1 Varki, A. Biological roles of glycans. Glycobiology 27, 3-49, doi:10.1093/glycob/cww086 (2017).
2 Reily, C., Stewart, T. J., Renfrow, M. B. & Novak, J. Glycosylation in health and disease. Nat Rev Nephrol 15, 346-366, doi:10.1038/s41581-019-0129-4 (2019).
3 Xu, C. & Ng, D. T. Glycosylation-directed quality control of protein folding. Nat Rev Mol Cell Biol 16, 742-752, doi:10.1038/nrm4073 (2015).
4 Gu, J. & Taniguchi, N. Regulation of integrin functions by N-glycans. Glycoconj J 21, 9-15, doi:10.1023/b:Glyc.0000043741.47559.30 (2004).
5 Takahashi, M., Tsuda, T., Ikeda, Y., Honke, K. & Taniguchi, N. Role of N-glycans in growth factor signaling. Glycoconj J 20, 207-212, doi:10.1023/B:GLYC.0000024252.63695.5c (2004).
6 Seales, E. C. et al. Hypersialylation of beta1 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility. Cancer Res 65, 4645-4652, doi:10.1158/0008-5472.Can-04-3117 (2005).
7 Kaszuba, K. et al. N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes. Proc Natl Acad Sci U S A 112, 4334-4339, doi:10.1073/pnas.1503262112 (2015).
8 Fukushima, K. & Yamashita, K. Interleukin-2 carbohydrate recognition modulates CTLL-2 cell proliferation. J Biol Chem 276, 7351-7356, doi:10.1074/jbc.M008781200 (2001).
9 Fukushima, K., Hara-Kuge, S., Ideo, H. & Yamashita, K. Carbohydrate recognition site of interleukin-2 in relation to cell proliferation. J Biol Chem 276, 31202-31208, doi:10.1074/jbc.M102789200 (2001).
10 Hanson, R. L. & Hollingsworth, M. A. Functional Consequences of Differential O-glycosylation of MUC1, MUC4, and MUC16 (Downstream Effects on Signaling). Biomolecules 6, doi:10.3390/biom6030034 (2016).
11 Burchell, J. M., Beatson, R., Graham, R., Taylor-Papadimitriou, J. & Tajadura-Ortega, V. O-linked mucin-type glycosylation in breast cancer. Biochem Soc Trans 46, 779-788, doi:10.1042/BST20170483 (2018).
12 Hussain, M. R., Hoessli, D. C. & Fang, M. N-acetylgalactosaminyltransferases in cancer. Oncotarget 7, 54067-54081, doi:10.18632/oncotarget.10042 (2016).
13 Zhang, Y. et al. Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide -acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen. J Biol Chem 278, 573-584, doi:10.1074/jbc.M203094200 (2003).
14 Guo, J. M. et al. Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family,pp-GalNAc-T12. FEBS Lett 524, 211-218, doi:10.1016/s0014-5793(02)03007-7(2002).
15 Narimatsu, Y. et al. Effect of glycosylation on cis/trans isomerization of prolines in IgA1-hinge peptide. J Am Chem Soc 132, 5548-5549, doi:10.1021/ja9106429 (2010).
16 Bagdonaite, I. & Wandall, H. H. Global aspects of viral glycosylation. Glycobiology 28, 443-467, doi:10.1093/glycob/cwy021 (2018).
17 Dube, D. H. & Bertozzi, C. R. Glycans in cancer and inflammation--potential for therapeutics and diagnostics. Nat Rev Drug Discov 4, 477-488, doi:10.1038/nrd1751 (2005).
18 Peixoto, A., Relvas-Santos, M., Azevedo, R., Santos, L. L. & Ferreira, J. A. Protein Glycosylation and Tumor Microenvironment Alterations Driving Cancer Hallmarks. Front Oncol 9, 380, doi:10.3389/fonc.2019.00380 (2019).
19 Raman, R., Tharakaraman, K., Sasisekharan, V. & Sasisekharan, R. Glycan-protein interactions in viral pathogenesis. Curr Opin Struct Biol 40, 153-162, doi:10.1016/j.sbi.2016.10.003 (2016).
