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GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM
Abstract
PERSPECTIVES AND SUMMARY 841 BINDING STUDIES USING LECTINS .. .. ........ 843 Lectin Binding Sites in the Nucleus . . . . . . . . . . . . . . . . . . . 843 Lectin Binding Sites in the Cytoplasm 848 BIOCHEMICAL STUDIES ... . . .. . . . . . . . .. . .. . 849 General Compositional Analyses and Metabolic Labeling Studies ... ... 849 High Mobility Group . ......... . . . . . 851 Proteoglycans and Glycosaminoglycans 851 Glycogenin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 857 Viruses. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 857 O-Linked N-Acetylglucosamine-Bearing Glycoproteins 858 NUCLEAR AND CYTOPLASMIC SACCHARIDE-BINDING PROTEINS 863 Endogenous Lectins . . . . . . .. . . .. . . . . . . . . . . ... .. . ...... . . . ..... 863 Glycosidases . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 866 Glycosyltransferases ...... ... . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . 867 FUTURE DIRECTIONS . . . . 868
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Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Blom, N., Sicheritz‐Pontén, T., Gupta, R., Gammeltoft, S., & Brunak, S. (2004) · PROTEOMICS · doi:10.1002/pmic.200300771 · Cited by 2,076
Glycosylation and the Immune System
Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Self-citationHart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317
Self-citationLis, H., & Sharon, N. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18347.x · Cited by 840
Drickamer, K., & Taylor, M. E. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.001321 · Cited by 777
Why are proteins O-glycosylated?
Jentoft, N. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90014-3 · Cited by 705
Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death
Perillo, N. L., Marcus, M. E., & Baum, L. G. (1998) · Journal of Molecular Medicine · doi:10.1007/s001090050232 · Cited by 640
Garcia-Bustos, J., Heitman, J., & Hall, M. N. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(91)90013-m · Cited by 543
How proteins enter the nucleus
Silver, P. A. (1991) · Cell · doi:10.1016/0092-8674(91)90233-o · Cited by 553
Richards, D. E., King, K. E., Aït-Ali, T., & Harberd, N. P. (2001) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.52.1.67 · Cited by 512
Dong, D. L., & Hart, G. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32170-1 · Cited by 508
Self-citationDYNAMIC O-LINKED GLYCOSYLATION OF NUCLEAR AND CYTOSKELETAL PROTEINS
Hart, G. W. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.315 · Cited by 503
Self-citationReboul, P., Pelletier, J., Tardif, G., Cloutier, J. M., & Martel‐Pelletier, J. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118636 · Cited by 488
Chou, T.-Y., Hart, G. W., & Dang, C. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18961 · Cited by 453
Self-citationHaltiwanger, R. S., Blomberg, M. A., & Hart, G. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50380-5 · Cited by 444
Self-citationHaltiwanger, R. S., Holt, G. D., & Hart, G. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39838-2 · Cited by 372
Self-citationO-Glycosylation of Nuclear and Cytosolic Proteins
Comer, F. I., & Hart, G. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000010200 · Cited by 361
Self-citationThe Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine
Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361
Self-citationO-Glycosylation of the Mucin Type
Hanisch, F. (2001) · Biological Chemistry · doi:10.1515/bc.2001.022 · Cited by 325
Lehle, L., Strahl, S., & Tanner, W. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601645 · Cited by 314
Post‐Translational Modification of Proteins
Krishna, R., & Wold, F. (1993) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123133.ch3 · Cited by 313
High-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
Alley, W. R., Mann, B. F., & Novotný, M. V. (2013) · Chemical Reviews · doi:10.1021/cr3003714 · Cited by 310
Strategies for analysis of glycoprotein glycosylation
Geyer, H., & Geyer, R. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.10.007 · Cited by 307
Hofsteenge, J., Mueller, D. R., de Beer, T., Loeffler, A., Richter, W. J., & Vliegenthart, J. F. G. (1994) · Biochemistry · doi:10.1021/bi00250a003 · Cited by 298
Strahl‐Bolsinger, S., Gentzsch, M., & Tanner, W. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(98)00131-7 · Cited by 293
Gurnett, C. A., WAARD, M. M. D., & Campbell, K. P. (1996) · Neuron · doi:10.1016/s0896-6273(00)80061-6 · Cited by 291
The Emerging Significance of O-GlcNAc in Cellular Regulation
Zachara, N. E., & Hart, G. W. (2002) · Chemical Reviews · doi:10.1021/cr000406u · Cited by 284
Self-citationProtein Import into the Nucleus: An Integrated View
Hicks, G. R., & Raikhel, N. V. (1995) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cb.11.110195.001103 · Cited by 279
Rauch, U., Gao, P., Janetzko, A., Flaccus, A., Hilgenberg, L., Tekotte, H., Margolis, R. K., & Margolis, R. U. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98755-7 · Cited by 267
Peattie, D. A., Harding, M. W., Fleming, M. A., DeCenzo, M. T., Lippke, J. A., Livingston, D. J., & Benasutti, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10974 · Cited by 251
Nothing in Glycobiology Makes Sense, except in the Light of Evolution
Varki, A. P. (2006) · Cell · doi:10.1016/j.cell.2006.08.022 · Cited by 253
Kraemer, D. M., Wozniak, R. W., Blobel, G. A., et al. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1519 · Cited by 241
Berezney, R. (1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240470204 · Cited by 237
A complex of nuclear pore proteins required for pore function.
