GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM

An Evaluation of Sialation of the Nucleoporin p62

Fang, B., Hanover, J. A., & Miller, M. W. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0767 · Cited by 6

Chemical and enzymatic synthesis of glycopeptides

Schultz, M., & Kunz, H. (1995) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-9061-8_10 · Cited by 6

Metabolic Radiolabeling of Animal Cell Glycoconjugates

Diaz, S. L., & Varki, A. P. (2009) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb1704s87 · Cited by 6

The Nuclear Matrix: Structure, Function and DNA Replication

Berezney, R. (1992) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60173-3 · Cited by 6

Glycosylation of Nuclear and Cytoplasmic Proteins Is as Abundant and as Dynamic as Phosphorylation

Hart, G. W., Kelly, W. G., Blomberg, M. A., Roquemore, E. P., Dong, L.-Y. D., Kreppel, L. K., Chou, T., Snow, D. M., & Greis, K. D. (1994) · Springer eBooks · doi:10.1007/978-3-642-78729-4_10 · Cited by 6

Use of Mammalian Cell Mutants to Study the Functions of N- and O-Linked Glycosylation

Stanley, P. (1993) · Elsevier eBooks · doi:10.1016/b978-0-12-589630-6.50010-1 · Cited by 6

Identification of novel O-GlcNAc transferase substrates using yeast cells expressing OGT

Li, F., Yang, G., Tachikawa, H., Shao, K., Yan, Y., Gao, X., & Nakanishi, H. (2020) · The Journal of General and Applied Microbiology · doi:10.2323/jgam.2020.04.002 · Cited by 5

Chapter 2c Glycoproteins of parasites

(1996) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60282-3 · Cited by 5

Synthesis of cell-wall glycoproteins and their characterization in oat coleoptiles

Pacoda, D., Montefusco, A., Piro, G., et al. (1997) · Phytochemistry · doi:10.1016/s0031-9422(96)00883-7 · Cited by 5

Effects of endogenous soluble β-galactoside binding lectins and protein inhibitor of fucosyltransferase on the enzymes involved in the intestinal fucosylation process

Ruggiero-Lopez, D., Louisot, P., & Martin, A. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91669-h · Cited by 5

Ubiquitin-RAS peptide extensions as substrates for farnesyl-protein transferase and carboxymethyltransferase

Yoo, Y., Watts, S. G., & RECHSTEINER, M. C. (1992) · Biochemical Journal · doi:10.1042/bj2850055 · Cited by 5

Structural and Functional Diversity of Glycoconjugates: A Formidable Challenge to the Glycoanalyst

Hart, G. W. (2003) · Humana Press eBooks · doi:10.1385/1-59259-294-5:3 · Cited by 4

Distribution of O-GlcNAc Transferase in the Rat Pancreas.

Akimoto, Y., Hart, G. W., & Hirano, H. (2000) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.33.163 · Cited by 4

Glycoproteins with N-Acetylglucosamine and Mannose Residues in Chinese Hamster Metaphase Chromosomes

Myllyharju, J., & Nokkala, S. (2004) · Hereditas · doi:10.1111/j.1601-5223.1996.00251.x · Cited by 4

Ultrastructural localization ofl-fucose residues in nuclei of root primordia of the green peaPisum sativum

Chamberland, H., & Lafontaine, J. G. (1992) · The Histochemical Journal · doi:10.1007/bf01043280 · Cited by 4

Investigation of glycosylation processes in mitochondria and microsomal membranes from human skeletal muscle

Gasnier, F., Lermé, F., Rousson, R., et al. (1991) · Clinica Chimica Acta · doi:10.1016/0009-8981(91)90010-a · Cited by 4

Bovine pancreatic DNase I binds very tightly to DNA fragments and may be mistaken for putative endogenous nuclear proteins convalently bound to DNA

Brotherton, T. W., & Zenk, D. W. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91965-u · Cited by 4

Enzymatic Approaches to Glycoprotein Synthesis

Sears, P. S., Tolbert, T. J., & Wong, C. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-47572-3_4 · Cited by 4

Developmental association of the β-galactoside-binding protein galectin-1 with the nuclear matrix of rat calvarial osteoblasts

Choi, J., van Wijnen, A. J., Aslam, F., et al. (1998) · Journal of Cell Science · doi:10.1242/jcs.20.111.3035 · Cited by 4

Do T2DM and Hyperglycaemia Affect the Expression Levels of the Regulating Enzymes of Cellular O-GlcNAcylation in Human Saphenous Vein Smooth Muscle Cells?