20 Fujioka, Y. et al. A Sialylated Voltage-Dependent Ca(2+) Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells. Cell Host Microbe 23, 809-818 e805, doi:10.1016/j.chom.2018.04.015 (2018).
21 Shirato, H. Norovirus and histo-blood group antigens. Japanese journal of infectious diseases 64, 95-103 (2011).
22 Shirato, H. Norovirus recognition sites on histo-blood group antigens. Front Microbiol 3, 177, doi:10.3389/fmicb.2012.00177 (2012).
23 Tuccillo, F. M. et al. Aberrant glycosylation as biomarker for cancer: focus on CD43.Biomed Res Int 2014, 742831, doi:10.1155/2014/742831 (2014).
24 Nguyen, A. T. et al. Organelle Specific O-Glycosylation Drives MMP14 Activation, Tumor Growth, and Metastasis. Cancer Cell 32, 639-653 e636, doi:10.1016/j.ccell.2017.10.001 (2017).
25 Vajaria, B. N. & Patel, P. S. Glycosylation: a hallmark of cancer? Glycoconj J 34, 147-156, doi:10.1007/s10719-016-9755-2 (2017).
26 Matsuda, A. et al. Development of an all-in-one technology for glycan profiling targeting formalin-embedded tissue sections. Biochem Biophys Res Commun 370, 259-263, doi:10.1016/j.bbrc.2008.03.090 (2008).
27 Matsuda, A. et al. Assessment of tumor characteristics based on glycoform analysis of membrane-tethered MUC1. Lab Invest 97, 1103-1113, doi:10.1038/labinvest.2017.53 (2017).
28 Krishna, K. & Bekaii-Saab, T. in Biomarkers in Cancer (eds Victor R. Preedy & Vinood B. Patel) 179-201 (Springer Netherlands, 2015).
29 Miyoshi, E., Moriwaki, K. & Nakagawa, T. Biological function of fucosylation in cancer biology. J Biochem 143, 725-729, doi:10.1093/jb/mvn011 (2008).
30 Kuno, A. et al. A serum "sweet-doughnut" protein facilitates fibrosis evaluation and therapy assessment in patients with viral hepatitis. Sci Rep 3, 1065, doi:10.1038/srep01065 (2013).
31 Dias Rde, O., Machado Ldos, S., Migliolo, L. & Franco, O. L. Insights into animal and plant lectins with antimicrobial activities. Molecules 20, 519-541, doi:10.3390/molecules20010519 (2015).
32 Mu, J., Hirayama, M., Sato, Y., Morimoto, K. & Hori, K. A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin. Mar Drugs 15, doi:10.3390/md15080255 (2017).
33 Van Holle, S. & Van Damme, E. J. M. Messages From the Past: New Insights in Plant Lectin Evolution. Front Plant Sci 10, 36, doi:10.3389/fpls.2019.00036 (2019).
34 Hirabayashi, J., Tateno, H., Shikanai, T., Aoki-Kinoshita, K. F. & Narimatsu, H. The Lectin Frontier Database (LfDB), and data generation based on frontal affinity chromatography. Molecules 20, 951-973, doi:10.3390/molecules20010951 (2015).
35 Kuno, A. et al. Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling. Nature methods 2, 851-856, doi:10.1038/nmeth803 (2005).
36 Hirabayashi, J., Yamada, M., Kuno, A. & Tateno, H. Lectin microarrays: concept, principle and applications. Chem Soc Rev 42, 4443-4458, doi:10.1039/c3cs35419a (2013).
37 Tateno, H. et al. Glycome diagnosis of human induced pluripotent stem cells using lectin microarray. J Biol Chem 286, 20345-20353, doi:10.1074/jbc.M111.231274 (2011).
38 Matsuda, A. et al. Comparative Glycomic Analysis of Exosome Subpopulations Derived from Pancreatic Cancer Cell Lines. J Proteome Res, doi:10.1021/acs.jproteome.0c00200 (2020).
39 Matsuda, A. et al. Lectin Microarray-Based Sero-Biomarker Verification Targeting Aberrant O-Linked Glycosylation on Mucin 1. Anal Chem 87, 7274-7281, doi:10.1021/acs.analchem.5b01329 (2015).
