Solution structure and synaptic analyses reveal determinants of bispecific T cell engager potency
Alexander Leithner(Institute of Science and Technology Austria), Michael L. Dustin(Nuffield Orthopaedic Centre), S. Hoerer(Boehringer Ingelheim (Germany)), Hannah Dada(Nuffield Orthopaedic Centre), Oskar Staufer(Nuffield Orthopaedic Centre), Omer Dushek(University of Oxford), Maureen Crames(Boehringer Ingelheim (United States)), Salvatore Valvo(University of Oxford), Edward Jenkins(John Radcliffe Hospital), Mikhail A. Kutuzov(University of Oxford), Stephen R. Comeau, David Klenerman(University of Cambridge), Herbert Nar(Boehringer Ingelheim (Germany)), Sophia Reindl(Boehringer Ingelheim (Germany)), Simon J. Davis(University of Oxford), Noah Pefaur(Boehringer Ingelheim (United States)), Sarah Löw(Boehringer Ingelheim (United States)), Falk Liberta(Boehringer Ingelheim (Germany)), Srinath Kasturirangan(Boehringer Ingelheim (France)), Tanmay Mitra(University of Oxford), Weijie Zhou(Boehringer Ingelheim (United States)), David Young(Boehringer Ingelheim (United States)), David Wyatt(Boehringer Ingelheim (Germany)), Felix Schiele(Boehringer Ingelheim (Germany)), J.‐M. Spaeth(Nuffield Orthopaedic Centre), Andrew E. Nixon
Cited by 12
Related Papers
Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5·5 and pH 9·0
|Journal of Molecular Biology|1991|487
Structure-Based Design of Novel Potent Nonpeptide Thrombin Inhibitors
|Journal of Medicinal Chemistry|2002|454
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
|Nature Communications|2019|450