Bolanle, I. O., Durham, G. A., Hobkirk, J., et al. (2024) · Diabetology · doi:10.3390/diabetology5020013 · Cited by 3

Nuclear and cytoplasmic glycoproteins

Greis, K. D., & Hart, G. W. (1997) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60615-8 · Cited by 3

Nuclear glycoproteins of hamster liver and kirkman-robbins hepatoma recognized by concanavalin A

Lipińska, A., & Gaczyński, M. (1992) · International Journal of Biochemistry · doi:10.1016/0020-711x(92)90063-7 · Cited by 3

PEF-1, an epithelial cell transcription factor which activates the long control region of human papillomavirus type 16, is glycosylated with N-acetylglucosamine.

Fergusson, D. A., & Campo, M. S. (1998) · Journal of General Virology · doi:10.1099/0022-1317-79-11-2753 · Cited by 3

Glycoconjugate Profiles of Insect Spermatogenesis: Lectin Cytochemical Analysis of the Cricket, Gryllus bimaculatus

Suzuki, A., & Nishimura, K. J. (1997) · ZOOLOGICAL SCIENCE · doi:10.2108/zsj.14.455 · Cited by 3

Synthetic Methods to Incorporate α‐Linked 2‐Amino‐2‐deoxy‐D‐glucopyranoside and 2‐Amino‐2‐deoxy‐D‐galactopyranoside Residues into Glycoconjugate Structures

Kerns, R. J., & Wei, P. (2007) · ChemInform · doi:10.1002/chin.200731253 · Cited by 3

Protein glycosylation

Lis, H., & Sharon, N. (1994) · Springer eBooks · doi:10.1007/978-3-642-78757-7_14 · Cited by 3

Histochemistry and Cytochemistry of Endogenous Animal Lectins

Akimoto, Y., Hirano, H., Imai, Y., Hirabayashi, J., & Kasai, K. (1998) · Progress in Histochemistry and Cytochemistry · doi:10.1016/s0079-6336(98)80002-8 · Cited by 3

Identification and Characterization of Glycosylated Phenylthiohydantoin Amino Acids

Pisano, A., Packer, N. H., Redmond, J. W., et al. (1995) · Springer eBooks · doi:10.1007/978-1-4899-1031-8_7 · Cited by 3

Sugar Specific Delivery of Drugs, Oligonucleotides and Genes

Monsigny, M. L. P., Roche, A., Midoux, P., & Mayer, R. (1994) · Springer eBooks · doi:10.1007/978-1-4899-1207-7_2 · Cited by 3

Non-Immunological High-Affinity Interactions Used for Labelling

Griffiths, G. O. (1993) · Springer eBooks · doi:10.1007/978-3-642-77095-1_9 · Cited by 3

Fucosylated Glycoproteins in Chinese Hamster Metaphase Chromosomes

Myllyharju, J., & Nokkala, S. (2004) · Hereditas · doi:10.1111/j.1601-5223.1996.00285.x · Cited by 3

Chemistry of glycopeptides

Kunz, H., Löhr, B., & Habermann, J. (1999) · Springer eBooks · doi:10.1007/978-94-015-9281-9_5 · Cited by 3

Glycopeptides and Glycoproteins: Synthetic Chemistry and Biology

Seitz, O. (2003) · NATO science series. Series II, Mathematics, physics and chemistry · doi:10.1007/978-94-007-0958-4_2 · Cited by 3

Glycosylation of Proteins — A Major Challenge in Mass Spectrometry and Proteomics

Hart, G. W., Cole, R. N., Kreppel, L. K., Arnold, C. S., Comer, F. I., Iyer, S. P. N., Cheng, X., Carroll, J., & Parker, G. J. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-719-2_19 · Cited by 3

Synthesis of Mannoproteins in Saccharomyces Cerevisiae

Lehle, L., Roitsch, T. G., Strahl, S., & Tanner, W. (1991) · NATO ASI series. Series H. Cell biology · doi:10.1007/978-3-642-76074-7_6 · Cited by 3

