Cited by 386Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisProteoglycans and glycosaminoglycans research

The DOI matches its Crossref record.

GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM

Hart, Gerald W., Haltiwanger, Robert S., Holt, Gordon D., Kelly, William G.·1989·Annual Review of Biochemistry

DOI 10.1146/annurev.bi.58.070189.004205

Open this paper in CoChat — free account

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

Integrity signals

Registry

Crossref · 10.1146/annurev.bi.58.070189.004205

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Sorted by citations

Items 101–200 of 386

Glucose regulation of transforming growth factor-alpha expression is mediated by products of the hexosamine biosynthesis pathway
Daniels, M. C., Kansal, P., Smith, T. M., Paterson, A. J., Kudlow, J. E., & McClain, D. A. (1993) · Molecular Endocrinology · doi:10.1210/mend.7.8.8232303 · Cited by 84
UDP-glucosyltransferase PpUGT85A2 controls volatile glycosylation in peach
Wu, B., Cao, X., Liu, H., et al. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery419 · Cited by 79
Dynamic Nuclear and Cytoplasmic Glycosylation: Enzymes of O-GlcNAc Cycling
Iyer, S. P. N., & Hart, G. W. (2003) · Biochemistry · doi:10.1021/bi020685a · Cited by 79
Self-citation
Effect of okadaic acid on O-linked N-acetylglucosamine levels in a neuroblastoma cell line
Lefebvre, T., Alonso, C., Mahboub, S., Dupire, M.-J., Zanetta, J., Caillet‐Boudin, M., & Michalski, J. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00105-1 · Cited by 78
Phosphorylation Generates Different Forms of Rotavirus NSP5
Afrikanova, I., Miozzo, M. C., Giambiagi, S., et al. (1996) · Journal of General Virology · doi:10.1099/0022-1317-77-9-2059 · Cited by 77
Molecular cloning and characterization of the acidic 80-kDa protein kinase C substrate from rat brain. Identification as a glycoprotein.
Erusalimsky, J. D., Brooks, S. F., Herget, T., Morris, C., & Rozengurt, E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89611-2 · Cited by 76
Amino acid sequence of rat kidney glutathione synthetase.
Huang, C. S., Wei, H., Meister, A., et al. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1232 · Cited by 76
Peptide anchor residue glycosylation: effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition
Haurum, J. S., Tan, L., Arsequell, G., Frodsham, P., Lellouch, A. C., Moss, P. A. H., Dwek, R. A., McMichael, A. J., & Elliott, T. J. (1995) · European Journal of Immunology · doi:10.1002/eji.1830251211 · Cited by 76
Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies.
Turner, J. R., Tartakoff, A. M., & Greenspan, N. S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5608 · Cited by 75
Radioactive tracer techniques in the sequencing of glycoprotein oligosaccharides
Varki, A. P. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.2.2004668 · Cited by 75
Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.
Heese-Peck, A., Cole, R. N., Borkhsenious, O. N., Hart, G. W., & Raikhel, N. V. (1995) · The Plant Cell · doi:10.1105/tpc.7.9.1459 · Cited by 75
Self-citation
Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.
Hakes, D. J., & Berezney, R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6186 · Cited by 75
Expression of the Arabidopsis gai gene under its own promoter causes a reduction in plant height in chrysanthemum by attenuation of the gibberellin response
Petty, L., Harberd, N. P., Carré, I. A., Thomas, B., & Jackson, S. D. (2003) · Plant Science · doi:10.1016/s0168-9452(02)00380-1 · Cited by 73
The Cytoplasmic F-box Binding Protein SKP1 Contains a Novel Pentasaccharide Linked to Hydroxyproline inDictyostelium
Teng-umnuay, P., Morris, H. R., Dell, A., Panico, M., Paxton, T., & West, C. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18242 · Cited by 75
