High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875-Reference-Cited by-同舟云学术

High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875

Published:2014-07-20 Issue:7516 Volume:513 Page:124-127
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Srivastava Ankita,Yano Jason,Hirozane Yoshihiko,Kefala Georgia,Gruswitz Franz,Snell Gyorgy,Lane Weston,Ivetac Anthony,Aertgeerts Kathleen,Nguyen Jasmine,Jennings Andy,Okada Kengo

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature13494.pdf

Reference41 articles.

1. Itoh, Y. et al. Free fatty acids regulate insulin secretion from pancreatic β cells through GPR40. Nature 422, 173–176 (2003)

2. McGarry, J. D. & Dobbins, R. L. Fatty acids, lipotoxicity and insulin secretion. Diabetologia 42, 128–138 (1999)

3. Yabuki, C. et al. A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-allosteric modulator of FFAR1. PLoS ONE 8, :e76280. (2013)

4. Negoro, N. et al. Discovery of TAK-875: a potent, selective, and orally bioavailable GPR40 agonist. ACS Med. Chem. Lett. 1, 290–294 (2010)

5. Burant, C. F. et al. TAK-875 versus placebo or glimepiride in type 2 diabetes mellitus: a phase 2, randomised, double-blind, placebo-controlled trial. Lancet 379, 1403–1411 (2012)

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