Finlay, D. R., Meier, E., Bradley, P. J., et al. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.114.1.169 · Cited by 235
Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins.
Kearse, K. P., & Hart, G. W. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1701 · Cited by 232
Self-citationGoldberg, M. W., & Allen, T. D. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.6.1429 · Cited by 230
Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored
Finlay, D. R., & Forbes, D. J. (1990) · Cell · doi:10.1016/0092-8674(90)90712-n · Cited by 229
Glycosylation of the c-Myc transactivation domain.
Chou, T., Dang, C. V., & Hart, G. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4417 · Cited by 225
Self-citationO Glycosylation of an Sp1-Derived Peptide Blocks Known Sp1 Protein Interactions
Roos, M. D., Su, K., Baker, J. R., & Kudlow, J. E. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6472 · Cited by 223
Gahmberg, C. G., Tolvanen, M. E. E., & Kotovuori, P. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00215.x · Cited by 222
The Malaria Pigment Haemozoin—A Focal Point of Action for Antimalarial Drugs
Senge, M. O., & Hatscher, S. S. (2000) · ChemBioChem · doi:10.1002/1439-7633(20001117)1:4 · Cited by 8
The use of mass spectrometry for the proteomic analysis of glycosylation
Morelle, W., Canis, K., Chirat, F., Faid, V., & Michalski, J. (2006) · PROTEOMICS · doi:10.1002/pmic.200600129 · Cited by 207
Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
Chou, C.-F., Smith, A. J., & Omary, M. B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50611-1 · Cited by 212
Differential Mitotic Phosphorylation of Proteins of the Nuclear Pore Complex
Macaulay, C., Meier, E., & Forbes, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.254 · Cited by 199
Li, W., Li, F., Zhang, X., Lin, H., & Xu, C. S. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00825-8 · Cited by 211
Implication of Mammalian Ribosomal Protein S3 in the Processing of DNA Damage
Kim, J., Chubatsu, L. S., Admon, A., Stahl, J., Fellous, R., & Linn, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.13620 · Cited by 192
Hart, G. W. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90134-x · Cited by 193
Self-citationHexosamines as mediators of nutrient sensing and regulation in diabetes
McClain, D. A. (2002) · Journal of Diabetes and its Complications · doi:10.1016/s1056-8727(01)00188-x · Cited by 196
Gewinner, C. A., Hart, G. W., Zachara, N. E., Cole, R. N., Beisenherz-Huss, C., & Groner, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306449200 · Cited by 187
Self-citationGoldberg, M. W., Wiese, C., Allen, T., et al. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.4.409 · Cited by 174
Neurofilament proteins in neurodegenerative diseases
Liu, Q., Xie, F., Siedlak, S. L., Nunomura, A., Honda, K., Moreira, P. I., Zhua, X., Smith, M. A., & Perry, G. L. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4268-8 · Cited by 174
Sayeski, P. P., & Kudlow, J. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.15237 · Cited by 171
Analytical and Biochemical Perspectives of Protein O-GlcNAcylation
Ma, J., Wu, C., & Hart, G. W. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00884 · Cited by 172
Self-citationGlycopeptides and glycoproteins: Focus on the glycosidic linkage
Taylor, C. M. (1998) · Tetrahedron · doi:10.1016/s0040-4020(98)00477-3 · Cited by 168
Site‐specific interplay between O‐GlcNAcylation and phosphorylation in cellular regulation
Hu, P., Shimoji, S., & Hart, G. W. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.044 · Cited by 170
Self-citationAnnulate Lamellae: A Last Frontier in Cellular Organelles
Kessel, R. G. (1992) · International review of cytology · doi:10.1016/s0074-7696(08)61858-6 · Cited by 167
Factors controlling the glycosylation potential of the Golgi apparatus
Varki, A. P. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01198-7 · Cited by 165
Kelly, W. G., & Hart, G. W. (1989) · Cell · doi:10.1016/0092-8674(89)90962-8 · Cited by 166
Self-citationStavenhagen, K., Hinneburg, H., Thaysen‐Andersen, M., et al. (2013) · Journal of Mass Spectrometry · doi:10.1002/jms.3210 · Cited by 153
hnRNP G: sequence and characterization of a glycosylated RNA-binding protein
Soulard, M., Valle, V. D., Siomi, M. C., Piñol-Roma, S., Codogno, P., Bauvy, C., Bellini, M., Lacroix, J. C., Monod, G., Dreyfuss, G., et al. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.18.4210 · Cited by 145
Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation
Kuraya, M., Ming, Z., Liu, X., Matsushita, M., & Fujita, T. (2005) · Immunobiology · doi:10.1016/j.imbio.2004.11.001 · Cited by 143
Clostridium novyi α-Toxin-catalyzed Incorporation of GlcNAc into Rho Subfamily Proteins
Selzer, J., Hofmann, F., Rex, G., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25173 · Cited by 144
Hart, G. W., Kreppel, L. K., Comer, F. I., Arnold, C. S., Snow, D. M., Ye, Z., Cheng, X., Manna, D. L. D., Caine, D. S., Earles, B. J., et al. (1996) · Glycobiology · doi:10.1093/glycob/6.7.711 · Cited by 140
Self-citationO-Linked N-Acetylglucosamine: The “Yin-Yang” of Ser/Thr Phosphorylation?
Hart, G. W., Greis, K. D., Dong, L.-Y. D., Blomberg, M. A., Chou, T., Jiang, M., Roquemore, E. P., Snow, D. M., Kreppel, L. K., Cole, R. N., et al. (1995) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1885-3_10 · Cited by 138
Self-citation[26] Detection of O-Linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins
Roquemore, E. P., Chou, T., & Hart, G. W. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)30028-3 · Cited by 136
Self-citationLocalization of O-GlcNAc modification on the serum response transcription factor.
Reason, A. J., Morris, H. R., Panico, M., Marais, R., Treisman, R., Haltiwanger, R. S., Hart, G. W., Kelly, W. G., & Dell, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41871-6 · Cited by 131
Self-citationImmunodetection of multiple species of retinoic acid receptor α: Evidence for phosphorylation
Gaub, M. P., Rochette‐Egly, C., Lutz, Y., Ali, S., Matthes, H. W. D., Scheuer, I., & Chambon, P. (1992) · Experimental Cell Research · doi:10.1016/0014-4827(92)90282-d · Cited by 124
O-glycosyl α-amino acids as building blocks for glycopeptide synthesis
Arsequell, G., & Valencia, G. (1997) · Tetrahedron Asymmetry · doi:10.1016/s0957-4166(97)00326-1 · Cited by 124
Kamemura, K., & Hart, G. W. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01004-3 · Cited by 125
Self-citationGlithero, A., Tormo, J., Haurum, J. S., Arsequell, G., Valencia, G., Edwards, J. H., Springer, S., Townsend, A., Pao, Y., Wormald, M. R., et al. (1999) · Immunity · doi:10.1016/s1074-7613(00)80007-2 · Cited by 123
Chou, C.-F., & Omary, M. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53632-2 · Cited by 118
Crystal Structure of an MHC Class I Presented Glycopeptide that Generates Carbohydrate-Specific CTL
Speir, J. A., Abdel‐Motal, U. M., Jondal, M., & Wilson, I. A. (1999) · Immunity · doi:10.1016/s1074-7613(00)80006-0 · Cited by 118
Dong, D. L.-Y., Xu, Z.-S., Hart, G. W., & Cleveland, D. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20845 · Cited by 112
Self-citationNuclear import of glycoconjugates is distinct from the classical NLS pathway
Duverger, E., Pellerin-Mendes, C., Mayer, R., Roche, A., & Monsigny, M. L. P. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.4.1325 · Cited by 112
Davidson, H. W., & Balch, W. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53599-7 · Cited by 107
Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
Roquemore, E. P., Dell, A., Morris, H. R., Panico, M., Reason, A. J., Savoy, L.-A., Wistow, G. J., Zigler, J. S., Earles, B. J., & Hart, G. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48530-4 · Cited by 105
Self-citationIdentification of a soluble precursor complex essential for nuclear pore assembly in vitro
Dabauvalle, M., Loos, K., & Scheer, U. (1990) · Chromosoma · doi:10.1007/bf00337603 · Cited by 105
Overexpression of the UGT73C6 alters brassinosteroid glucoside formation in Arabidopsis thaliana
Husar, S., Berthiller, F., Fujioka, S., et al. (2011) · BMC Plant Biology · doi:10.1186/1471-2229-11-51 · Cited by 104
Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine
González, S. A., & Burrone, Ó. R. (1991) · Virology · doi:10.1016/0042-6822(91)90642-o · Cited by 102
O’Neill, R. A. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00502-1 · Cited by 102
Owen, J. B., Domenico, F. D., Rukhsana Sultana, A., Marzia Perluigi, A., Cini, C., Pierce, W. M. J., & Butterfield, D. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800667a · Cited by 102
Goldberg, M. W., & Allen, T. D. (1993) · Journal of Cell Science · doi:10.1242/jcs.106.1.261 · Cited by 100
O-Glycosylation of Nuclear and Cytoplasmic Proteins: Regulation Analogous to Phosphorylation?
