GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM

Biological roles of glycans

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

Prediction of post‐translational glycosylation and phosphorylation of proteins from the amino acid sequence

Blom, N., Sicheritz‐Pontén, T., Gupta, R., Gammeltoft, S., & Brunak, S. (2004) · PROTEOMICS · doi:10.1002/pmic.200300771 · Cited by 2,076 · see citing works

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 · see citing works

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 · see citing works

Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Hart, 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 · see citing works

Protein glycosylation

Lis, H., & Sharon, N. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18347.x · Cited by 840 · see citing works

Biology of Animal Lectins

Drickamer, K., & Taylor, M. E. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.001321 · Cited by 777 · see citing works

Why are proteins O-glycosylated?

Jentoft, N. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90014-3 · Cited by 705 · see citing works

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 · see citing works

Nuclear protein localization

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 · see citing works

How proteins enter the nucleus

Silver, P. A. (1991) · Cell · doi:10.1016/0092-8674(91)90233-o · Cited by 553 · see citing works

H OW G IBBERELLIN R EGULATES P LANT G ROWTH AND D EVELOPMENT : A Molecular Genetic Analysis of Gibberellin Signaling

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 · see citing works

Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol.

Dong, D. L., & Hart, G. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32170-1 · Cited by 508 · see citing works

DYNAMIC 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 · see citing works

The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes. A role in osteoarthritis.

Reboul, P., Pelletier, J., Tardif, G., Cloutier, J. M., & Martel‐Pelletier, J. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118636 · Cited by 488 · see citing works

c-Myc Is Glycosylated at Threonine 58, a Known Phosphorylation Site and a Mutational Hot Spot in Lymphomas

Chou, T.-Y., Hart, G. W., & Dang, C. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18961 · Cited by 453 · see citing works

Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.

Haltiwanger, R. S., Blomberg, M. A., & Hart, G. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50380-5 · Cited by 444 · see citing works

Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase.

Haltiwanger, R. S., Holt, G. D., & Hart, G. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39838-2 · Cited by 372 · see citing works

O-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 · see citing works

The 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 · see citing works

O-Glycosylation of the Mucin Type

Hanisch, F. (2001) · Biological Chemistry · doi:10.1515/bc.2001.022 · Cited by 322 · see citing works

Protein Glycosylation, Conserved from Yeast to Man: A Model Organism Helps Elucidate Congenital Human Diseases

Lehle, L., Strahl, S., & Tanner, W. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601645 · Cited by 314 · see citing works

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 · see citing works

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 307 · see citing works

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 299 · see citing works

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

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 · see citing works

Protein O-mannosylation

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 · see citing works

Dual Function of the Voltage-Dependent Ca2+ Channel α2δ Subunit in Current Stimulation and Subunit Interaction

Gurnett, C. A., WAARD, M. M. D., & Campbell, K. P. (1996) · Neuron · doi:10.1016/s0896-6273(00)80061-6 · Cited by 291 · see citing works

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 · see citing works

Protein 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 · see citing works

Isolation and characterization of developmentally regulated chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of brain identified with monoclonal antibodies

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 · see citing works

Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes.

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 · see citing works

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 250 · see citing works

The human CAN protein, a putative oncogene productassociated with myeloid leukemogenesis, is a nuclear pore complex protein thatfaces the cytoplasm.

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 · see citing works

The nuclear matrix: A heuristic model for investigating genomic organization and function in the cell nucleus

Berezney, R. (1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240470204 · Cited by 237 · see citing works

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 · see citing works

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 · see citing works

High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores.

Goldberg, M. W., & Allen, T. D. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.6.1429 · Cited by 230 · see citing works

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 · see citing works

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 · see citing works

O 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 · see citing works

Leukocyte Adhesion

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 · see citing works

Preparation and Antimalarial Activities of “Trioxaquines”, New Modular Molecules with a Trioxane Skeleton Linked to a 4-Aminoquinoline

Dechy‐Cabaret, O., Benoit‐Vical, F., Robert, A., & Meunier, B. (2000) · ChemBioChem · doi:10.1002/1439-7633(20001117)1:4 · Cited by 160 · see citing works

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 · see citing works

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 208 · see citing works

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 · see citing works

Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment

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 203 · see citing works

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 · see citing works

Glycosylation

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

Hexosamines 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 193 · see citing works

The Coactivator of Transcription CREB-binding Protein Interacts Preferentially with the Glycosylated Form of Stat5

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 178 · see citing works

Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly

Goldberg, M. W., Wiese, C., Allen, T., et al. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.4.409 · Cited by 174 · see citing works

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 172 · see citing works

Glucose Metabolism to Glucosamine Is Necessary for Glucose Stimulation of Transforming Growth Factor-α Gene Transcription

