Thermodynamically coupled biosensors for detecting neutralizing antibodies against SARS-CoV-2 variants.

Autor: Zhang JZ; Department of Biochemistry, University of Washington, Seattle, WA, USA. jason.zhang0428@gmail.com.; Institute for Protein Design, University of Washington, Seattle, WA, USA. jason.zhang0428@gmail.com., Yeh HW; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Walls AC; Department of Biochemistry, University of Washington, Seattle, WA, USA., Wicky BIM; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Sprouse KR; Department of Biochemistry, University of Washington, Seattle, WA, USA., VanBlargan LA; Department of Medicine, Washington University School of Medicine, St. Louis, MO, USA., Treger R; Department of Laboratory Medicine & Pathology, University of Washington, Seattle, WA, USA., Quijano-Rubio A; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Department of Bioengineering, University of Washington, Seattle, WA, USA., Pham MN; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Kraft JC; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Haydon IC; Institute for Protein Design, University of Washington, Seattle, WA, USA., Yang W; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., DeWitt M; Institute for Protein Design, University of Washington, Seattle, WA, USA., Bowen JE; Department of Biochemistry, University of Washington, Seattle, WA, USA., Chow CM; Institute for Protein Design, University of Washington, Seattle, WA, USA., Carter L; Institute for Protein Design, University of Washington, Seattle, WA, USA., Ravichandran R; Institute for Protein Design, University of Washington, Seattle, WA, USA., Wener MH; Department of Laboratory Medicine & Pathology, University of Washington, Seattle, WA, USA., Stewart L; Institute for Protein Design, University of Washington, Seattle, WA, USA., Veesler D; Department of Biochemistry, University of Washington, Seattle, WA, USA.; Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA., Diamond MS; Department of Medicine, Washington University School of Medicine, St. Louis, MO, USA.; Department of Pathology & Immunology, Washington University School of Medicine, St. Louis, MO, USA.; Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA.; Andrew M. and Jane M. Bursky Center for Human Immunology and Immunotherapy Programs, Washington University School of Medicine, Saint Louis, MO, USA., Greninger AL; Department of Laboratory Medicine & Pathology, University of Washington, Seattle, WA, USA.; Vaccine and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA., Koelle DM; Department of Laboratory Medicine & Pathology, University of Washington, Seattle, WA, USA.; Vaccine and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.; Department of Medicine, Division of Allergy and Infectious Diseases, University of Washington, Seattle, WA, USA.; Translational Research Program, Benaroya Research Institute at Virginia Mason, Seattle, WA, USA.; Department of Global Health, University of Washington, Seattle, WA, USA., Baker D; Department of Biochemistry, University of Washington, Seattle, WA, USA. dabaker@uw.edu.; Institute for Protein Design, University of Washington, Seattle, WA, USA. dabaker@uw.edu.; Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA. dabaker@uw.edu.

Publikováno v: Nature biotechnology [Nat Biotechnol] 2022 Sep; Vol. 40 (9), pp. 1336-1340. Date of Electronic Publication: 2022 Apr 28.

Tight and specific lanthanide binding in a de novo TIM barrel with a large internal cavity designed by symmetric domain fusion.

Autor: Caldwell SJ; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195., Haydon IC; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195., Piperidou N; Laboratory of Organic Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich, Switzerland., Huang PS; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195.; Department of Bioengineering, Stanford University, Shriram Center for Bioengineering and Chemical Engineering, Stanford, CA 94305., Bick MJ; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195., Sjöström HS; Laboratory of Organic Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich, Switzerland., Hilvert D; Laboratory of Organic Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich, Switzerland., Baker D; Department of Biochemistry, University of Washington, Seattle, WA 98195; dabaker@uw.edu cathleen.zeymer@tum.de.; Institute for Protein Design, University of Washington, Seattle, WA 98195.; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195., Zeymer C; Laboratory of Organic Chemistry, Eidgenössische Technische Hochschule (ETH) Zürich, 8093 Zürich, Switzerland; dabaker@uw.edu cathleen.zeymer@tum.de.; Department of Chemistry, Technische Universität München, 85747 Garching, Germany.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Dec 01; Vol. 117 (48), pp. 30362-30369. Date of Electronic Publication: 2020 Nov 17.