Fang Yi
Janssen Pharmaceutica
5 Papers
5 Citations
Fang Yi is an academic researcher from Janssen Pharmaceutica. The author has contributed to research in topics: Antibody & Chemistry. The author has an hindex of 3, co-authored 4 publications.
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Papers
Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokinetics
TL;DR: The engineering of a novel albumin binding domain (ABD) three-helix bundle protein, called ABDCon, is described, which binds human, monkey and mouse serum albumins with affinity as high as 61 pM and is highly stable.
Evaluation of a Centyrin-Based Near-Infrared Probe for Fluorescence-Guided Surgery of Epidermal Growth Factor Receptor Positive Tumors
Sakkarapalayam M. Mahalingam,Vadim Dudkin,Shalom Goldberg,Donna Klein,Fang Yi,Sunil Singhal,Karyn O'neil,Philip S. Low +7 more
TL;DR: Data suggest that CNDCs can be used for intraoperative identification and surgical removal of EGFR-expressing lesions and that Centyrins targeted to other tumor-specific antigens should prove similarly useful in fluorescence guided surgery of cancer.
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“Stapling” scFv for multispecific biotherapeutics of superior properties
Lauren E. Boucher,Elisabeth G. Prinslow,Michael Feldkamp,Fang Yi,Rupesh Nanjunda,Sheng-Jiun Wu,Eilyn R. Lacy,Steven A. Jacobs,Natalia Kozlyuk,Bingyuan Wu,Nicholas Mazzanti,James Testa,Michael D. Diem,Elsa Gorre,Andrew Mahan,Hirsh Nanda,Harsha P. Gunawardena,Alexis Gervais,Anthony A. Armstrong,Alexey Teplyakov,Chichi Huang,Adam Zwolak,Partha Chowdhury,Wan Cheung Cheung,Jinquan Luo +24 more
TL;DR: In this article , the authors proposed a stapling strategy that introduces two disulfide bonds between the single-chain fragment variable (scFv) linker and the two variable domains to minimize scFv breathing.
11
Induced conformational change in human IL-4 upon binding of a signal-neutralizing DARPin
Galina Obmolova,Alexey Teplyakov,Thomas J. Malia,Edward Keough,Jinquan Luo,Raymond Sweet,Steven Jacobs,Fang Yi,Randi Hippensteel,Karyn O'neil,Gary L. Gilliland +10 more
TL;DR: The crystal structure of DARPin 44C12V5 that neutralizesIL‐4 signaling has been determined alone and bound to human IL‐4 and reveals how the DARPin neutralizes IL‐ 4 signaling.
6
Selection of high-affinity Centyrin FN3 domains from a simple library diversified at a combination of strand and loop positions
Michael D. Diem,Linus Hyun,Fang Yi,Randi Hippensteel,Elise Kuhar,Cassandra Lowenstein,Edward J. Swift,Karyn O'neil,Steven Jacobs +8 more
TL;DR: The generation of a library built upon the framework of a consensus FN3 domain sequence resulting in binding proteins the authors call Centyrins is described, which provides important data contributing to the understanding of potential FN3 binding interfaces and a new tool for generating high-affinity scaffold molecules.