M. Ambrosio, A. Zurn, and M. Lohse. Neuropharmacology, (August 2010)Journal article Neuropharmacology Neuropharmacology. 2010 Aug 18..
Abstract
G protein-coupled receptors (GPCRs) are the key elements of a highly
regulated transduction machinery that generates different signaling
outcomes to hormones and neurotransmitters. Until recently, it was
assumed that diverse ligands of a given GPCR differ only in their
ability to alter the balance between the OFF and the ON state of
the receptor. However, it has now become evident that their activation
mechanisms are more complex and that receptors presumably display
distinguishable active conformational states, which are induced by
different agonists and correlate to specific signaling outputs. The
use of different labeling strategies to insert fluorescent labels
into purified, reconstituted receptors, or into receptors in intact
cells, has made it possible to sense receptor activation via changes
in their fluorescence. Here, we summarize recent progress in the
analysis of agonist-dependent activation mechanisms of GPCRs acquired
using modern spectroscopic and crystallographic techniques.
%0 Journal Article
%1 Ambrosio2010a
%A Ambrosio, M.
%A Zurn, A.
%A Lohse, M. J.
%D 2010
%J Neuropharmacology
%K imported
%T Sensing G protein-coupled receptor activation
%U http://www.ncbi.nlm.nih.gov/pubmed/20727363
%X G protein-coupled receptors (GPCRs) are the key elements of a highly
regulated transduction machinery that generates different signaling
outcomes to hormones and neurotransmitters. Until recently, it was
assumed that diverse ligands of a given GPCR differ only in their
ability to alter the balance between the OFF and the ON state of
the receptor. However, it has now become evident that their activation
mechanisms are more complex and that receptors presumably display
distinguishable active conformational states, which are induced by
different agonists and correlate to specific signaling outputs. The
use of different labeling strategies to insert fluorescent labels
into purified, reconstituted receptors, or into receptors in intact
cells, has made it possible to sense receptor activation via changes
in their fluorescence. Here, we summarize recent progress in the
analysis of agonist-dependent activation mechanisms of GPCRs acquired
using modern spectroscopic and crystallographic techniques.
@article{Ambrosio2010a,
abstract = {G protein-coupled receptors (GPCRs) are the key elements of a highly
regulated transduction machinery that generates different signaling
outcomes to hormones and neurotransmitters. Until recently, it was
assumed that diverse ligands of a given GPCR differ only in their
ability to alter the balance between the OFF and the ON state of
the receptor. However, it has now become evident that their activation
mechanisms are more complex and that receptors presumably display
distinguishable active conformational states, which are induced by
different agonists and correlate to specific signaling outputs. The
use of different labeling strategies to insert fluorescent labels
into purified, reconstituted receptors, or into receptors in intact
cells, has made it possible to sense receptor activation via changes
in their fluorescence. Here, we summarize recent progress in the
analysis of agonist-dependent activation mechanisms of GPCRs acquired
using modern spectroscopic and crystallographic techniques.},
added-at = {2010-12-14T18:12:02.000+0100},
author = {Ambrosio, M. and Zurn, A. and Lohse, M. J.},
biburl = {https://www.bibsonomy.org/bibtex/247cc1fbbba63609f7118f512f7e15600/pharmawuerz},
endnotereftype = {Journal Article},
groups = {private},
interhash = {e4d25f15c9dafaad106e83e1e2b1e4da},
intrahash = {47cc1fbbba63609f7118f512f7e15600},
issn = {1873-7064 (Electronic) 0028-3908 (Linking)},
journal = {Neuropharmacology},
keywords = {imported},
month = {Aug 18},
note = {Journal article Neuropharmacology Neuropharmacology. 2010 Aug 18.},
shorttitle = {Sensing G protein-coupled receptor activation},
timestamp = {2010-12-14T18:12:03.000+0100},
title = {Sensing G protein-coupled receptor activation},
url = {http://www.ncbi.nlm.nih.gov/pubmed/20727363},
year = 2010
}