Metabolic Radiolabeling of Animal Cell Glycoconjugates

Diaz, S. L., & Varki, A. P. (1994) · Current Protocols in Immunology · doi:10.1002/0471142735.im0813s09 · Cited by 2

Purification and characterization of a novel human acidic nuclease/intra-cyclobutyl-pyrimidine-dimer-DNA phosphodiesterase

Famulski, K. S., Liuzzi, M., Bashir, S., et al. (2000) · Biochemical Journal · doi:10.1042/bj3450583 · Cited by 2

The Con-A-peroxidase method for tissue localization of glucosyl and mannosyl groups applied to mouse hepatocytes and chicken erythrocytes

Moraes, A. D. S., & Mello, M. L. S. (2006) · Acta Histochemica · doi:10.1016/j.acthis.2006.09.001 · Cited by 2

LOCALIZATION AND IDENTIFICATION OF GALACTOSE/N‐ACETYLGALACTOSAMINE AND SIALIC ACID‐CONTAINING PROTEINS IN CHINESE HAMSTER METAPHASE CHROMOSOMES

Myllyharju, J., & Nokkala, S. (1998) · Cell Biology International · doi:10.1006/cbir.1997.0211 · Cited by 2

Structure and Biogenesis of Glyoxysomes and Peroxisomes

Sautter, C. (1992) · Plant gene research · doi:10.1007/978-3-7091-9138-5_12 · Cited by 2

Nuclear transport and nuclear pores in yeast

Nehrbass, U., & Hurt, E. C. (1992) · Springer eBooks · doi:10.1007/978-94-011-2504-8_1 · Cited by 2

Mitochondrial biogenesis: Do liver mitochondria contain glycoproteins and glycosyltransferases?

Ades, I. Z. (1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90108-f · Cited by 2

Lectin-binding glycoproteins in nuclear fractions from hamster liver and Kirkman-Robbins hepatoma

Lipińska, A., Wḱlodarczyk, M. M., Gaczyński, M., & Krześlak, A. (1994) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(94)90066-3 · Cited by 2

Expression of blood group A and B antigens in nuclear heterochromatin in mucous cells of human cervical glands.

Nakajima, M., Ito, N., NISHI, K., et al. (1991) · Journal of Histochemistry & Cytochemistry · doi:10.1177/39.4.1706375 · Cited by 2

MAPPING THE ORGANIZATION AND FUNCTIONAL TOPOGRAPHY OF THE CELL NUCLEUS

Berezney, R. (1992) · Elsevier eBooks · doi:10.1016/b978-0-12-168562-1.50042-2 · Cited by 2

Genetic Rescue of Pathogenic O-GlcNAc Dyshomeostasis Associated with Microcephaly and Motor Deficits

Authier, F., Esperon‐Abril, I., Coquelin, K.-S., Skoven, C. S., Eskildsen, S. F., Ondrušková, N., Ferenbach, A. T., Thomsen, J. S., Hansen, B., & van Aalten, D. M. F. (2026) · eNeuro · doi:10.1523/eneuro.0453-25.2026 · Cited by 1

Sugars And Proteins: How They Get It Together

Bill, R. M., Revers, L., & Wilson, I. B. H. (1998) · Springer eBooks · doi:10.1007/978-1-4615-4939-0_3 · Cited by 1

Biosynthesis and Function of Glycoconjugates

Bakar, E., Türker, N. P., & Erim, Z. (2023) · Recent advances in biotechnology · doi:10.2174/9789815179422123080009 · Cited by 1

Applications of Recombinant DNA Technology in Gastrointestinal Medicine and Hepatology: Basic Paradigms of Molecular Cell Biology. Part C: Protein Synthesis and Post-Translational Processing in Eukaryotic Cells

Wild, G., Papalia, P., Ropeleski, M. J., et al. (2000) · Canadian Journal of Gastroenterology · doi:10.1155/2000/198641 · Cited by 1

Structures and Functions of Nuclear and Cytoplasmic Glycoproteins

Haltiwanger, R. S. (2000) · Carbohydrates in Chemistry and Biology · doi:10.1002/9783527618255.ch78 · Cited by 1

Localization of choline acetyltransferase-expressing neurons inDrosophila nervous system

Yasuyama, K., & Salvaterra, P. M. (1999) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19990415)45:2 · Cited by 146

Remodeling of chick embryonic ventricular myoarchitecture under experimentally changed loading conditions

Sedmera, D., Pexieder, T., Rychterová, V., Hu, N., & Clark, E. B. (1999) · The Anatomical Record · doi:10.1002/(sici)1097-0185(19990201)254:2 · Cited by 252

Inhibition of Nuclear Envelope Reconstitution in Xenopus Interphase Egg Extract by Hemin.