Haltiwanger, R. S., Busby, S. A., Grove, K., Li, X., Mason, D., Medina, L., Moloney, D. J., Philipsberg, G. A., & Scartozzi, R. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6110 · Cited by 100
Self-citationSalvador, L. A., Elofsson, M., & Kihlberg, J. O. (1995) · Tetrahedron · doi:10.1016/0040-4020(95)00224-v · Cited by 100
Maternal-fetal cross-talk via the placenta: influence on offspring development and metabolism
Kramer, A. C., Jansson, T., Bale, T. L., & Powell, T. L. (2023) · Development · doi:10.1242/dev.202088 · Cited by 119
A glycopeptide in complex with MHC class I uses the GalNAc residue as an anchor
Apostolopoulos, V., Yuriev, E., Ramsland, P. A., Halton, J., Osinski, C., Li, W., Plebanski, M., Paulsen, H. M., & McKenzie, I. F. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2432220100 · Cited by 97
Detection and Analysis of Proteins Modified by O‐Linked N‐Acetylglucosamine
Zachara, N. E., Vosseller, K., & Hart, G. W. (2011) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1208s66 · Cited by 100
Self-citationFrost, R. A., & Tseng, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55239-x · Cited by 95
Demystifying the O-GlcNAc Code: A Systems View
Ma, J., Hou, C., & Wu, C. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01006 · Cited by 97
Radu, A.-M., Blobel, G., & Wozniak, R. W. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.1.1 · Cited by 89
Whitford, M. F., & Faulkner, P. (1992) · Journal of Virology · doi:10.1128/jvi.66.6.3324-3329.1992 · Cited by 88
Hsi, K.-L., Copeland, W. C., & Wang, T. S. ‐. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.21.6231 · Cited by 88
Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation.
Meier, E., Miller, B., & Forbes, D. J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.6.1459 · Cited by 86
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Jiang, M.-S., & Hart, G. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2421 · Cited by 83
Self-citationGianazza, E. (1995) · Journal of Chromatography A · doi:10.1016/0021-9673(94)01251-9 · Cited by 83
Nuclear and Cytoplasmic Glycosylation
Snow, D. M., & Hart, G. W. (1998) · International review of cytology · doi:10.1016/s0074-7696(08)60416-7 · Cited by 83
Self-citationOligosaccharides in vertebrate development
Varki, A. P., & Marth, J. D. (1995) · Seminars in Developmental Biology · doi:10.1016/s1044-5781(06)80022-8 · Cited by 79
Nuclear Transport of Human DDB Protein Induced by Ultraviolet Light
Liu, W., Nichols, A. F., Graham, J. A., Dualan, R., Abbas, A., & Linn, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000961200 · Cited by 81
Metadata
- Authors
- Hart, G. W., Haltiwanger, R. S., Holt, G. D., & Kelly, W. G.
- Affiliations
- Johns Hopkins University (US)
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1989-06
- Volume
- 58
- Issue
- 1
- Pages
- 841-874
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2101458293
- Cited by
- 386
- References
- 0
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 4 · 2023: 2 · 2022: 1 · 2021: 7 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 3 · 2012: 12
- FWCI
- 9.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA-42486)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD13563)
- 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 › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- lectin binding sites, high mobility group proteins, proteoglycans, glycosaminoglycans, glycogenin, viral glycoproteins, O-GlcNAc, endogenous lectins, glycoside hydrolases, glycosyltransferases
- MeSH terms
- Animals, Cell Nucleus, Cytoplasm, Glycoproteins, Glycosylation, Humans, Nucleoproteins, Lectins, Carbohydrate Metabolism
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