Chapter 1
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4. Kesimer, M., Ehre, C., Burns, K. et al. Molecular organization of the mucins and glycocalyx underlying mucus transport over mucosal surfaces of the airways. Mucosal Immunol 2013, 6, 379–392
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14. Ohyabu, N. et al. An essential epitope of anti-MUC1 monoclonal antibody KL-6 revealed by focused glycopeptide library. J Am Chem Soc. 2016, 131, 17102–17109
15. Takahiko Matsushita, Naoki Ohyabu, Naoki Fujitani, Kentaro Naruchi, Hiroki Shimizu, Hiroshi Hinou, and Shin-Ichiro Nishimura. Site-Specific Conformational Alteration Induced by Sialylation of MUC1 Tandem Repeating Glycopeptides at an Epitope Region for the Anti-KL-6 Monoclonal Antibody. Biochemistry 2013, 52, 2, 402-414.
16. Takahiko Matsushita, Wataru Takada, Kota Igarashi, Kentaro Naruchi, Risho Miyoshi, Fayna Garcia-Martin, Maho Amano, Hiroshi Hinou, Shin-Ichiro Nishimura. A straightforward protocol for the preparation of high performance microarray displaying synthetic MUC1 glycopeptides. Biochimica et Biophysica Acta (BBA) - General Subjects 2014, 1840, 3, 1105-1116.
17. Shobith Rangappa, Gerard Artigas, Risho Miyoshi, Yasuhiro Yokoi, Shun Hayakawa, Fayna Garcia-Martin, Hiroshi Hinou, Shin-Ichiro Nishimura. Effects of the multiple O-glycosylation states on antibody recognition of the immunodominant motif in MUC1 extra-cellular tandem repeats. MedChemComm 2016, 7, 6, 1102-1122.
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Chapter 2
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2. Kudelka, M. R. et al., Simple sugars to complex disease: Mucin-type O- glycans in cancer. Adv. Cancer Res. 2015, 126, 53-135.
3. Hollingsworth M. A.; Swanson, B. J. Mucins in cancer: Protection and control of the cell surface. Nat. Rev. Cancer 2004, 4, 45-60.
4. Hattrup, C. L.; Gendler, S. J. Structure and function of the cell surface mucins. Annu. Rev. Physiol. 2007, 70, 431-457.
5. Kufe, D. W. Mucins in cancer: Function, prognosis and therapy. Nat. Rev. Cancer 2009, 9, 874-885.
6. Price, M. R. et al., ISOBM TD-4 International workshop on monoclonal antibodies against MUC1. Tumor Biol. 1998, 19, 1-152.
7. Karsten, U. et al., Binding patterns of DTR-specific antibodies reveal a glycosylationconditioned tumor-specific epitope of the epithelial mucin (MUC1). Glycobiology 2004, 14, 681-692.
8. Danielezyk, A. et al., PankoMab: A potent new generation anti-tumour MUC1 antibody. Cancer Immunol. Immunother. 2006, 55, 1337-1347.
9. Springer, G. F. Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy. J. Mol. Med. 1997, 75, 594-602.
10. Matsushita, T. et al., A straightforward protocol for the prepara-tion of highperformance microarray displaying synthetic MUC1 glycopeptides. Biochim. Biophys.Acta 2014, 1840, 1105-1116.
11. Rangappa, S. et al., Effects of the multiple O-glycosylation states on antibody recognition of the immunodominant motif in MUC1 extra- cellular tandem repeats. Med. Chem. Commun. 2016, 7, 1102-1122.
12. Martínez-Sáez, N. et al., Deciphering the non-equivalence of serine and threonine Oglycosylation points: Implications for molecular recognition of the Tn antigen by an antiMUC1 antibody. Angew. Chem. Int. Ed. 2015, 54, 9830-9834.
13. Movahedin, M. et al., Glycosylation of MUC1 influences the binding of a therapeutic antibody by altering the conformational equilibrium of the antigen. Glycobiology 2017, 27, 677-687.
14. Ishikawa, N. et al., Utility of KL-6/MUC1 in the clinical management of interstitial lung diseases. Respir. Invest. 2012, 50, 3-13.
15. Ohyabu, N. et al., An essential epitope of anti-MUC1 monoclonal antibody KL-6 revealed by focused glycopeptide library. J. Am. Chem. Soc. 2009, 131, 17102-17109.
16. Matsushita, T. et al., Site-specific conformational alteration induced by sialylation of MUC1 tandem repeating glycopeptides at an epitope region for the anti-KL-6 monoclonal antibody. Biochemistry 2013, 52, 402-414.
17. Tanaka, S. et al., Krebs von den Lungen-6 (KL-6) is a prognostic biomarker in patients with surgically resected non-small cell lung cancer, Int. J. Cancer 2012, 130, 377-387.
18. Matsushita, T., et al., Rapid microwave-assisted solid-phase glycopeptide synthesis. Org. Lett. 2005, 7, 877–880.
19. Fumoto, M. et al., Combinatorial synthesis of MUC1 glycopeptides: Polymer blotting facilitates chemical and enzymatic synthesis of highly complicated mucin glycopeptides. J. Am. Chem. Soc. 2005, 127, 11804- 11818.
20. Matsushita, T. et al., Construction of highly glycosylated mucin-type glycopeptides based on microwave-assisted solid-phase syntheses and enzymatic modifications. J. Org.Chem. 2006, 71, 3051-3063.