Impaired Vasodilator Activity in Deoxycorticosterone Acetate-Salt Hypertension Is Associated With Increased Protein O-GlcNAcylation
Lima, V. V., Giachini, F. R. C., Choi, H., Carneiro, F. S., Carneiro, Z. N., Fortes, Z. B., de Carvalho, M. H. C., Webb, R. C., & Tostes, R. C. (2009) · Hypertension · doi:10.1161/hypertensionaha.108.116798 · Cited by 72
Protein O-GlcNAc Modulates Motility-associated Signaling Intermediates in Neutrophils
Kneass, Z. T., & Marchase, R. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414066200 · Cited by 70
Evidence for virus-encoded glycosylation specificity.
Wang, I. N., Li, Y., Que, Q. Q., et al. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.3840 · Cited by 67
Phosphoglycosylation: A new structural class of glycosylation?
Haynes, P. A. (1998) · Glycobiology · doi:10.1093/glycob/8.1.1 · Cited by 67
O-GlcNAcylation contributes to the vascular effects of ET-1 via activation of the RhoA/Rho-kinase pathway
Lima, V. V., Giachini, F. R. C., Carneiro, F. S., de Carvalho, M. H. C., Fortes, Z. B., Webb, R. C., & Tostes, R. C. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq338 · Cited by 66
Construction of a Database of Collision Cross Section Values for Glycopeptides, Glycans, and Peptides Determined by IM-MS
Glaskin, R. S., Khatri, K., Wang, Q., Zaia, J., & Costello, C. E. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04146 · Cited by 65
Exploring the glycan repertoire of genetically modified mice by isolation and profiling of the major glycan classes and nano-NMR analysis of glycan mixtures
Manzi, A. E., Norgard-Sumnicht, K. E., Argade, S. P., Marth, J. D., van HALBEEK, H., & Varki, A. P. (2000) · Glycobiology · doi:10.1093/glycob/10.7.669 · Cited by 64
Characterization of protein glycosylation by mass spectrometry
Burlingame, A. L. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80088-7 · Cited by 65
Prediction of Glycosylation Sites in Proteins
Julenius, K., Johansen, M. B., Zhang, Y., Brunak, S., & Gupta, R. (2009) · doi:10.1002/9780470029619.ch9 · Cited by 65
High Molecular Weight Microtubule-associated Proteins Contain O-Linked N-Acetylglucosamine
Ding, M., & Vandré, D. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12555 · Cited by 64
The Nuclear Pore Complex Protein p62 Is One of Several Sialic Acid-containing Proteins of the Nuclear Envelope
Emig, S., Schmalz, D., Shakibaei, M., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.13787 · Cited by 63
Identification and Mutational Analysis of the Glycosylation Sites of Human Keratin 18
Ku, N., & Omary, M. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11820 · Cited by 63
Commentary soluble vertebrate lectins: Ubiquitous but inscrutable proteins
Harrison, F. L. (1991) · Journal of Cell Science · doi:10.1242/jcs.100.1.9 · Cited by 63
GROWTH REGULATING FACTOR 7-mediated arbutin metabolism enhances rice salt tolerance
Chen, Y., Dan, Z., & Li, S. (2024) · The Plant Cell · doi:10.1093/plcell/koae140 · Cited by 62
Neutrophils Exhibit Rapid Agonist-induced Increases in Protein-associated O-GlcNAc
Kneass, Z. T., & Marchase, R. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407911200 · Cited by 62
Functional nuclear pores reconstituted with beta 1-4 galactose-modified O-linked N-acetylglucosamine glycoproteins.
Miller, M. W., & Hanover, J. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37106-5 · Cited by 62
Intracellular posttranslational modifications of S1133 avian reovirus proteins
Varela, R., Martı́nez-Costas, J., Mallo, M., et al. (1996) · Journal of Virology · doi:10.1128/jvi.70.5.2974-2981.1996 · Cited by 61
Identification of EFEMP2 as a Serum Biomarker for the Early Detection of Colorectal Cancer with Lectin Affinity Capture Assisted Secretome Analysis of Cultured Fresh Tissues
