Baldwin, A. D., and K. L. Kiick. Tunable degradation of maleimide-thiol adducts in reducing environments. Bioconjug. Chem. 22:1946–1953, 2011.
Barrientos, G., N. Freitag, I. Tirado-González, L. Unverdorben, U. Jeschke, V. L. J. L. Thijssen, and S. M. Blois. Involvement of galectin-1 in reproduction: past, present and future. Hum. Reprod. Update 20:175–193, 2014.
Camby, I., M. Le Mercier, F. Lefranc, and R. Kiss. Galectin-1: a small protein with major functions. Glycobiology 16:137R–157R, 2006.
Cedeno-Laurent, F., S. R. Barthel, M. J. Opperman, D. M. Lee, R. A. Clark, and C. J. Dimitroff. Development of a nascent galectin-1 chimeric molecule for studying the role of leukocyte galectin-1 ligands and immune disease modulation. J. Immunol. 185:4659–4672, 2010.
Chien, C.-T. H., M.-R. Ho, C.-H. Lin, and S.-T. D. Hsu. Lactose binding induces opposing dynamics changes in human galectins revealed by NMR-based hydrogen–deuterium exchange. Molecules 22(8):1357, 2017.
Earl, L. A., S. Bi, and L. G. Baum. Galectin multimerization and lattice formation are regulated by linker region structure. Glycobiology 21:6–12, 2011.
Elbert, D. L., and J. A. Hubbell. Conjugate addition reactions combined with free-radical cross-linking for the design of materials for tissue engineering. Biomacromolecules 2:430–441, 2001.
Farhadi, S. A., M. M. Fettis, R. Liu, and G. A. Hudalla. A synthetic tetramer of galectin-1 and galectin-3 amplifies pro-apoptotic signaling by integrating the activity of both galectins. Front. Chem. 7:898, 2020.
Farhadi, S. A., and G. A. Hudalla. Engineering galectin–glycan interactions for immunotherapy and immunomodulation. Exp. Biol. Med. 241:1074–1083, 2016.
Fettis, M. M., and G. A. Hudalla. Engineering reactive oxygen species-resistant galectin-1 dimers with enhanced lectin activity. Bioconjug. Chem. 29:2489–2496, 2018.
Fontaine, S. D., R. Reid, L. Robinson, G. W. Ashley, and D. V. Santi. Long-term stabilization of maleimide–thiol conjugates. Bioconjug. Chem. 26:145–152, 2015.
Guardia, C. M., J. J. Caramelo, M. Trujillo, S. P. Méndez-Huergo, R. Radi, D. A. Estrin, and G. A. Rabinovich. Structural basis of redox-dependent modulation of galectin-1 dynamics and function. Glycobiology 24:428–441, 2014.
Hong, L., Z. Wang, X. Wei, J. Shi, and C. Li. Antibodies against polyethylene glycol in human blood: a literature review. J. Pharmacol. Toxicol. Methods 102:2020.
Huang, W., X. Wu, X. Gao, Y. Yu, H. Lei, Z. Zhu, Y. Shi, Y. Chen, M. Qin, W. Wang, and Y. Cao. Maleimide–thiol adducts stabilized through stretching. Nat. Chem. 11:310–319, 2019.
Hudalla, G. A., T. S. Eng, and W. L. Murphy. An approach to modulate degradation and mesenchymal stem cell behavior in poly(ethylene glycol) networks. Biomacromolecules 9:842–849, 2008.
Ito, K., K. Stannard, E. Gabutero, A. M. Clark, S.-Y. Neo, S. Onturk, H. Blanchard, and S. J. Ralph. Galectin-1 as a potent target for cancer therapy: role in the tumor microenvironment. Cancer Metastasis Rev. 31:763–778, 2012.
Ko, J. H., and H. D. Maynard. A guide to maximizing the therapeutic potential of protein–polymer conjugates by rational design. Chem. Soc. Rev. 47:8998–9014, 2018.
Koniev, O., and A. Wagner. Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chem. Soc. Rev. 44:5495–5551, 2015.
Lorenzo, M. M., C. G. Decker, M. U. Kahveci, S. J. Paluck, and H. D. Maynard. Homodimeric protein-polymer conjugates via the tetrazine-trans-cyclooctene ligation. Macromolecules 49:30–37, 2016.
Miura, T., M. Takahashi, H. Horie, H. Kurushima, D. Tsuchimoto, K. Sakumi, and Y. Nakabeppu. Galectin-1β, a natural monomeric form of galectin-1 lacking its six amino-terminal residues promotes axonal regeneration but not cell death. Cell Death Differ. 11:1076–1083, 2004.
