References
- Korherr C, Hofmeister R, Wesche H, et al. A critical role for interleukin-1 receptor accessory protein in interleukin-1 signaling. Eur J Immunol. 1997;27(1):262–267.
- Palmer G, Lipsky BP, Smithgall MD, et al. The IL-1 receptor accessory protein (AcP) is required for IL-33 signaling and soluble AcP enhances the ability of soluble ST2 to inhibit IL-33. Cytokine 2008;42(3):358–364.
- Drube S, Heink S, Walter S, et al. The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in mast cells. Blood. 2010;115(19):3899–3906.
- Shastri A, Will B, Steidl U, et al. Stem and progenitor cell alterations in myelodysplastic syndromes. Blood. 2017;129(12):1586–1594.
- Barreyro L, Will B, Bartholdy B, et al. Overexpression of IL-1 receptor accessory protein in stem and progenitor cells and outcome correlation in AML and MDS. Blood. 2012;120(6):1290–1298.
- Järås M, Johnels P, Hansen N, et al. Isolation and killing of candidate chronic myeloid leukemia stem cells by antibody targeting of IL-1 receptor accessory protein. Proc Natl Acad Sci USA. 2010;107:16280–16285.
- Mitchell K, Barreyro L, Todorova TI, et al. IL1RAP potentiates multiple oncogenic signaling pathways in AML. J Exp Med. 2018;215(6):1709–1727.
- Askmyr M, Ågerstam H, Hansen N, et al. Selective killing of candidate AML stem cells by antibody targeting of IL1RAP. Blood. 2013;121(18):3709–3713.
- Fisher S, Brandt M. 2017. Humanized anti-IL-1R3 antibodies. Patent, WO 2017/191325 A9.
- Warda W, Larosa F, Neto Da Rocha M, et al. CML hematopoietic stem cells expressing IL-1RAP can be targeted by chimeric antigen receptor (CAR)-engineered T cells. Cancer Res. 2019;79(3):663–675.
- Gao C, Mao S, Kaufmann G, et al. A method for the generation of combinatorial antibody libraries using pIX phage display. Proc Natl Acad Sci USA. 2002;99(20):12612–12616.
- Van Deventer JA, Wittrup KD. Yeast surface display for antibody isolation: Library construction, library screening, and affinity maturation. Methods Mol Biol. 2014;1131:151–181.
- Jia Y, Ren P, Duan S, et al. An optimized yeast display strategy for efficient scFv antibody selection using ribosomal skipping system and thermo resistant yeast. Biotechnol Lett. 2019;41(8–9):1067–1076.
- Joung J, Konermann S, Gootenberg JS, et al. Genome-scale CRISPR-Cas9 knockout and transcriptional activation screening. Nat Protoc. 2017;12(4):828–863.
- Yusakul G, Sakamoto S, Pongkitwitoon B, et al. Effect of linker length between variable domains of single chain variable fragment antibody against daidzin on its reactivity. Biosci Biotechnol Biochem. 2016;80(7):1306–1312.
- Paudel MK, Sakamoto S, Van Huy L, et al. The effect of varying the peptide linker length in a single chain variable fragment antibody against wogonin glucuronide. J Biotechnol. 2017;251:47–52.
- Dolezal O, De Gori R, Walter M, et al. Single-chain Fv multimers of the anti-neuraminidase antibody NC10: The residue at position 15 in the V(L) domain of the scFv-0 (V(L)-V(H)) molecule is primarily responsible for formation of a tetramer-trimer equilibrium. Protein Eng. 2003;16(1):47–56.
- Arndt MA, Krauss J, Rybak SM. Antigen binding and stability properties of non-covalently linked anti-CD22 single-chain Fv dimers. Febs Lett. 2004;578(3):257–261.