@article{22959,
  abstract     = {With this status report, we aim to provide a timely snapshot of the protein engineering field as a broad and rapidly advancing discipline that integrates computational, molecular biology, structure-guided, evolutionary, and synthetic approaches to create new and improved proteins with tailored structures and useful functions. The report is organized into eight thematic areas spanning core methodologies and major application domains, including enzymes, therapeutics, detection, synthetic biology, and materials. Contributions from experts across these areas highlight both the historical foundations and recent advances in their respective fields, with particular emphasis on the growing influence of machine learning and artificial intelligence-based methods. Emerging from this broad overview is a central message: protein engineering appears to be entering a golden age, defined by a rapidly accelerating pace of progress, even as significant challenges in design, screening, and real-world application remain. Looking ahead, the continued integration of computational and experimental strategies is poised to further accelerate the impact of protein engineering across an expanding range of economically and societally important sectors, from therapeutics and molecular imaging to diagnostics, plastic recycling, and industrial chemistry.},
  author       = {Ai, Hui-wang and Arnold, Frances H and Barrick, Doug and Bayley, Hagan and Brownless, Alfie-Louise R and Campbell, Robert E and Castells-Graells, Roger and Chaiyen, Pimchai and Chica, Roberto A and Chisholm, Lauren O and Christ, Daniel and Chu, Guo-Chao and Chungyoun, Michael and Eijsink, Vincent G H and Elowitz, Michael B and Fansher, Douglas J and Fasan, Rudi and Foley, Gabriel and Frei, Michelle S and Gagsteiger, Andreas and Gao, Ruiyan and Gillam, Elizabeth M J and Gray, Jeffrey J and Guerra, Luis F and Höcker, Birte and Jin, Zhiyang and Kamerlin, Shina Caroline Lynn and Koga, Nobuyasu and Kontermann, Roland E and Kuhlman, Brian and Langlois, Olivia A and Li, Dongyang and Lins, Roberto D and Liu, Chang C and Liu, Lei and López Barreiro, Diego and Lu, Peilong and Mehta, Sohum and Miyazaki, Ikumi and Müller, Manuel M and Muyldermans, Serge and Nemoto, Naoto and Nivala, Jeff and Nuñez, James K and Ornelas, Izaiah J and Pelletier, Joelle N and Plückthun, Andreas and Porth, Owen T and Prakinee, Kridsadakorn and Qing, Yujia and Reisenbauer, Julia and Schmidt, Sandy and Seifert, Oliver and Shapiro, Mikhail G and Sharma, Rachna and Singh, Nilmani and Smith, Benjamin J and Spangler, Jamie B and Tatsumi-Koga, Rie and Terai, Takuya and Terholsen, Henrik and Tolhurst, Mattias and Tripp, Katherine W and Trossmann, Vanessa Tanja and Tucker, Chandra L and Turak, Onur and Van Deventer, James A and Várnai, Anikó and Viana, Isabelle F T and Weeks, Amy M and Wittrup, K Dane and Wong, Kingsley L-J and Xi, Chenggang and Yeates, Todd O and Yeh, Andy Hsien-Wei and Zhang, Jin and Zhang, Tiger S and Zhao, Huimin and Zheng, Fang and Zhu, Jingyi and Zinn, Sacha},
  issn         = {1741-0134},
  journal      = {Protein Engineering, Design and Selection},
  publisher    = {Oxford University Press},
  title        = {{Protein engineering: Status report}},
  doi          = {10.1093/protein/gzag020},
  volume       = {39},
  year         = {2026},
}

@article{10363,
  abstract     = {Erythropoietin enhances oxygen delivery and reduces hypoxia-induced cell death, but its pro-thrombotic activity is problematic for use of erythropoietin in treating hypoxia. We constructed a fusion protein that stimulates red blood cell production and neuroprotection without triggering platelet production, a marker for thrombosis. The protein consists of an anti-glycophorin A nanobody and an erythropoietin mutant (L108A). The mutation reduces activation of erythropoietin receptor homodimers that induce erythropoiesis and thrombosis, but maintains the tissue-protective signaling. The binding of the nanobody element to glycophorin A rescues homodimeric erythropoietin receptor activation on red blood cell precursors. In a cell proliferation assay, the fusion protein is active at 10−14 M, allowing an estimate of the number of receptor–ligand complexes needed for signaling. This fusion protein stimulates erythroid cell proliferation in vitro and in mice, and shows neuroprotective activity in vitro. Our erythropoietin fusion protein presents a novel molecule for treating hypoxia.},
  author       = {Lee, Jungmin and Vernet, Andyna and Gruber, Nathalie and Kready, Kasia M. and Burrill, Devin R. and Way, Jeffrey C. and Silver, Pamela A.},
  issn         = {1741-0134},
  journal      = {Protein Engineering, Design and Selection},
  publisher    = {Oxford University Press},
  title        = {{Rational engineering of an erythropoietin fusion protein to treat hypoxia}},
  doi          = {10.1093/protein/gzab025},
  volume       = {34},
  year         = {2021},
}