Nair, D. P., M. Podgórski, S. Chatani, T. Gong, W. Xi, C. R. Fenoli, and C. N. Bowman. The thiol-michael addition click reaction: a powerful and widely used tool in materials chemistry. Chem. Mater. 26:724–744, 2014.
Nesmelova, I. V., E. Ermakova, V. A. Daragan, M. Pang, M. Menéndez, L. Lagartera, D. Solís, L. G. Baum, and K. H. Mayo. Lactose binding to galectin-1 modulates structural dynamics, increases conformational entropy, and occurs with apparent negative cooperativity. J Mol Biol 397:1209–1230, 2010.
Nishi, N., A. Abe, J. Iwaki, H. Yoshida, A. Itoh, H. Shoji, S. Kamitori, J. Hirabayashi, and T. Nakamura. Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. Glycobiology 18:1065–1073, 2008.
Nishi, N., A. Itoh, A. Fujiyama, N. Yoshida, S. Araya, M. Hirashima, H. Shoji, and T. Nakamura. Development of highly stable galectins: truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins. FEBS Lett. 579:2058–2064, 2005.
Odom, O. W., W. Kudlicki, G. Kramer, and B. Hardesty. An effect of polyethylene glycol 8000 on protein mobility in sodium dodecyl sulfate–polyacrylamide gel electrophoresis and a method for eliminating this effect. Anal. Biochem. 245:249–252, 1997.
Pace, K. E., H. P. Hahn, and L. G. Baum. Preparation of recombinant human galectin-1 and use in T cell death assays. Methods Enzymol. 363:499–518, 2003.
Pelegri-O’Day, E. M., E.-W. Lin, and H. D. Maynard. Therapeutic protein–polymer conjugates: advancing beyond PEGylation. J. Am. Chem. Soc. 136:14323–14332, 2014.
Ravasco, J. M. J. M., H. Faustino, A. Trindade, and P. M. P. Gois. Bioconjugation with maleimides: a useful tool for chemical biology. Chem. Eur. J. 25:43–59, 2019.
Schellekens, H., W. E. Hennink, and V. Brinks. The immunogenicity of polyethylene glycol: facts and fiction. Pharm. Res. 30:1729–1734, 2013.
Shen, B.-Q., K. Xu, L. Liu, H. Raab, S. Bhakta, M. Kenrick, K. L. Parsons-Reponte, J. Tien, S.-F. Yu, E. Mai, D. Li, J. Tibbitts, J. Baudys, O. M. Saad, S. J. Scales, P. J. McDonald, P. E. Hass, C. Eigenbrot, T. Nguyen, W. A. Solis, R. N. Fuji, K. M. Flagella, D. Patel, S. D. Spencer, L. A. Khawli, A. Ebens, W. L. Wong, R. Vandlen, S. Kaur, M. X. Sliwkowski, R. H. Scheller, P. Polakis, and J. R. Junutula. Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates. Nat. Biotechnol. 30:184–189, 2012.
Sundblad, V., L. G. Morosi, J. R. Geffner, and G. A. Rabinovich. Galectin-1: a jack-of-all-trades in the resolution of acute and chronic inflammation. J. Immunol. 199:3721–3730, 2017.
Tao, L., C. S. Kaddis, R. R. O. Loo, G. N. Grover, J. A. Loo, and H. D. Maynard. Synthetic approach to homodimeric protein-polymer conjugates. Chem. Commun. 16:2148–2150, 2009.
Thijssen, V. L., and A. W. Griffioen. Galectin-1 and -9 in angiogenesis: a sweet couple. Glycobiology 24:915–920, 2014.
van der Leij, J., A. van den Berg, G. Harms, H. Eschbach, H. Vos, P. Zwiers, R. van Weeghel, H. Groen, S. Poppema, and L. Visser. Strongly enhanced IL-10 production using stable galectin-1 homodimers. Mol. Immunol. 44:506–513, 2007.
White, C. J., and J. W. Bode. PEGylation and dimerization of expressed proteins under near equimolar conditions with potassium 2-pyridyl acyltrifluoroborates. ACS Cent. Sci. 4:197–206, 2018.
Zhang, B., P. Chakma, M. P. Shulman, J. Ke, Z. A. Digby, and D. Konkolewicz. Probing the mechanism of thermally driven thiol-michael dynamic covalent chemistry. Org. Biomol. Chem. 16:2725–2734, 2001.
Zheng, C. Y., G. Ma, and Z. Su. Native PAGE eliminates the problem of PEG–SDS interaction in SDS-PAGE and provides an alternative to HPLC in characterization of protein PEGylation. Electrophoresis 28:2801–2807, 2007.