Yao, L., Lao, W., Zhang, Y., Tang, X., Hu, X., He, C., Xu, L. X., & Xu, L. X. (2012) · Journal of Proteome Research · doi:10.1021/pr300020p · Cited by 59
Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II
Pohl, T., & Waldmann, H. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970709e · Cited by 59
Role of glucosamine synthesis in the stimulation of TGF-alpha gene transcription by glucose and EGF
Roos, M. D., Han, I., Paterson, A. J., & Kudlow, J. E. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.270.3.c803 · Cited by 56
Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAc’s
Chou, C.-F., & Omary, M. B. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.7.1833 · Cited by 56
Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain
Murphy, J. E., Hanover, J. A., Froehlich, M., DuBois, G., & Keen, J. H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31968-3 · Cited by 54
Studies on O‐glycans of Plasmodium‐falciparum‐infected human erythrocytes Evidence for O‐GlcNAc and O‐GlcNAc‐transferase in malaria parasites
Dieckmann-Schuppert, A., Bause, E., & Schwarz, R. Τ. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18198.x · Cited by 55
The cytoskeletal protein talin is O-glycosylated.
Hagmann, J., Grob, M., & Burger, M. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49729-9 · Cited by 54
[2] Metabolic radiolabeling of glycoconjugates
Varki, A. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)30004-6 · Cited by 54
Carbohydrates and antigen recognition by T cells
Carbone, F., & Gleeson, P. A. (1997) · Glycobiology · doi:10.1093/glycob/7.6.725-d · Cited by 52
The analysis of fluorophore-labeled carbohydrates by polyacrylamide gel electrophoresis
Jackson, P. (1996) · Molecular Biotechnology · doi:10.1007/bf02789060 · Cited by 53
N‐Terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface
Baratova, L. A., Fedorova, N. V., Dobrov, E. N., et al. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04243.x · Cited by 52
DNA replication in cell-free extracts from Xenopus eggs is prevented by disrupting nuclear envelope function
Cox, L. S. (1992) · Journal of Cell Science · doi:10.1242/jcs.101.1.43 · Cited by 52
Nuclear assembly with lambda DNA in fractionated Xenopus egg extracts: an unexpected role for glycogen in formation of a higher order chromatin intermediate
Hartl, P. M., Olson, E. C., Dang, T., et al. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.3.235 · Cited by 52
Identifying the CHO Secretome using Mucin-type O-Linked Glycosylation and Click-chemistry
Slade, P. G., Hajivandi, M., Bartel, C. M., & Gorfien, S. F. (2012) · Journal of Proteome Research · doi:10.1021/pr300810f · Cited by 51
Dithiasuccinoyl (Dts) amino-protecting group used in syntheses of 1,2-trans-amino sugar glycosides
Meinjohanns, E., Meldal, M., Paulsen, H. M., et al. (1995) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/p19950000405 · Cited by 51
O-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension
Lima, V. V., Rigsby, C. S., Hardy, D. M., Webb, R. C., & Tostes, R. C. (2009) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2009.09.004 · Cited by 53
Purification to Homogeneity and Properties of UDP-GlcNAc (GalNAc) Pyrophosphorylase
Szumilo, T., Zeng, Y., Pastuszak, I., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13147 · Cited by 48
UDP-N-acetylglucosamine transferase and glutamine: fructose 6-phosphate amidotransferase activities in insulin-sensitive tissues
Yki-Järvinen, H., Vogt, C., Iozzo, P., Pipek, R., Daniels, M. C., Virkamäki, A., Mäkimattila, S., Mandarino, L. J., DeFronzo, R. A., McClain, D. A., et al. (1997) · Diabetologia · doi:10.1007/s001250050645 · Cited by 46
Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of equine herpesvirus 1 and 4
Whittaker, G. R., Riggio, M. P., Halliburton, I. W., et al. (1991) · Journal of Virology · doi:10.1128/jvi.65.5.2320-2326.1991 · Cited by 47
Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O‐Glc NA c)
Zachara, N. E. (2018) · FEBS Letters · doi:10.1002/1873-3468.13286 · Cited by 44
Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration
Han, I., Oh, E., & Kudlow, J. E. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3500109 · Cited by 46
Chapter 2 Primary Structure of Glycoprotein Glycans
Vliegenthart, J. F. G., & Montreuil, J. (1995) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60585-2 · Cited by 46
Synthetic peptide conjugates—tailor-made probes for the biology of protein modification and protein processing
Seitz, O., Heinemann, I., Mattes, A., & Waldmann, H. (2001) · Tetrahedron · doi:10.1016/s0040-4020(00)01115-7 · Cited by 46
A cytoplasmic prolyl hydroxylation and glycosylation pathway modifies Skp1 and regulates O2-dependent development in Dictyostelium
West, C. M., Wang, Z. A., & van der Wel, H. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.11.006 · Cited by 43
O-GlcNAcylation: a novel pathway contributing to the effects of endothelin in the vasculature
Lima, V. V., Giachini, F. R. C., Hardy, D. M., Webb, R. C., & Tostes, R. C. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00230.2010 · Cited by 47
Folding of branched RNA species
Lilley, D. M. J. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(1998)48:2 · Cited by 37
GLUCOSAMINE ADMINISTRATION IMPROVES SURVIVAL RATE AFTER SEVERE HEMORRHAGIC SHOCK COMBINED WITH TRAUMA IN RATS
Nöt, L. G., Marchase, R. B., Fülöp, N., Brocks, C. A., & Chatham, J. C. (2007) · Shock · doi:10.1097/shk.0b013e3180487ebb · Cited by 45
Transcriptional regulation by butyrate of mouse galectin-1 gene in embryonal carcinoma cells
Lu, Y. W., & Lotan, R. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00257-7 · Cited by 43
Synapsins Contain O‐Linked N‐Acetylglucosamine
Liithi, T., Haltiwanger, R. S., Greengard, P., & Bähler, M. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02043.x · Cited by 43
Self-citation
Historical Overview of Glycoanalysis
Bielik, A. M., & Zaia, J. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-454-8_2 · Cited by 41
Emerging roles of protein O-GlcNAcylation in cardiovascular diseases: Insights and novel therapeutic targets
Bolanle, I. O., Riches‐Suman, K., Williamson, R., & Palmer, T. M. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105467 · Cited by 44
UDP-N-acetylglucosamine Pyrophosphorylase, a Key Enzyme in Encysting Giardia, Is Allosterically Regulated
Bulik, D. A., OPHEM, P. W. V., Manning, J. M., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14722 · Cited by 40
Characterization of FP21, a Cytosolic Glycoprotein from Dictyostelium
Kozarov, E. V., van der Wel, H., Field, M., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3022 · Cited by 40
Monitoring Human Milk β-Casein Phosphorylation and O-Glycosylation Over Lactation Reveals Distinct Differences between the Proteome and Endogenous Peptidome
Dingess, K. A., Gazi, I., van den Toorn, H., Mank, M., Stahl, B., Reiding, K. R., & Heck, A. J. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158140 · Cited by 39
Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.
Mariller, C., Hardivillé, S., Hoedt, E., Huvent, I., Pina-Canseco, M. D. S., & Pierce, A. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-070 · Cited by 39
Topology of O-linked N-acetylglucosamine in murine lymphocytes
Kearse, K. P., & Hart, G. W. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90579-8 · Cited by 39
Self-citation
An intrinsic membrane glycoprotein with cytosolically oriented n-linked sugars.
Pedemonte, C. H., Sachs, G. M., & Kaplan, J. H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9789 · Cited by 39
The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae.
