M
Martin Caffrey
Researcher at Trinity College, Dublin
Publications - 227
Citations - 18372
Martin Caffrey is an academic researcher from Trinity College, Dublin. The author has contributed to research in topics: Phase (matter) & Membrane protein. The author has an hindex of 64, co-authored 223 publications receiving 17083 citations. Previous affiliations of Martin Caffrey include Ithaca College & Indiana University – Purdue University Indianapolis.
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Journal ArticleDOI
Crystal structure of the β2 adrenergic receptor-Gs protein complex.
Søren G. F. Rasmussen,Brian T. DeVree,Yaozhong Zou,Andrew C. Kruse,Ka Young Chung,Tong Sun Kobilka,Foon Sun Thian,Pil Seok Chae,Els Pardon,Els Pardon,Diane M. Calinski,Jesper Mosolff Mathiesen,Syed T. A. Shah,Joseph A. Lyons,Martin Caffrey,Samuel H. Gellman,Jan Steyaert,Jan Steyaert,Georgios Skiniotis,William I. Weis,Roger K. Sunahara,Brian K. Kobilka +21 more
TL;DR: This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.
Journal ArticleDOI
Phases and phase transitions of the phosphatidylcholines
Rumiana Koynova,Martin Caffrey +1 more
TL;DR: A review of the data subset referring to phosphatidylcholine phase behavior reflecting changes in lipid chain length, unsaturation, asymmetry and branching, type of chain-glycerol linkage (ester, ether, amide), and position of chain attachment to the glycerol backbone are presented.
Journal ArticleDOI
Structure and function of an irreversible agonist-β2 adrenoceptor complex
Daniel M. Rosenbaum,Cheng Zhang,Joseph A. Lyons,Joseph A. Lyons,Ralph Holl,David Aragão,Daniel H. Arlow,Sã̧ren G F Rasmussen,Hee Jung Choi,Brian T. DeVree,Roger K. Sunahara,Pil Seok Chae,Samuel H. Gellman,Ron O. Dror,David E. Shaw,William I. Weis,Martin Caffrey,Peter Gmeiner,Brian K. Kobilka +18 more
TL;DR: A covalent agonist-bound β2AR–T4L fusion protein is designed that can be covalently tethered to a specific site on the receptor through a disulphide bond, and is capable of activating a heterotrimeric G protein.
Journal ArticleDOI
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Yanyong Kang,X. Edward Zhou,Xiang Gao,Yuanzheng He,Wei Liu,Andrii Ishchenko,Anton Barty,Thomas A. White,Oleksandr Yefanov,Gye Won Han,Qingping Xu,Parker W. de Waal,Jiyuan Ke,M. H. Eileen Tan,Chenghai Zhang,Arne Moeller,Graham M. West,Bruce D. Pascal,Ned Van Eps,Lydia N. Caro,Sergey A. Vishnivetskiy,Regina J. Lee,Kelly Suino-Powell,Xin Gu,Kuntal Pal,Jinming Ma,Xiaoyong Zhi,Sébastien Boutet,Garth J. Williams,Marc Messerschmidt,Cornelius Gati,Nadia A. Zatsepin,Dingjie Wang,Daniel James,Shibom Basu,Shatabdi Roy-Chowdhury,Chelsie E. Conrad,Jesse Coe,Haiguang Liu,Stella Lisova,Christopher Kupitz,Ingo Grotjohann,Raimund Fromme,Yi Jiang,Minjia Tan,Huaiyu Yang,Jun Li,Meitian Wang,Zhong Zheng,Dianfan Li,Nicole Howe,Yingming Zhao,Jörg Standfuss,Kay Diederichs,Yuhui Dong,Clinton S. Potter,Bridget Carragher,Martin Caffrey,Hualiang Jiang,Henry N. Chapman,John C. H. Spence,Petra Fromme,Uwe Weierstall,Oliver P. Ernst,Vsevolod Katritch,Vsevolod V. Gurevich,Patrick R. Griffin,Wayne L. Hubbell,Raymond C. Stevens,Vadim Cherezov,Karsten Melcher,H. Eric Xu +71 more
TL;DR: The crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin is determined by serial femtosecond X-ray laser crystallography and provides a basis for understanding GPCR-mediated arrestin-biased signalling.
Journal ArticleDOI
Crystallizing membrane proteins using lipidic mesophases
Martin Caffrey,Vadim Cherezov +1 more
TL;DR: The method has been shown to be quite general in that it has been used to solve X-ray crystallographic structures of prokaryotic and eukaryotic proteins, proteins that are monomeric, homo- and hetero-multimeric, chromophore-containing and chromophile-free, and α-helical and β-barrel proteins.