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Cited by in CrossRef
For: Ogawa M, Furukawa K, Okajima T. Extracellular O-linked β-N-acetylglucosamine: Its biology and relationship to human disease. World J Biol Chem 2014; 5(2): 224-230 [PMID: 24921011 DOI: 10.4331/wjbc.v5.i2.224]
URL: https://www.wjgnet.com/1949-8454/full/v5/i2/224.htm
Number Citing Articles
1
Fiona Grüninger. Invited review: Drug development for tauopathiesNeuropathology and Applied Neurobiology 2015; 41(1) doi: 10.1111/nan.12192
2
Mitsutaka Ogawa, Shogo Sawaguchi, Takami Kawai, Daita Nadano, Tsukasa Matsuda, Hirokazu Yagi, Koichi Kato, Koichi Furukawa, Tetsuya Okajima. Impaired O-Linked N-Acetylglucosaminylation in the Endoplasmic Reticulum by Mutated Epidermal Growth Factor (EGF) Domain-specific O-Linked N-Acetylglucosamine Transferase Found in Adams-Oliver SyndromeJournal of Biological Chemistry 2015; 290(4) doi: 10.1074/jbc.M114.598821
3
Antonio Blanco, Gustavo Blanco. Medical Biochemistry2022;  doi: 10.1016/B978-0-323-91599-1.00030-4
4
Ashwini S. Sanji, Manasa J., Maruti J. Gurav, Surinder K. Batra, Vishwanath B. Chachadi. Cancer snap-shots: Biochemistry and glycopathology of O-glycans: A reviewInternational Journal of Biological Macromolecules 2024; 260 doi: 10.1016/j.ijbiomac.2024.129318
5
Mitsutaka Ogawa, Shogo Sawaguchi, Koichi Furukawa, Tetsuya Okajima. N-acetylglucosamine modification in the lumen of the endoplasmic reticulumBiochimica et Biophysica Acta (BBA) - General Subjects 2015; 1850(6) doi: 10.1016/j.bbagen.2015.03.003
6
Nathan Torbick, Megan Corbiere. A Multiscale Mapping Assessment of Lake Champlain Cyanobacterial Harmful Algal BloomsInternational Journal of Environmental Research and Public Health 2015; 12(9) doi: 10.3390/ijerph120911560
7
Pamela Stanley. What Have We Learned from Glycosyltransferase Knockouts in Mice?Journal of Molecular Biology 2016; 428(16) doi: 10.1016/j.jmb.2016.03.025
8
Silviya R. Stateva, Antonio Villalobo. O-GlcNAcylation of the human epidermal growth factor receptorOrganic & Biomolecular Chemistry 2015; 13(30) doi: 10.1039/C5OB00443H
9
Mitsutaka Ogawa, Tetsuya Okajima. Structure and function of extracellular O-GlcNAcCurrent Opinion in Structural Biology 2019; 56 doi: 10.1016/j.sbi.2018.12.002
10
Ailin Yang, Ganggang Yu, Yanjun Wu, Haoyan Wang. Role of β2-adrenergic receptors in chronic obstructive pulmonary diseaseLife Sciences 2021; 265 doi: 10.1016/j.lfs.2020.118864
11
Hui-Ju Kao, Chien-Hsun Huang, Neil Arvin Bretaña, Cheng-Tsung Lu, Kai-Yao Huang, Shun-Long Weng, Tzong-Yi Lee. A two-layered machine learning method to identify protein O-GlcNAcylation sites with O-GlcNAc transferase substrate motifsBMC Bioinformatics 2015; 16(S18) doi: 10.1186/1471-2105-16-S18-S10
12
Ri Wu, Xiangfeng Chen, Wei‐Jing Wu, Ze Wang, Yik‐Ling Winnie Hung, Hei‐Tung Wong, T.‐W. Dominic Chan. Fine adjustment of gas modifier loadings for separation of epimeric glycopeptides using differential ion mobility spectrometry mass spectrometryRapid Communications in Mass Spectrometry 2020; 34(9) doi: 10.1002/rcm.8751
13
Florian Malard, Lilyanna Massman, Sébastien Campagne, Stephanie Olivier-Van Stichelen. The O-GlcNAc database: introducing new features and tools developed from community feedbackAnalytical and Bioanalytical Chemistry 2025; 417(5) doi: 10.1007/s00216-024-05571-8
14
Joanne Muter, Mohammad T Alam, Pavle Vrljicak, Flavio S V Barros, Peter T Ruane, Lauren J Ewington, John D Aplin, Melissa Westwood, Jan J Brosens. The Glycosyltransferase EOGT Regulates Adropin Expression in Decidualizing Human EndometriumEndocrinology 2018; 159(2) doi: 10.1210/en.2017-03064
15
Moran Frenkel-Pinter, Merav Daniel Shmueli, Chen Raz, Michaela Yanku, Shai Zilberzwige, Ehud Gazit, Daniel Segal. Interplay between protein glycosylation pathways in Alzheimer’s diseaseScience Advances 2017; 3(9) doi: 10.1126/sciadv.1601576
16
Deborah Chang, Joseph Zaia. Methods to improve quantitative glycoprotein coverage from bottom‐up LC‐MS dataMass Spectrometry Reviews 2022; 41(6) doi: 10.1002/mas.21692