Akiko Koide
University of Chicago
96 Papers
479 Citations
Akiko Koide is an academic researcher from University of Chicago. The author has contributed to research in topics: Chemistry & Monobody. The author has an hindex of 37, co-authored 71 publications. Previous affiliations of Akiko Koide include University of Rochester Medical Center & University of Rochester.
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Papers
The fibronectin type III domain as a scaffold for novel binding proteins
TL;DR: Heteronuclear NMR characterization revealed that the selected mutant FN3s which bind to a test ligand, ubiquitin, with significant affinities, while the wild-type FN3 shows no measurable affinity.
719
Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide
Arun K. Shukla,Aashish Manglik,Andrew C. Kruse,Kunhong Xiao,Rosana I. Reis,Wei Chou Tseng,Dean P. Staus,Daniel Hilger,Serdar Uysal,Li-Yin Huang,Marcin Paduch,Prachi Tripathi-Shukla,Akiko Koide,Shohei Koide,William I. Weis,Anthony A. Kossiakoff,Brian K. Kobilka,Robert J. Lefkowitz,Robert J. Lefkowitz +18 more
TL;DR: The crystal structure of β-arrestin-1 in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the human V2 vasopressin receptor is reported, and results indicate a potentially general molecular mechanism for activation of these multifunctional signalling and regulatory proteins.
High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries.
Frederic A. Fellouse,Kaori Esaki,Sara C. Birtalan,Demetrios Raptis,Vincenzo J. Cancasci,Akiko Koide,Parkash Jhurani,Mark Vasser,Christian Wiesmann,Anthony A. Kossiakoff,Shohei Koide,Sachdev S. Sidhu +11 more
TL;DR: This fully synthetic, minimalist library has essentially recapitulated the capacity of the natural immune system to generate high-affinity antibodies by systematically augmented the original binary library with additional levels of diversity and examined the effects.
404
Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies
TL;DR: Structural insights are provided into how this widely used dye recognizes a prominent subset of peptide self-assemblies, and a strategy to elucidate the mechanisms of fibril-ligand interactions is proposed.
360
High-affinity single-domain binding proteins with a binary-code interface
TL;DR: It is shown that Tyr/Ser binary-code interfaces consisting of only 15–20 positions within a fibronectin type III domain are capable of producing specific binding proteins (termed “monobodies”) with a low-nanomolar Kd.
212