40 Zou, X. et al. A standardized method for lectin microarray-based tissue glycome mapping. Sci Rep 7, 43560, doi:10.1038/srep43560 (2017).
41 Nagai-Okatani, C., Nagai, M., Sato, T. & Kuno, A. An Improved Method for Cell Type-Selective Glycomic Analysis of Tissue Sections Assisted by Fluorescence Laser Microdissection. Int J Mol Sci 20, doi:10.3390/ijms20030700 (2019).
42 Kuno, A. et al. Focused differential glycan analysis with the platform antibody-assisted lectin profiling for glycan-related biomarker verification. Molecular & cellular proteomics : MCP 8, 99-108, doi:10.1074/mcp.M800308-MCP200 (2009).
43 Kaji, H. et al. Glycoproteomic discovery of serological biomarker candidates for HCV/HBV infection-associated liver fibrosis and hepatocellular carcinoma. J Proteome Res 12, 2630-2640, doi:10.1021/pr301217b (2013).
44 Sogabe, M. et al. Novel glycobiomarker for ovarian cancer that detects clear cell carcinoma. J Proteome Res 13, 1624-1635, doi:10.1021/pr401109n (2014).
45 Hirao, Y. et al. Glycoproteomics approach for identifying Glycobiomarker candidate molecules for tissue type classification of non-small cell lung carcinoma. J Proteome Res 13, 4705-4716, doi:10.1021/pr5006668 (2014).
46 Trepo, C., Chan, H. L. & Lok, A. Hepatitis B virus infection. Lancet (London, England) 384, 2053-2063, doi:10.1016/s0140-6736(14)60220-8 (2014).
47 Yu, M. W. et al. Prospective study of hepatocellular carcinoma and liver cirrhosis in asymptomatic chronic hepatitis B virus carriers. American journal of epidemiology 145, 1039-1047, doi:10.1093/oxfordjournals.aje.a009060 (1997).
48 Nguyen, M. H., Wong, G., Gane, E., Kao, J. H. & Dusheiko, G. Hepatitis B Virus: Advances in Prevention, Diagnosis, and Therapy. Clinical microbiology reviews 33, doi:10.1128/cmr.00046-19 (2020).
49 Seto, W. K. et al. Reduction of hepatitis B surface antigen levels and hepatitis B surface antigen seroclearance in chronic hepatitis B patients receiving 10 years of nucleoside analogue therapy. Hepatology 58, 923-931, doi:10.1002/hep.26376 (2013).
50 Furusyo, N. et al. Long-term lamivudine treatment for chronic hepatitis B in Japanese patients: a project of Kyushu University Liver Disease Study. World J Gastroenterol 12, 561-567, doi:10.3748/wjg.v12.i4.561 (2006).
51 Dervite, I., Hober, D. & Morel, P. Acute hepatitis B in a patient with antibodies to hepatitis B surface antigen who was receiving rituximab. N Engl J Med 344, 68-69, doi:10.1056/nejm200101043440120 (2001).
52 Yeo, W. et al. Hepatitis B virus reactivation in lymphoma patients with prior resolved hepatitis B undergoing anticancer therapy with or without rituximab. J Clin Oncol 27, 605-611, doi:10.1200/JCO.2008.18.0182 (2009).
53 Hwang, J. P. & Lok, A. S. Management of patients with hepatitis B who require immunosuppressive therapy. Nature reviews. Gastroenterology & hepatology 11, 209-219, doi:10.1038/nrgastro.2013.216 (2014).
54 Dryden, K. A. et al. Native hepatitis B virions and capsids visualized by electron cryomicroscopy. Mol Cell 22, 843-850, doi:10.1016/j.molcel.2006.04.025 (2006).
55 Bruss, V. Hepatitis B virus morphogenesis. World J Gastroenterol 13, 65-73 (2007).
56 Heermann, K. H. et al. Large surface proteins of hepatitis B virus containing the pre-s sequence. J Virol 52, 396-402 (1984).