Sayeski, P. P., & Kudlow, J. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.15237 · Cited by 171 · see citing works

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 171 · see citing works

Glycopeptides and glycoproteins: Focus on the glycosidic linkage

Taylor, C. M. (1998) · Tetrahedron · doi:10.1016/s0040-4020(98)00477-3 · Cited by 168 · see citing works

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 167 · see citing works

Annulate 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 · see citing works

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 · see citing works

Glycosylation of chromosomal proteins: Localization of O-linked N-acetylglucosamine in Drosophila chromatin

Kelly, W. G., & Hart, G. W. (1989) · Cell · doi:10.1016/0092-8674(89)90962-8 · Cited by 166 · see citing works

Quantitative mapping of glycoprotein micro‐heterogeneity and macro‐heterogeneity: an evaluation of mass spectrometry signal strengths using synthetic peptides and glycopeptides

Stavenhagen, K., Hinneburg, H., Thaysen‐Andersen, M., et al. (2013) · Journal of Mass Spectrometry · doi:10.1002/jms.3210 · Cited by 153 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

O-GlcNAcylation of key nuclear and cytoskeletal proteins: reciprocity with O-phosphorylation and putative roles in protein multimerization

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 · see citing works

O-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 · see citing works

[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 · see citing works

Localization 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 · see citing works

Immunodetection 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 · see citing works

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 · see citing works

Dynamic Interplay between O-Glycosylation and O-Phosphorylation of Nucleocytoplasmic Proteins: A New Paradigm for Metabolic Control of Signal Transduction and Transcription

Kamemura, K., & Hart, G. W. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01004-3 · Cited by 122 · see citing works

Crystal Structures of Two H-2Db/Glycopeptide Complexes Suggest a Molecular Basis for CTL Cross-Reactivity

Glithero, 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 · see citing works

Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18.

Chou, C.-F., & Omary, M. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53632-2 · Cited by 118 · see citing works

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 · see citing works

Cytoplasmic O-GlcNAc Modification of the Head Domain and the KSP Repeat Motif of the Neurofilament Protein Neurofilament-H

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 · see citing works

Nuclear 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 · see citing works

Differential inhibition of multiple vesicular transport steps between the endoplasmic reticulum and trans Golgi network.

Davidson, H. W., & Balch, W. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53599-7 · Cited by 107 · see citing works

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 · see citing works

Identification 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 · see citing works

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 · see citing works

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 · see citing works

Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis

O’Neill, R. A. (1996) · Journal of Chromatography A · doi:10.1016/0021-9673(95)00502-1 · Cited by 102 · see citing works

Proteomics-Determined Differences in the Concanavalin-A-Fractionated Proteome of Hippocampus and Inferior Parietal Lobule in Subjects with Alzheimer’s Disease and Mild Cognitive Impairment: Implications for Progression of AD

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 100 · see citing works

The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis

Goldberg, M. W., & Allen, T. D. (1993) · Journal of Cell Science · doi:10.1242/jcs.106.1.261 · Cited by 100 · see citing works

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 · see citing works

Preparation of building blocks for glycopeptide synthesis by glycosylation of Fmoc amino acids having unprotected carboxyl groups

Salvador, L. A., Elofsson, M., & Kihlberg, J. O. (1995) · Tetrahedron · doi:10.1016/0040-4020(95)00224-v · Cited by 100 · see citing works

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 110 · see citing works

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 · see citing works

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 96 · see citing works

Insulin-like growth factor-binding protein-1 is phosphorylated by cultured human endometrial stromal cells and multiple protein kinases in vitro.

Frost, R. A., & Tseng, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55239-x · Cited by 95 · see citing works

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 96 · see citing works

Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA.

Radu, A.-M., Blobel, G., & Wozniak, R. W. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.1.1 · Cited by 89 · see citing works

A structural polypeptide of the baculovirus Autographa californica nuclear polyhedrosis virus contains O-linked N-acetylglucosamine

Whitford, M. F., & Faulkner, P. (1992) · Journal of Virology · doi:10.1128/jvi.66.6.3324-3329.1992 · Cited by 88 · see citing works

Human DNA polymerase α catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus

Hsi, K.-L., Copeland, W. C., & Wang, T. S. ‐. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.21.6231 · Cited by 88 · see citing works

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 · see citing works

A Subpopulation of Estrogen Receptors Are Modified by O-Linked N-Acetylglucosamine

Jiang, M.-S., & Hart, G. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2421 · Cited by 83 · see citing works

Isoelectric focusing as a tool for the investigation of post-translational processing and chemical modifications of proteins

Gianazza, E. (1995) · Journal of Chromatography A · doi:10.1016/0021-9673(94)01251-9 · Cited by 83 · see citing works

Nuclear and Cytoplasmic Glycosylation

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