified Complex N-Linked Glycans

von Schaewen, A., Sturm, A., O'Neill, J., & Chrispeels, M. J. (1993) · Plant Physiology · doi:10.1104/pp.102.4.1109 · Cited by 251

Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus

Röttger, S., White, J., Wandall, H. H., Olivo, J.-C., Stark, A., Bennett, E. P., Whitehouse, C., Berger, E. G., Clausen, H., & Nilsson, T. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.1.45 · Cited by 239

The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function

Theos, A. C., Truschel, S. T., Raposo, G., & Marks, M. S. (2005) · Pigment Cell Research · doi:10.1111/j.1600-0749.2005.00269.x · Cited by 224

Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi

Nohturfft, A., DeBose-Boyd, R. A., Scheek, S., Goldstein, J. L., & Brown, M. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11235 · Cited by 212

Glycan analysis of therapeutic glycoproteins

Zhang, L., Luo, S., & Zhang, B. (2016) · mAbs · doi:10.1080/19420862.2015.1117719 · Cited by 207

Glycosylation

Hart, G. W. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90134-x · Cited by 193

Site-specific protein O-glycosylation modulates proprotein processing — Deciphering specific functions of the large polypeptide GalNAc-transferase gene family

Schjoldager, K. T.-B. G., & Clausen, H. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.014 · Cited by 193

Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail

Leung, H. T., Bradshaw, J., Cleaveland, J. S., & Linsley, P. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.25107 · Cited by 191

Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex

Stein, B. S., & Engleman, E. G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39849-7 · Cited by 189

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin, C., Roche, A. C., Monsigny, M., & Hauri, H. P. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.3.483 · Cited by 179

Why mammalian cell surface proteins are glycoproteins

Gahmberg, C. G., & Tolvanen, M. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10034-7 · Cited by 177

Protein Native-State Stabilization by Placing Aromatic Side Chains in N-Glycosylated Reverse Turns

Culyba, E. K., Price, J. L., Hanson, S. R., Dhar, A., Wong, C.-H., Gruebele, M., Powers, E. T., & Kelly, J. W. (2011) · Science · doi:10.1126/science.1198461 · Cited by 171

Congenital disorders of glycosylation: genetic model systems lead the way

Aebi, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)01925-0 · Cited by 167

Lysosome biogenesis in health and disease

Bajaj, L., Lotfi, P., Pal, R., Ronza, A. D., Sharma, J., & Sardiello, M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14564 · Cited by 153

Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts.

Panneerselvam, K., & Freeze, H. H. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118570 · Cited by 146

A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus

Jimenez del Val, I., Nagy, J. M., & Kontoravdi, C. (2011) · Biotechnology Progress · doi:10.1002/btpr.688 · Cited by 135

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

Functional Organization of Golgi N- and O-Glycosylation Pathways Involves pH-dependent Complex Formation That Is Impaired in Cancer Cells

Hassinen, A., Pujol, F. M., Kokkonen, N., Pieters, C., Kihlström, M., Korhonen, K., & Kellokumpu, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277681 · Cited by 131

Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcγ receptor binding and antibody-dependent cell-mediated cytotoxicity activities

Chung, S., Quarmby, V., Gao, X., Ying, Y., Lin, L., Reed, C., Fong, C., Lau, W., Qiu, Z. J., Shen, A., et al. (2012) · mAbs · doi:10.4161/mabs.19941 · Cited by 127

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

N- and O-linked oligosaccharides of allergenic glycoproteins

Fötisch, K., & Vieths*, S. (2001) · Glycoconjugate Journal · doi:10.1023/a:1014860030380 · Cited by 118

An intrinsic mechanism of secreted protein aging and turnover

Yang, W. H., Aziz, P. V., Heithoff, D. M., Mahan, M. J., Smith, J. W., & Marth, J. D. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1515464112 · Cited by 110

Advances in mass spectrometry driven O-glycoproteomics

Levery, S. B., Steentoft, C., Halim, A., Narimatsu, Y., Clausen, H., & Vakhrushev, S. Y. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.09.026 · Cited by 111

Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans

STRASSER, R., STADLMANN, J., SVOBODA, B., ALTMANN, F., GLÖSSL, J., & MACH, L. (2005) · Biochemical Journal · doi:10.1042/bj20041686 · Cited by 105

A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1

Costantini, C., Ko, M. H., Jonas, M. C., & Puglielli, L. (2007) · Biochemical Journal · doi:10.1042/bj20070040 · Cited by 99

RNA interference of sialidase improves glycoprotein sialic acid content consistency

Ngantung, F. A., Miller, P. G., Brushett, F. R., Tang, G. L., & Wang, D. I. C. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20997 · Cited by 97

Core glycosylation of cytochrome P-450(arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen

Shimozawa, O., Sakaguchi, M., Ogawa, H., Harada, N., Mihara, K., & Omura, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36937-6 · Cited by 91

SUGAR-seq enables simultaneous detection of glycans, epitopes, and the transcriptome in single cells