57 Gilbert, R. J. et al. Hepatitis B small surface antigen particles are octahedral. Proc Natl Acad Sci U S A 102, 14783-14788, doi:10.1073/pnas.0505062102 (2005).
58 Schmitt, S. et al. Analysis of the pre-S2 N- and O-linked glycans of the M surface protein from human hepatitis B virus. J Biol Chem 274, 11945-11957, doi:10.1074/jbc.274.17.11945 (1999).
59 Schmitt, S. et al. Structure of pre-S2 N- and O-linked glycans in surface proteins from different genotypes of hepatitis B virus. J Gen Virol 85, 2045-2053, doi:10.1099/vir.0.79932-0 (2004).
60 Yu, D. M. et al. N-glycosylation mutations within hepatitis B virus surface major hydrophilic region contribute mostly to immune escape. J Hepatol 60, 515-522, doi:10.1016/j.jhep.2013.11.004 (2014).
61 Salpini, R. et al. Hepatitis B surface antigen genetic elements critical for immune escape correlate with hepatitis B virus reactivation upon immunosuppression. Hepatology 61, 823-833, doi:10.1002/hep.27604 (2015).
62 Ito, K. et al. Impairment of hepatitis B virus virion secretion by single-amino-acid substitutions in the small envelope protein and rescue by a novel glycosylation site. J Virol 84, 12850-12861, doi:10.1128/JVI.01499-10 (2010).
63 Block, T. M. et al. Secretion of human hepatitis B virus is inhibited by the imino sugar N-butyldeoxynojirimycin. Proc Natl Acad Sci U S A 91, 2235-2239 (1994).
64 Block, T. M. et al. Treatment of chronic hepadnavirus infection in a woodchuck animal model with an inhibitor of protein folding and trafficking. Nat Med 4, 610-614 (1998).
65 Werr, M. & Prange, R. Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles. J Virol 72,778-782 (1998).
66 Takahashi, T., Nakagawa, S., Hashimoto, T., Takahashi, K. & Imai, M. Large-scale isolation of Dane particles from plasma containing hepatitis B antigen and deomnstration of circular double-stranded DNA molecule extruding directly from their cores. Journal of immunology (Baltimore, Md. : 1950) 117, 1392-1397 (1976).
67 Tajiri, K. et al. Analysis of the epitope and neutralizing capacity of human monoclonal antibodies induced by hepatitis B vaccine. Antiviral Res 87, 40-49, doi:10.1016/j.antiviral.2010.04.006 (2010).
68 Hamada-Tsutsumi, S. et al. Validation of cross-genotype neutralization by hepatitis B virus-specific monoclonal antibodies by in vitro and in vivo infection. PLoS One 10, e0118062, doi:10.1371/journal.pone.0118062 (2015).
69 Sunbul, M. Hepatitis B virus genotypes: global distribution and clinical importance.World J Gastroenterol 20, 5427-5434, doi:10.3748/wjg.v20.i18.5427 (2014).
70 Inaba, S. et al. Individual nucleic amplification technology does not prevent all hepatitis B virus transmission by blood transfusion. Transfusion 46, 2028-2029, doi:10.1111/j.1537-2995.2006.01011.x (2006).
71 Candotti, D. & Laperche, S. Hepatitis B Virus Blood Screening: Need for Reappraisal of Blood Safety Measures? Front Med (Lausanne) 5, 29, doi:10.3389/fmed.2018.00029 (2018).
72 Vaughn, D. W. et al. Evaluation of a rapid immunochromatographic test for diagnosis of dengue virus infection. Journal of clinical microbiology 36, 234-238 (1998).
73 Akkapinyo, C., Khownarumit, P., Waraho-Zhmayev, D. & Poo-Arporn, R. P. Development of a multiplex immunochromatographic strip test and ultrasensitive electrochemical immunosensor for hepatitis B virus screening. Anal Chim Acta 1095, 162-171, doi:10.1016/j.aca.2019.10.016 (2020).
74 Loeffelholz, M. J. & Tang, Y. W. Laboratory diagnosis of emerging human coronavirus infections - the state of the art. Emerg Microbes Infect 9, 747-756, doi:10.1080/22221751.2020.1745095 (2020).
