[1] Y. Wang et al., “Small molecule inhibitors reveal allosteric regulation of USP14 via steric blockade," Cell Res. 28(12), 1186–1194 (2018).
[2] Q. Zhao et al., “A dual-specific anti-IGF-1/IGF-2 human monoclonal antibody alone and in combination with temsirolimus for therapy of neuroblastoma," Int. J. Cancer 137(9), 2243–2252 (2015).
[3] D. Z. Li et al., “N-terminal alpha-amino group modification of antibodies using a site-selective click chemistry method," MAbs 10(5), 712–719 (2018).
[4] D. Li et al., “Engineered antibody CH2 domains binding to nucleolin: Isolation, characterization and improvement of aggregation," Biochem. Biophys. Res. Commun. 485(2), 446–453 (2017).
[5] Q. Zhao et al., “Human monoclonal antibody fragments binding to insulin-like growth factors I and II with picomolar a±nity," Mol. Cancer Ther. 10(9), 1677–1685 (2011).
[6] Q. Zhao, Z. Zhu, D. S. Dimitrov, “Yeast display of engineered antibody domains," Methods Mol. Biol. 899, 73–84 (2012).
[7] Z. Chen et al., “Generation of bispecific antibodies by Fc heterodimerization and their application," Curr. Pharm. Biotechnol. 17, 1324–1332 (2016).
[8] Z. Chen et al., “A dual-specific IGF-I/II human engineered antibody domain inhibits IGF signaling in breast cancer cells," Int. J. Biol. Sci. 14(7), 799–806 (2018).
[9] Y. Wang et al., “Screening and expressing HIV-1 specific antibody fragments in Saccharomyces cerevisiae," Mol. Immunol. 103, 279–285 (2018).
[10] T. Xu et al., “A native-like bispecific antibody suppresses the inflammatory cytokine response by simultaneously neutralizing tumor necrosis factoralpha and interleukin-17A," Oncotarget 8(47), 81860–81872 (2017).
[11] D. Li et al., “N-terminal residues of an HIV-1 gp41 membrane-proximal external region antigen influence broadly neutralizing 2F5-like antibodies," Virol. Sin. 30(6), 449–456 (2015).
[12] Q. Zhao et al., “Alteration of electrostatic surface potential enhances a±nity and tumor killing properties of anti-ganglioside GD2 monoclonal antibody hu3F8," J. Biol. Chem. 290(21), 13017–13027 (2015).
[13] D. Chu et al., “Photosensitization priming of tumor microenvironments improves delivery of nanotherapeutics via neutrophil infiltration," Adv. Mater. 29 (27), (2017).
[14] D. Chu et al., “Nanoparticle targeting of neutrophils for improved cancer immunotherapy," Adv. Health. Mater. 5(9), 1088–1093 (2016).
[15] Y. Wu et al., “Recombinant-fully-human-antibody decorated highly-stable far-red AIEdots for in vivo HER-2 receptor-targeted imaging," Chem. Commun. (Camb) 54(53), 7314–7317 (2018).
[16] Q. Zhao et al., “A±nity maturation of T-cell receptor-like antibodies for Wilms tumor 1 peptide greatly enhances therapeutic potential," Leukemia 29(11), 2238–2247 (2015).
[17] D. L. Stanculeanu et al., “Development of new immunotherapy treatments in different cancer types," J. Med. Life 9(3), 240–248 (2016).
[18] M. J. Smyth et al., “Activation of NK cell cytotoxicity," Mol. Immunol. 42(4), 501–510 (2005).
[19] T. Tonn et al., “Treatment of patients with advanced cancer with the natural killer cell line NK-92," Cytotherapy 15(12), 1563–1570 (2013).
[20] L. Boissel et al., “Retargeting NK-92 cells by means of CD19- and CD20-specific chimeric antigen receptors compares favorably with antibody-dependent cellular cytotoxicity," Oncoimmunol. 2(10), e26527 (2013).
[21] H. Klingemann, L. Boissel, F. Toneguzzo, “Natural killer cells for immunotherapy - Advantages of the NK-92 cell line over blood NK cells," Front. Immunol. 7, 91 (2016).
[22] Y. Chen et al., “Gene-modified NK-92MI cells expressing a chimeric CD16-BB-zeta or CD64-BBzeta receptor exhibit enhanced cancer-killing ability in combination with therapeutic antibody," Oncotarget 8(23), 37128–37139 (2017).
[23] M. Ahmed et al., “Humanized a±nity-matured monoclonal antibody 8H9 has potent antitumor activity and binds to FG loop of tumor antigen B7-H3," J. Biol. Chem. 290(50), 30018–30029 (2015).
[24] N. J. Topham, E. W. Hewitt, “Natural killer cell cytotoxicity: How do they pull the trigger ," Immunology 128(1), 7–15 (2009).
[25] L. Sercombe et al., “Advances and challenges of liposome assisted drug delivery," Front Pharmacol. 6, 286 (2015).
[26] F. Xu et al., “Loading of indocyanine green within polydopamine-coated laponite nanodisks for targeted cancer photothermal and photodynamic therapy," Nanomater. (Basel) 8(5), 347 (2018).
[27] J. R. Melamed, R. S. Edelstein, E. S. Day, “Elucidating the fundamental mechanisms of cell death triggered by photothermal therapy," ACS Nano 9(1), 6–11 (2015).
[28] N. Onda et al., “Preferential tumor cellular uptake and retention of indocyanine green for in vivo tumor imaging," Int. J. Cancer 139(3), 673–682 (2016).
[29] S. Luo et al., “A review of NIR dyes in cancer targeting and imaging," Biomater. 32(29), 7127–7138 (2011).
[30] H. J. Yoon et al., “Liposomal indocyanine green for enhanced photothermal therapy," ACS Appl. Mater. Interfaces 9(7), 5683–5691 (2017).
[31] A. K. Kirchherr, A. Briel, K. Mader, “Stabilization of indocyanine green by encapsulation within micellar systems," Mol. Pharm. 6(2), 480–491 (2009).