Kearney, C. J., Vervoort, S. J., Ramsbottom, K. M., Todorovski, I., Lelliott, E. J., Zethoven, M., Pijpers, L., Martin, B. P., Semple, T., Martelotto, L., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe3610 · Cited by 87

Modulation of Glycan Recognition by Clustered Saccharide Patches

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Maturation-driven transport and AP-1–dependent recycling of a secretory cargo in the Golgi

Casler, J. C., Papanikou, E., Barrero, J. J., & Glick, B. S. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201807195 · Cited by 77

Free oligosaccharide regulation during mammalian protein N-glycosylation

Chantret, I., & Moore, S. E. H. (2007) · Glycobiology · doi:10.1093/glycob/cwn003 · Cited by 75

Mannose supplementation corrects GDP-mannose deficiency in cultured fibroblasts from some patients with Congenital Disorders of Glycosylation (CDG)

Rush, J. S., Panneerselvam, K., Waechter, C. J., & Freeze, H. H. (2000) · Glycobiology · doi:10.1093/glycob/10.8.829 · Cited by 63

The - and -subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver

Treml, K., Meimaroglou, D., Hentges, A., & Bause, E. (2000) · Glycobiology · doi:10.1093/glycob/10.5.493 · Cited by 63

Oligosaccharide transport: pumping waste from the ER into lysosomes

Moore, S. E. H. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01648-7 · Cited by 57

Identification of the CD45-associated 116-kDa and 80-kDa Proteins as the α- and β-Subunits of α-Glucosidase II

Arendt, C. W., & Ostergaard, H. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13117 · Cited by 55

Swainsonine reduces 5-fluorouracil tolerance in the multistage resistance of colorectal cancer cell lines

Hamaguchi, J., Nakagawa, H., Takahashi, M., Kudo, T., Kamiyama, N., Sun, B., Oshima, T., Sato, Y., Deguchi, K., Todo, S., et al. (2007) · Molecular Cancer · doi:10.1186/1476-4598-6-58 · Cited by 45

Emerging Structural Insights into Glycoprotein Quality Control Coupled with N-Glycan Processing in the Endoplasmic Reticulum

Satoh, T., Yamaguchi, T., & Kato, K. (2015) · Molecules · doi:10.3390/molecules20022475 · Cited by 42

Cellular effects of deoxynojirimycin analogues: Inhibition of N-linked oligosaccharide processing and generation of free glucosylated oligosaccharides

MELLOR, H. R., NEVILLE, D. C. A., HARVEY, D. J., PLATT, F. M., DWEK, R. A., & BUTTERS, T. D. (2004) · Biochemical Journal · doi:10.1042/bj20031824 · Cited by 41

Glycosylation processing inhibition by castanospermine prevents experimental autoimmune encephalomyelitis by interference with IL-2 receptor signal transduction

Walter, S., Fassbender, K., Gulbins, E., Liu, Y., Rieschel, M., Herten, M., Bertsch, T., & Engelhardt, B. (2002) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(02)00308-9 · Cited by 41

Novel forms of protein glycosylation

Hayes, B. K., & Hart, G. W. (1994) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(94)90167-8 · Cited by 39

Mammalian legumain - A lysosomal cysteine protease with extracellular functions?

Lunde, N. N., Bosnjak, T., Solberg, R., & Johansen, H. T. (2019) · Biochimie · doi:10.1016/j.biochi.2019.06.002 · Cited by 29

Affinity purification and characterization of glucosidase II from pig liver

Hentges, A., & Bause, E. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.9.1031 · Cited by 29

Formation of highly ordered cross-linked lattices between asparagine-linked oligosaccharides and lectins observed by electron microscopy

Bhattacharyya, L., Khan, M. I., Fant, J., & Brewer, C. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80095-3 · Cited by 23

Processing enzyme glucosidase II: proposed catalytic residues and developmental regulation during the ontogeny of the mouse mammary gland

Feng, J. (2004) · Glycobiology · doi:10.1093/glycob/cwh110 · Cited by 17

Endosomal trafficking is required for glycosylation and normal maturation of the Alzheimer’s-associated protein sorLA

Christensen, S. K., Narimatsu, Y., Simoes, S., Goth, C. K., Vægter, C. B., Small, S. A., Clausen, H., & Andersen, O. M. (2020) · doi:10.1101/2020.07.12.199885 · Cited by 11

Thyrotropin N-glycosylation and Glycan Composition in Severe Primary Hypothyroidism

Wide, L., & Eriksson, K. (2021) · Journal of the Endocrine Society · doi:10.1210/jendso/bvab006 · Cited by 9

Cell‐specific constraints to the lateral diffusion of a membrane glycoprotein

Barbour, S., & Edidin, M. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041500313 · Cited by 7

Cryo-EM structure of native honey bee vitellogenin

Montserrat-Canals, M., Schnelle, K., Leipart, V., Halskau, Ø., Amdam, G. V., Moeller, A., Cunha, E. S., & Luecke, H. (2025) · Nature Communications · doi:10.1038/s41467-025-58575-y · Cited by 7