Dey, N. B., Bounelis, P., Fritz, T. A., Bedwell, D. M., & Marchase, R. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47136-0 · Cited by 38
ALG gene expression and cell cycle progression
Kukuruzinska, M. A., & Lennon-Hopkins, K. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(98)00136-6 · Cited by 38
Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins
West, C. M., van der Wel, H., & Gaucher, E. A. (2002) · Glycobiology · doi:10.1093/glycob/12.2.17r · Cited by 39
Targeting of drugs to various blood cell types using (neo-)glycoproteins, antibodies and other protein carriers
Molema, G., & Meijer, D. K. F. (1994) · Advanced Drug Delivery Reviews · doi:10.1016/0169-409x(94)90004-3 · Cited by 38
Glycosyltransferase Structure and Function
Schuman, B., Alfaro, J. A., & Evans, S. V. (2006) · Topics in Current Chemistry · doi:10.1007/128_2006_089 · Cited by 37
Versatile solid-phase thiolytic reduction of azido and N-Dts groups in the synthesis of haemoglobin (67–76) O-glycopeptides and photoaffinity labelled analogues to study glycan T-cell specificity
Meinjohanns, E., Meldal, M., Jensen, T., Werdelin, O., Galli‐Stampino, L., Mouritsen, S., & Bock, K. (1997) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/a606725e · Cited by 37
Initiation Binding Receptor, a Factor That Binds to the Transcription Initiation Site of the Histone h5 Gene, Is a Glycosylated Member of a Family of Cell Growth Regulators
Gómez-Cuadrado, A., Martı́n, M., Noël, M., & Ruiz-Carrillo, A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6670 · Cited by 37
Glycosylation in Intestinal Epithelium
Taatjes, D. J., & Roth, J. (1991) · International review of cytology · doi:10.1016/s0074-7696(08)60684-1 · Cited by 37
Immunocytochemical Localization of Chondroitin and Chondroitin 4‐ and 6‐Sulfates in Developing Rat Cerebellum
Flaccus, A., Janetzko, A., Tekotte, H., et al. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb02058.x · Cited by 37
Chromatin supraorganization and extensibility in mouse hepatocytes with development and aging
Moraes, A. D. S., Guaraldo, A. M. A., & Mello, M. L. S. (2007) · Cytometry Part A · doi:10.1002/cyto.a.20356 · Cited by 36
Tuning the conformation properties of a peptide by glycosylation and phosphorylation
Liang, F., Chen, R. P. ‐., Lin, C., Huang, K., & Chan, S. I. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.168 · Cited by 35
Detection and Analysis of Proteins Modified by O‐Linked N‐Acetylglucosamine
Zachara, N. E., Cole, R. N., Hart, G. W., et al. (2001) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1208s25 · Cited by 35
Self-citation
Hexosamine regulation of glucose-mediated laminin synthesis in mesangial cells involves protein kinases A and C
Singh, L. P., & Crook, E. D. (2000) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2000.279.4.f646 · Cited by 35
Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase
Han, J. W., Valdez, J. L., Ho, D. V., Lee, C. S., Kim, H. M., Wang, X., Huang, L., & Chan, J. Y. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.06.008 · Cited by 35
Chromatin supraorganization and extensibility in mouse hepatocytes following starvation and refeeding
Moraes, A. D. S., Vidal, B. D. C., Guaraldo, A. M. A., et al. (2005) · Cytometry Part A · doi:10.1002/cyto.a.20113 · Cited by 34
Effect of β‐O‐Glucosylation on L ‐Ser and L ‐Thr Diamides: A Bias toward α‐Helical Conformations
Corzana, F., Busto, J. H., Engelsen, S. B., et al. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200600128 · Cited by 34
Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis
Yang, T., Echols, M., Martin, A., et al. (2010) · Biochemical Journal · doi:10.1042/bj20100315 · Cited by 34
Human meprinbeta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion
Leuenberger, B., Hahn, D., Pischitzis, A., Hansen, M. K., & Sterchi, E. E. (2003) · Biochemical Journal · doi:10.1042/bj20021398 · Cited by 33