Nishiyama, R., Ikami, M., Yamao, F., et al. (1998) · Cell Structure and Function · doi:10.1247/csf.23.291 · Cited by 1

Dynamic O-GlcNAcylation of Nucleocytoplasmic Proteins

Hart, G. W., & Sakabe, K. (2007) · Elsevier eBooks · doi:10.1016/b978-044451967-2/00088-x · Cited by 1

Glycosylation patterns in mucus glycoproteins

Slominay, A., Kasinathan, C., & Slomiany, B. L. (1997) · Advances in macromolecular carbohydrate research · doi:10.1016/s1874-5261(97)80006-6 · Cited by 1

Metabolic Radiolabeling of Animal Cell Glycoconjugates

Diaz, S. L., & Varki, A. P. (1995) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1202s00 · Cited by 1

Nuclear transport and nuclear pores in yeast

Nehrbass, U., & Hurt, E. C. (1992) · Antonie van Leeuwenhoek · doi:10.1007/bf00584458 · Cited by 1

Rôle des antigènes tissulaires de groupes sanguins humains A, B, H et Lewis dans l'évolution des Norovirus GII.4

de Rougemont, A. (2011) · doi:10.70675/6d0cb989z1d6az41c7za009z3e17c5bb5497 · Cited by 1

Use of Complex Carbohydrates as Targets and Ligands for Imaging

Tauber, R., Emig, S., Volz, B., Fieger, C. B., & Bührer, C. (1997) · Springer eBooks · doi:10.1007/978-3-642-60844-5_9

Alternating Phosphorylation with O-GlcNAc Modification: Another Way to Control Protein Function

Victor, V., & Rita, C. (2012) · InTech eBooks · doi:10.5772/38821

Analysis of the functional role of nucleoporin Nup214 in nuclear transport and other cellular processes

Paulillo, S. M. (2007) · edoc (University of Basel) · doi:10.5451/unibas-004250304

Enzym- und Proteinanalytik

Westermann, P. (1997) · Springer eBooks · doi:10.1007/978-3-662-08822-7_4

Chapter 11 The role of glycosylation in cell regulation

Hounsell, E. F. (1995) · Principles of medical biology · doi:10.1016/s1569-2582(06)80013-9

Development and validation of a LC-MS/MS method for the pharmacokinetic study of thiamet-G and its analogues in rat

Ko, S. M. S. (2010) · Summit (Simon Fraser University)

Nuclear labelling in primordial germ cells ofRana dalmatinaembryos byDolichos biflorusagglutinin

Riccio, M., Telò, T., Giorgi, P. P., et al. (1998) · The European Zoological Journal · doi:10.1080/11250008809386754

Evidence for incorporation of n-acetylglucosamine in endogenous nuclear acceptors during the nuclear matrix preparation

Bellemin-Magninot, P., Azzar, G., Létoublon, R., et al. (1993) · International Journal of Biochemistry · doi:10.1016/0020-711x(93)90634-q

Coordinate Synthesis but Discrete Localization of Homologous N ‐Glycosylated Proteins, CLP and CLB , in N aegleria pringsheimi Flagellates

Baek, I. K., Chung, S., Suh, M. R., et al. (2012) · Journal of Eukaryotic Microbiology · doi:10.1111/j.1550-7408.2012.00642.x

Distribution of sugar‐binding sites within interphase nuclei and mitotic chromosomes of a human cell line

Bourgeois, C. A., & Monsigny, M. L. P. (1990) · Biology of the Cell · doi:10.1111/j.1768-322x.1990.tb00007.x

Sugars And Proteins: Why They Get It Together

Bill, R. M., Revers, L., & Wilson, I. B. H. (1998) · Springer eBooks · doi:10.1007/978-1-4615-4939-0_2

Transcriptional regulation of mortalin and the hexosamine biosynthetic pathway by the orphan nuclear receptor ERRalpha

Sylvain-Drolet, G. (2011) · eScholarship@McGill (McGill) · doi:10.82308/43435

Identifizierung und funktionelle Charakterisierung von Glykomimetika für das Tn-Antigen