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22. Möller, H. et al., NMR-based determination of the binding epitope and conformational analysis of MUC1 glycopeptides and peptides bound to the breast cancerselective monoclonal antibody SM3. Eur. J. Biochem. 2002, 269, 1444-1455.
23. Schuman, J. et al., Probing the conformational and dynamical effects of Oglycosylation within the immunodominant region of a MUC1 peptide tumor antigen. J.Peptide Res. 2003, 61, 91-108.
24. Kinarsky, L. et al., Conformational studies on the MUC1 tandem repeat glycopeptides: Implication for the enzymatic O-glycosylation of the mucin protein core. Glycobiology 2003, 13, 929-939.
25. Naito, S. et al., Generation of novel anti-MUC1 monoclonal antibodies with designed carbohydrate specificities using MUC1 glycopeptide library. ACS Omega 2017, 2, 7493-7505.
26. Cheever, M. A. et al., The prioritization of cancer antigens: A National Cancer Institute pilot project for the acceleration of translational research. Clin. Cancer Res. 2009, 15, 5323-5337.
27. Farouk, S. et al., The value of the tumor marker CA 15-3 in diagnosing and monitoring breast cancer. Cancer 1991, 68, 574-582.
28. Curry, J. M. et al., The use of novel MUC1 antibody to identify cancer stem cells and circulating MUC1 in mice and patients with pancreatic cancer. J. Surg. Oncol. 2013, 107, 713-722.
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33. Beatson, R. et al., The breast cancer-associated glycoforms of MUC1, MUC1-Tn and sialyl-Tn, are expressed in COSMC wild-type cells and bind the C-type lectin MGL. PLOS ONE 2015, 10, e0125994.
34. Beatson, R. et al., The mucin MUC1 modulates the tumor immunological microenvironment through engagement of the lectin siglec-9. Nat. Immunol. 2016, 17, 1273-1281.
35. Brooks, C. L. et al., Antibody recognition of a unique tumor-specific glycopeptide antigen. Proc. Natl. Acad. Sci. 2010, 107, 10056-10061.
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Chapter 3
1. Nath, N.; Mukherjee, P. MUC1: A multifaceted oncoprotein with a key role in cancerprogression. Trends in Mol. Med. 2014, 20, 332–342.
2. Kudelka, M. R. et al., Simple sugars to complex disease: Mucin-type O- glycans in cancer. Adv. Cancer Res. 2015, 126, 53-135.
3. Bose, M.; Mukherjee, P. Potential of Anti-MUC1 Antibodies as a Targeted Therapy for Gastrointestinal Cancers. Vaccines 2020, 8, 659.
4. J. Ledermann, J. A. Zurlo et al, LBA41 - A double-blind, placebo- controlled, randomized, phase 2 study to evaluate the efficacy and safety of switch maintenance therapy with the anti-TA-MUC1 antibody PankoMab-GEX after chemotherapy in patients with recurrent epithelial ovarian carcinoma, Annals of Oncology, 2017, 28, 626
5. Puregmaa Khongorzul, Cai Jia Ling, Farhan Ullah Khan, Awais Ullah Ihsan and Juan Zhang, Antibody–Drug Conjugates: A Comprehensive Review, Mol Cancer Res, 2020, 18, 1
6. Rafiq, S., et al., Engineering strategies to overcome the current roadblocks in CAR T cell therapy. Nat Rev Clin Oncol 2020 17, 147–167
7. Céline Nicolazzi et al., An Antibody–Drug Conjugate Targeting MUC1- Associated Carbohydrate CA6 Shows Promising Antitumor Activities, Mol Cancer Ther, 2020, 19, 8 1660-1669
8. Avery D. Posey, et al., Engineered CAR T Cells Targeting the Cancer- Associated Tn-Glycoform of the Membrane Mucin MUC1 Control Adenocarcinoma, Immunity, 2016, 6, 44
9. Beatson, R., Tajadura-Ortega, V., Achkova, D. et al. The mucin MUC1 modulates the tumor immunological microenvironment through engagement of the lectin Siglec-9. Nat Immunol., 2016, 17, 1273–1281.
10. Mehla K, et al., Combination of mAb-AR20.5, anti-PD-L1 and PolyICLC inhibits tumor progression and prolongs survival of MUC1.Tg mice challenged with pancreatic tumors. Cancer Immunol Immunother. 2018, 67, 3, 445-457.
11. Martínez-Sáez, N. et al., Deciphering the non-equivalence of serine and threonine Oglycosylation points: Implications for molecular recognition of the Tn antigen by an antiMUC1 antibody. Angew. Chem. Int. Ed. 2015, 54, 9830-9834.
12. Movahedin, M. et al., Glycosylation of MUC1 influences the binding of a therapeutic antibody by altering the conformational equilibrium of the antigen. Glycobiology 2017, 27, 677-687.
13. Macías-León J, et al., Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody. Chem Commun 2020 in press
14. C.E. Wagner, K.M. Wheeler, K. Ribbeck, Mucins and Their Role in Shaping the Functions of Mucus Barriers Annual Review of Cell and Developmental Biology 2018, 34, 1, 189-215
15. Reily, C., Stewart, T.J., Renfrow, M.B. et al. Glycosylation in health and disease. Nat Rev Nephrol 2019, 15, 346–366
16. Lorenzo Casalino, et al., Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein ACS Cent. Sci. 2020, 6, 10, 1722–1734
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