75 Pan, Y. et al. Serological immunochromatographic approach in diagnosis with SARS-CoV-2 infected COVID-19 patients. J Infect 81, e28-e32, doi:10.1016/j.jinf.2020.03.051 (2020).
76 Houg, D. S. & Bijlsma, M. F. The hepatic pre-metastatic niche in pancreatic ductal adenocarcinoma. Mol Cancer 17, 95, doi:10.1186/s12943-018-0842-9 (2018).
77 Orth, M. et al. Pancreatic ductal adenocarcinoma: biological hallmarks, current status, and future perspectives of combined modality treatment approaches. Radiat Oncol 14, 141, doi:10.1186/s13014-019-1345-6 (2019).
78 Adamska, A., Domenichini, A. & Falasca, M. Pancreatic Ductal Adenocarcinoma: Current and Evolving Therapies. Int J Mol Sci 18, doi:10.3390/ijms18071338 (2017).
79 Rahib, L. et al. Projecting cancer incidence and deaths to 2030: the unexpected burden of thyroid, liver, and pancreas cancers in the United States. Cancer Res 74, 2913-2921, doi:10.1158/0008-5472.CAN-14-0155 (2014).
80 McGuigan, A. et al. Pancreatic cancer: A review of clinical diagnosis, epidemiology, treatment and outcomes. World J Gastroenterol 24, 4846-4861, doi:10.3748/wjg.v24.i43.4846 (2018).
81 Masugi, Y. et al. Upregulation of integrin beta4 promotes epithelial-mesenchymal transition and is a novel prognostic marker in pancreatic ductal adenocarcinoma. Lab Invest 95, 308-319, doi:10.1038/labinvest.2014.166 (2015).
82 Zhu, Z. et al. Nerve growth factor expression correlates with perineural invasion and pain in human pancreatic cancer. J Clin Oncol 17, 2419-2428, doi:10.1200/jco.1999.17.8.2419 (1999).
83 Koide, N. et al. Establishment of perineural invasion models and analysis of gene expression revealed an invariant chain (CD74) as a possible molecule involved in perineural invasion in pancreatic cancer. Clin Cancer Res 12, 2419-2426, doi:10.1158/1078-0432.CCR-05-1852 (2006).
84 Yamazaki, K. et al. Upregulated SMAD3 promotes epithelial-mesenchymal transition and predicts poor prognosis in pancreatic ductal adenocarcinoma. Lab Invest 94, 683-691, doi:10.1038/labinvest.2014.53 (2014).
85 Shimomura, O. et al. A Novel Therapeutic Strategy for Pancreatic Cancer: Targeting Cell Surface Glycan Using rBC2LC-N Lectin-Drug Conjugate (LDC). Mol Cancer Ther 17, 183-195, doi:10.1158/1535-7163.MCT-17-0232 (2018).
86 Tada, K. et al. Fucosyltransferase 8 plays a crucial role in the invasion and metastasis of pancreatic ductal adenocarcinoma. Surg Today 50, 767-777, doi:10.1007/s00595-019-01953-z (2020).
87 Chang, Y. et al. Comprehensive characterization of cancer-testis genes in testicular germ cell tumor. Cancer Med 8, 3511-3519, doi:10.1002/cam4.2223 (2019).
88 Ravn, V. & Dabelsteen, E. Tissue distribution of histo-blood group antigens. APMIS : acta pathologica, microbiologica, et immunologica Scandinavica 108, 1-28, doi:10.1034/j.1600-0463.2000.d01-1.x (2000).
89 Dotz, V. & Wuhrer, M. Histo-blood group glycans in the context of personalized medicine. Biochim Biophys Acta 1860, 1596-1607, doi:10.1016/j.bbagen.2015.12.026 (2016).
90 de Mattos, L. C. Structural diversity and biological importance of ABO, H, Lewis and secretor histo-blood group carbohydrates. Rev Bras Hematol Hemoter 38, 331-340, doi:10.1016/j.bjhh.2016.07.005 (2016).
91 Ishii, E. et al. The advent of medical artificial intelligence: lessons from the Japanese approach. J Intensive Care 8, 35, doi:10.1186/s40560-020-00452-5 (2020).
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