1. Biechele, P.; Busse, C.; Solle, D.; Scheper, T.; Reardon, K. Sensor systems for bioprocess monitoring. Eng. Life Sci. 2015, 15, 469–488. [CrossRef]
2. Fernández-Robledo, J.A.; Vasta, G.R. Production of recombinant proteins from protozoan parasites. Trends Parasitol. 2010, 26, 244–254. [CrossRef] [PubMed]
3. Loughran, S.T.; Bree, R.T.; Walls, D. Purification of polyhistidine-tagged proteins. In Protein Chromatography; Springer: Berlin/Heidelberg, Germany, 2017; pp. 275–303.
4. Raducanu, V.-S.; Isaioglou, I.; Raducanu, D.-V.; Merzaban, J.S.; Hamdan, S.M. Simplified detection of polyhistidine-tagged proteins in gels and membranes using a UV-excitable dye and a multiple chelator head pair. J. Biol. Chem. 2020, 295, 12214–12223. [CrossRef]
5. Kryšt ˚ufek, R.; Šácha, P. An iBody-based lateral flow assay for semi-quantitative determination of His-tagged protein concentration. J. Immunol. Methods 2019, 473, 112640. [CrossRef] [PubMed]
6. Cao, Z.; Wang, S.; Liu, Z.; Xue, C.; Mao, X. A rapid, easy, and sensitive method for detecting His-tag-containing chitinase based on ssDNA aptamers and gold nanoparticles. Food Chem. 2020, 330, 127230. [CrossRef] [PubMed]
7. Kökpinar, Ö.; Walter, J.G.; Shoham, Y.; Stahl, F.; Scheper, T. Aptamer-based downstream processing of his-tagged proteins utilizing magnetic beads. Biotechnol. Bioeng. 2011, 108, 2371–2379. [CrossRef] [PubMed]
8. Kreisig, T.; Prasse, A.A.; Zscharnack, K.; Volke, D.; Zuchner, T. His-tag protein monitoring by a fast mix-and-measure immunoassay. Sci. Rep. 2014, 4, 1–5. [CrossRef] [PubMed]
9. Abe, R.; Ohashi, H.; Iijima, I.; Ihara, M.; Takagi, H.; Hohsaka, T.; Ueda, H. “Quenchbodies”: Quench-based antibody probes that show antigen-dependent fluorescence. J. Am. Chem. Soc. 2011, 133, 17386–17394. [CrossRef] [PubMed]
10. Dong, J.; Ueda, H. Recent Advances in Quenchbody, a Fluorescent Immunosensor. Sensors 2021, 21, 1223. [CrossRef]
11. Inoue, A.; Ohmuro-Matsuyama, Y.; Kitaguchi, T.; Ueda, H. Creation of a Nanobody-Based Fluorescent Immunosensor Mini Q-body for Rapid Signal-On Detection of Small Hapten Methotrexate. ACS Sens. 2020, 5, 3457–3464. [CrossRef]
12. Takahashi, R.; Yasuda, T.; Ohmuro-Matsuyama, Y.; Ueda, H. BRET Q-Body: A Ratiometric Quench-based Bioluminescent Immunosensor Made of Luciferase–Dye–Antibody Fusion with Enhanced Response. Anal. Chem. 2021, 93, 7571–7578. [CrossRef]
13. Kaufmann, M.; Lindner, P.; Honegger, A.; Blank, K.; Tschopp, M.; Capitani, G.; Plückthun, A.; Grütter, M.G. Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen. J. Mol. Biol. 2002, 318, 135–147. [CrossRef]
14. Yamagata, H.; Nakahama, K.; Suzuki, Y.; Kakinuma, A.; Tsukagoshi, N.; Udaka, S. Use of Bacillus brevis for efficient synthesis and secretion of human epidermal growth factor. Proc. Natl. Acad. Sci. USA 1989, 86, 3589–3593. [CrossRef]
15. Van der Linden, R.; Frenken, L.; De Geus, B.; Harmsen, M.; Ruuls, R.; Stok, W.; De Ron, L.; Wilson, S.; Davis, P.; Verrips, C. Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol. 1999, 1431, 37–46. [CrossRef]
16. Hamers-Casterman, C.; Atarhouch, T.; Muyldermans, S.; Robinson, G.; Hammers, C.; Songa, E.B.; Bendahman, N.; Hammers, R. Naturally occurring antibodies devoid of light chains. Nature 1993, 363, 446–448. [CrossRef] [PubMed]
17. Frenken, L.G.; Van Der Linden, R.H.; Hermans, P.W.; Bos, J.W.; Ruuls, R.C.; De Geus, B.; Verrips, C.T. Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J. Biotechnol. 2000, 78, 11–21. [CrossRef]
18. Jeong, H.-J.; Kawamura, T.; Dong, J.; Ueda, H. Q-Bodies from recombinant single-chain Fv fragment with better yield and expanded palette of fluorophores. ACS Sens. 2016, 1, 88–94. [CrossRef]
19. Ohmuro-Matsuyama, Y.; Ueda, H. Homogeneous noncompetitive luminescent immunodetection of small molecules by ternary protein fragment complementation. Anal. Chem. 2018, 90, 3001–3004. [CrossRef] [PubMed]
20. Henkel, M.; Röckendorf, N.; Frey, A. Selective and efficient cysteine conjugation by maleimides in the presence of phosphine reductants. Bioconjug. Chem. 2016, 27, 2260–2265. [CrossRef]
21. Wu, G.; Robertson, D.H.; Brooks, C.L., III; Vieth, M. Detailed analysis of grid-based molecular docking: A case study of CDOCKER—A CHARMm-based MD docking algorithm. J. Comp. Chem. 2003, 24, 1549–1562. [CrossRef]
22. Kabat, E.A.; Wu, T.T.; Perry, H.M.; Gottesman, K.S.; Foeller, C. Sequences of Proteins of Immunological Interest, 5th ed.; U.S. Government Printing Office: Bethesda, MD, USA, 1991.
23. Jia, Q.; Luo, Y.E. The selective roles of chaperone systems on over-expression of human-like collagen in recombinant Escherichia coli. J. Ind. Microbiol. Biotechnol. 2014, 41, 1667–1675. [CrossRef] [PubMed]
24. Nishihara, K.; Kanemori, M.; Kitagawa, M.; Yanagi, H.; Yura, T. Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 1998, 64, 1694–1699. [CrossRef] [PubMed]
25. Rampogu, S.; Rampogu Lemuel, M. Network Based Approach in the Establishment of the Relationship between Type 2 Diabetes Mellitus and Its Complications at the Molecular Level Coupled with Molecular Docking Mechanism. Biomed. Res. Int. 2016, 2016, 6068437. [CrossRef] [PubMed]