Schachner, M. (2012)

Synthesis of Glycoconjugates: Their Use to Study the Intracellular Traffic of Endogenous Lectins and to Deliver Oligonucleotides and Genes

Monsigny, M. L. P., Quétard, C., Bourgerie, S., Carriere, V., Duverger, E., Altemayer-Caillard, V., Pichon, C., Mayer, R., Midoux, P., & Roche, A. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46865-4_3

Posttranslational Processing of Proteins

Aerts, J. M. F. G., & Schram, A. W. (1993) · Humana Press eBooks · doi:10.1007/978-1-59259-438-2_6

MHC Class I binding glycopeptides

Arsequell, G., Lellouch, A. C., Haurum, J. S., Elliott, T. J., & Dwek, R. A. (1995) · Springer eBooks · doi:10.1007/978-94-011-1468-4_338

Chapter 1 The covalent structure of proteins

Allen, G. (1997) · Protein · doi:10.1016/s1874-5989(97)80003-8

The effect of Galectin-3 in experimental uraemia

Findlay, A. (2016) · Queen Mary Research Online (Queen Mary University of London)

Identification of proteins with the CDw75 epitope in human colorectal cancer

o‐Crespo, Ï. ⁄. S. M. ⁄., ndez‐Briera, A. F. ⁄., & n, E. G. M. (2017) · Oncology Letters · doi:10.3892/ol.2017.7336

Aberrant Glycosylation in HEMPAS Patients

Kameh, H. (1997) · Library and Archives Canada (Government of Canada)

Transformative Technologies to Advance Our Understanding of the Functions of O-GlcNAc

Fahie, K., Narayanan, B., Zahra, F., Fernandes, S. M., & Zachara, N. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819475-1.00091-2

Enzym- und Proteinanalytik

Westermann, P., & Wittmann‐Liebold, B. (2003) · Springer eBooks · doi:10.1007/978-3-662-07588-3_14

Vital Functions of Glycans in the Biological Systems

Rani, R., Malik, P., Singh, R., Kumar, R., Patel, V. H., & Mukherjee, T. K. (2025) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815322521125010004

Activité antitumorale des isoformes de la lactoferrine, une approche comparative et quantitative

Hoedt, E. (2012) · doi:10.70675/6f75c2c6z7a94z4550z8d0az30d431eb5626

La delta-lactoferrine : un facteur de transcription régulé par SUMOylation

Escobar-Ramírez, A. (2014) · theses.fr (ABES) · doi:10.70675/2e482992z08c5z4e61zbf6fzbdd738e30c6f

Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications

Tong, J., Qin, L., Zhang, Y., et al. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1913410

Disrupted O-GlcNAc homeostasis links microglial dysfunction to cerebellar hypoplasiaPreprint

Almeida, S., Balasubramaniam, S. T., Jusiel, A., Burmeister, T.-S., Martins, L., Toft, G. U., Lebre, C., Õunap, K., Ilves, P., Lin, L., et al. (2026) · medRxiv · doi:10.64898/2026.09.26.26363519

Synthesis of glycosylated amino acids. Solid-phase assembly of T-cell immunogenic glycopeptides and fragments from HIV gp120

Elofsson, M. (1996) · Lund University Publications (Lund University)

Passage of material containing uracil-14C between the nucleus and cytoplasm of Amoeba proteus

Iverson, R. M. (1962) · Experimental Cell Research · doi:10.1016/0014-4827(62)90049-6 · Cited by 9

Experimental Evaluation of the Density of Water in a Cell by Raman Microscopy

Takeuchi, M., Kajimoto, S., & Nakabayashi, T. (2017) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.7b02154 · Cited by 52

Cytoplasmic induction of changes in the ultrastructure of the Acetabularia nucleus and perinuclear cytoplasm

Berger, S., & Schweiger, H. (1975) · Journal of Cell Science · doi:10.1242/jcs.17.3.517 · Cited by 29

Proteins in nucleocytoplasmic interactions

Legname, C., & Goldstein, L. (1972) · Experimental Cell Research · doi:10.1016/0014-4827(72)90526-5 · Cited by 31

Cytoplasmic pools of guanine derivatives in Euglena?

Bryhni, E. (1971) · Experimental Cell Research · doi:10.1016/0014-4827(71)90597-0