Evidence for a glycoconjugate form of glutathione S‐transferase pI
Kuzmich, S., Vanderveer, L., & Tew, K. D. (1991) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1991.tb00776.x · Cited by 34
Nuclear localization of an o-glycosylated protein phosphotyrosine phosphatase from human cells
Meikrantz, W., Smith, D. M., Sladicka, M. M., et al. (1991) · Journal of Cell Science · doi:10.1242/jcs.98.3.303 · Cited by 34
Histochemical and Cytochemical Localization of Blood Group Antigens
Ito, N., & Hirota, T. (1992) · Progress in Histochemistry and Cytochemistry · doi:10.1016/s0079-6336(11)80056-2 · Cited by 34
A stereoselective synthesis of a C-glycosylated peptoid building block
Dechantsreiter, M. A., Burkhart, F., & Kessler, H. (1998) · Tetrahedron Letters · doi:10.1016/s0040-4039(97)10566-4 · Cited by 33
Efficient synthesis of O-(2-acetamido-2-deoxy-β-D- glucopyranosyl)-serine and -threonine building blocks for glycopeptide formation
Saha, U. K., & Schmidt, R. R. (1997) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/a700210f · Cited by 33
A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes
Ewald, A., Kossner, U., Scheer, U., et al. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.7.1813 · Cited by 33
Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase.
Marchase, R. B., Bounelis, P., Brumley, L. M., Dey, N. B., Browne, B. L., Auger, D., Fritz, T. A., Kulesza, P. J., & Bedwell, D. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53101-x · Cited by 33
A novel 43-kDa glycoprotein is detected in the nucleus of mammalian cells by autoantibodies from dogs with autoimmune disorders
Soulard, M., Barque, J.-P., Valle, V. D., et al. (1991) · Experimental Cell Research · doi:10.1016/0014-4827(91)90538-6 · Cited by 33
Highly stereoselective α-glycosylation with GalN 3 donors enabled collective synthesis of mucin-related tumor associated carbohydrate antigens
Shou, K., Zhang, Y., Ji, Y., et al. (2024) · Chemical Science · doi:10.1039/d4sc01348d · Cited by 32
Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver.
Satir, B. H., Srisomsap, C., Reichman, M., et al. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.901 · Cited by 32
Identification of Subtilase Cytotoxin (SubAB) Receptors Whose Signaling, in Association with SubAB-Induced BiP Cleavage, Is Responsible for Apoptosis in HeLa Cells
Yahiro, K., Satoh, M., Morinaga, N., Tsutsuki, H., Ogura, K., Nagasawa, S., Nomura, F., Moss, J., & Noda, M. (2010) · Infection and Immunity · doi:10.1128/iai.01020-10 · Cited by 31
Do de-N-glycosylation enzymes have an important role in plant cells?
Berger, S. L., Menudier, A., Julien, R., & Karamanos, Y. (1995) · Biochimie · doi:10.1016/0300-9084(96)88193-4 · Cited by 30
A mutation in the signal recognition particle 7S RNA of the yeast Yarrowia lipolytica preferentially affects synthesis of the alkaline extracellular protease: in vivo evidence for translational arrest.
Yaver, D., Matoba, S., & Ogrydziak, D. M. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.116.3.605 · Cited by 31
Efficient synthesis of O-(2-acetamido-2-deoxy-β-d-glucopyranosyl)-ser/thr building blocks for spps of o-glcnac glycopeptides
Meinjohanns, E., Meldal, M., & Bock, K. (1995) · Tetrahedron Letters · doi:10.1016/0040-4039(95)01941-a · Cited by 31

Authors: Hart, G. W., Haltiwanger, R. S., Holt, G. D., & Kelly, W. G.
Affiliations: Johns Hopkins University (US)
ORCID: Hart, Gerald W.
Haltiwanger, Robert S.
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
DOI: 10.1146/annurev.bi.58.070189.004205
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

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

GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Citations

Cited by

Related

Metadata

Record

About these checks