Biotinylated Polyacrylamide-Based Metal-Chelating Polymers and Their Influence on Antigen Recognition Following Conjugation to a Trastuzumab Fab Fragment

2012 ◽  
Vol 13 (9) ◽  
pp. 2831-2842 ◽  
Author(s):  
Peng Liu ◽  
Amanda J. Boyle ◽  
Yijie Lu ◽  
Raymond M. Reilly ◽  
Mitchell A. Winnik
2021 ◽  
Author(s):  
Penny J. Le ◽  
Shane Miersch ◽  
Matthew W. Forbes ◽  
Nick Jarvik ◽  
Anthony Ku ◽  
...  

2017 ◽  
Vol 3 (3) ◽  
pp. 279-290 ◽  
Author(s):  
Yijie Lu ◽  
Amanda J. Boyle ◽  
Ping-Jiang Cao ◽  
David Hedley ◽  
Raymond M. Reilly ◽  
...  

2012 ◽  
Vol 13 (8) ◽  
pp. 2359-2369 ◽  
Author(s):  
Nicolas Illy ◽  
Daniel Majonis ◽  
Isaac Herrera ◽  
Olga Ornatsky ◽  
Mitchell A. Winnik

2016 ◽  
Vol 7 (1) ◽  
pp. 164-170 ◽  
Author(s):  
Irene Roncero-Ramos ◽  
Silvia Pastoriza ◽  
M. Pilar Navarro ◽  
Cristina Delgado-Andrade

The behaviour of dietary Maillard reaction compounds (MRP) as metal chelating polymers can alter mineral absorption and/or retention.


2015 ◽  
Vol 16 (11) ◽  
pp. 3613-3623 ◽  
Author(s):  
Peng Liu ◽  
Amanda J. Boyle ◽  
Yijie Lu ◽  
Jarrett Adams ◽  
Yuechuan Chi ◽  
...  

2016 ◽  
Vol 17 (4) ◽  
pp. 1292-1302 ◽  
Author(s):  
Simmyung Yook ◽  
Yijie Lu ◽  
Jenny Jooyoung Jeong ◽  
Zhongli Cai ◽  
Lemuel Tong ◽  
...  

2018 ◽  
Vol 16 (2) ◽  
pp. 768-778 ◽  
Author(s):  
Sadaf Aghevlian ◽  
Zhongli Cai ◽  
Yijie Lu ◽  
David W. Hedley ◽  
Mitchell A. Winnik ◽  
...  

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Fu-Lien Hsieh ◽  
Matthew K Higgins

Antibodies are critical components of the human adaptive immune system, providing versatile scaffolds to display diverse antigen-binding surfaces. Nevertheless, most antibodies have similar architectures, with the variable immunoglobulin domains of the heavy and light chain each providing three hypervariable loops, which are varied to generate diversity. The recent identification of a novel class of antibody in humans from malaria endemic regions of Africa was therefore surprising as one hypervariable loop contains the entire collagen-binding domain of human LAIR1. Here, we present the structure of the Fab fragment of such an antibody. We show that its antigen-binding site has adopted an architecture that positions LAIR1, while itself being occluded. This therefore represents a novel means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking a human protein insert with antigen-binding potential to the constant antibody regions which mediate immune cell recruitment.


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