New innovations in allergy treatment and phenotyping

2021 ◽  
Vol 51 (4) ◽  
pp. 514-517
Author(s):  
Mohamed H. Shamji ◽  
Robert J. Boyle
Keyword(s):  
2018 ◽  
Vol 12 (2) ◽  
pp. 110-119 ◽  
Author(s):  
Jeronimo Carnes ◽  
Maria T. Gallego ◽  
Raquel Moya ◽  
Victor Iraola
Keyword(s):  

2020 ◽  
Vol 61 (3) ◽  
pp. 492-499 ◽  
Author(s):  
Aziz Homayouni Rad ◽  
Leili Aghebati Maleki ◽  
Hossein Samadi Kafil ◽  
Amin Abbasi

Author(s):  
Moaz Abdelwadoud ◽  
Sanaz Eftekhari ◽  
Hannah Jaffee ◽  
Melanie Carver ◽  
T. Joseph Mattingly

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ruixue Xia ◽  
Na Wang ◽  
Zhenmei Xu ◽  
Yang Lu ◽  
Jing Song ◽  
...  

AbstractHistamine receptors play important roles in various pathophysiological conditions and are effective targets for anti-allergy treatment, however the mechanism of receptor activation remain elusive. Here, we present the cryo-electron microscopy (cryo-EM) structure of the human H1R in complex with a Gq protein in an active conformation via a NanoBiT tethering strategy. The structure reveals that histamine activates receptor via interacting with the key residues of both transmembrane domain 3 (TM3) and TM6 to squash the binding pocket on the extracellular side and to open the cavity on the intracellular side for Gq engagement in a model of “squash to activate and expand to deactivate”. The structure also reveals features for Gq coupling, including the interaction between intracellular loop 2 (ICL2) and the αN-β junction of Gq/11 protein. The detailed analysis of our structure will provide a framework for understanding G-protein coupling selectivity and clues for designing novel antihistamines.


2016 ◽  
Vol 45 (4) ◽  
pp. e150-e156 ◽  
Author(s):  
Hetu Parekh ◽  
Sami L. Bahna

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