Optimising the combination of thermostabilising mutations in the neurotensin receptor for structure determination-Reference-Cited by-同舟云学术

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Optimising the combination of thermostabilising mutations in the neurotensin receptor for structure determination

Published:2013-04 Issue:4 Volume:1828 Page:1293-1301
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Shibata Yoko,Gvozdenovic-Jeremic Jelena,Love James,Kloss Brian,White Jim F.,Grisshammer Reinhard,Tate Christopher G.

Funder

Pfizer Global Research and Development and the MRCT Development Gap Fund

UK Medical Research Council

Intramural Research Program of the National Institutes of Health, National Institute of Neurological Disorders and Stroke

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference37 articles.

1. Crystal structure of rhodopsin: a G protein-coupled receptor;Palczewski;Science,2000

2. Crystal structure of the ligand-free G-protein-coupled receptor opsin;Park;Nature,2008

3. Crystal structure of opsin in its G-protein-interacting conformation;Scheerer;Nature,2008

4. Structure of bovine rhodopsin in a trigonal crystal form;Li;J. Mol. Biol.,2004

5. Restructuring G-protein- coupled receptor activation;Audet;Cell,2012

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4. Protein Design Strategies for the Structural–Functional Studies of G Protein-Coupled Receptors;Biochemistry (Moscow);2023-01

5. Development of an Outward Proton Pumping Rhodopsin with a New Record in Thermostability by Means of Amino Acid Mutations;The Journal of Physical Chemistry B;2022-01-28

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