GPCR and G proteins: drug efficacy and activation in live cells
J. Vilardaga, M. Bunemann, T. Feinstein, N. Lambert, V. Nikolaev, S. Engelhardt, M. Lohse, and C. Hoffmann. Mol Endocrinol, 23 (5):
590-9(May 2009)Vilardaga, Jean-Pierre Bunemann, Moritz Feinstein, Timothy N Lambert,
Nevin Nikolaev, Viacheslav O Engelhardt, Stefan Lohse, Martin J Hoffmann,
Carsten Research Support, Non-U.S. Gov't Review United States Molecular
endocrinology (Baltimore, Md.) Mol Endocrinol. 2009 May;23(5):590-9.
Epub 2009 Feb 5..
Abstract
Many biochemical pathways are driven by G protein-coupled receptors,
cell surface proteins that convert the binding of extracellular chemical,
sensory, and mechanical stimuli into cellular signals. Their interaction
with various ligands triggers receptor activation that typically
couples to and activates heterotrimeric G proteins, which in turn
control the propagation of secondary messenger molecules (e.g. cAMP)
involved in critically important physiological processes (e.g. heart
beat). Successful transfer of information from ligand binding events
to intracellular signaling cascades involves a dynamic interplay
between ligands, receptors, and G proteins. The development of Forster
resonance energy transfer and bioluminescence resonance energy transfer-based
methods has now permitted the kinetic analysis of initial steps involved
in G protein-coupled receptor-mediated signaling in live cells and
in systems as diverse as neurotransmitter and hormone signaling.
The direct measurement of ligand efficacy at the level of the receptor
by Forster resonance energy transfer is also now possible and allows
intrinsic efficacies of clinical drugs to be linked with the effect
of receptor polymorphisms.
Vilardaga, Jean-Pierre Bunemann, Moritz Feinstein, Timothy N Lambert,
Nevin Nikolaev, Viacheslav O Engelhardt, Stefan Lohse, Martin J Hoffmann,
Carsten Research Support, Non-U.S. Gov't Review United States Molecular
endocrinology (Baltimore, Md.) Mol Endocrinol. 2009 May;23(5):590-9.
Epub 2009 Feb 5.
%0 Journal Article
%1 Vilardaga2009
%A Vilardaga, J. P.
%A Bunemann, M.
%A Feinstein, T. N.
%A Lambert, N.
%A Nikolaev, V. O.
%A Engelhardt, S.
%A Lohse, M. J.
%A Hoffmann, C.
%D 2009
%J Mol Endocrinol
%K Animals Biological Energy Fluorescence G-Protein-Coupled/chemistry/*metabolism GTP-Binding Humans Kinetics Luminescent Measurements Models, Proteins/chemistry/*metabolism Resonance Signal Transduction/*physiology Transfer Receptor
%N 5
%P 590-9
%T GPCR and G proteins: drug efficacy and activation in live cells
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19196832
%V 23
%X Many biochemical pathways are driven by G protein-coupled receptors,
cell surface proteins that convert the binding of extracellular chemical,
sensory, and mechanical stimuli into cellular signals. Their interaction
with various ligands triggers receptor activation that typically
couples to and activates heterotrimeric G proteins, which in turn
control the propagation of secondary messenger molecules (e.g. cAMP)
involved in critically important physiological processes (e.g. heart
beat). Successful transfer of information from ligand binding events
to intracellular signaling cascades involves a dynamic interplay
between ligands, receptors, and G proteins. The development of Forster
resonance energy transfer and bioluminescence resonance energy transfer-based
methods has now permitted the kinetic analysis of initial steps involved
in G protein-coupled receptor-mediated signaling in live cells and
in systems as diverse as neurotransmitter and hormone signaling.
The direct measurement of ligand efficacy at the level of the receptor
by Forster resonance energy transfer is also now possible and allows
intrinsic efficacies of clinical drugs to be linked with the effect
of receptor polymorphisms.
@article{Vilardaga2009,
abstract = {Many biochemical pathways are driven by G protein-coupled receptors,
cell surface proteins that convert the binding of extracellular chemical,
sensory, and mechanical stimuli into cellular signals. Their interaction
with various ligands triggers receptor activation that typically
couples to and activates heterotrimeric G proteins, which in turn
control the propagation of secondary messenger molecules (e.g. cAMP)
involved in critically important physiological processes (e.g. heart
beat). Successful transfer of information from ligand binding events
to intracellular signaling cascades involves a dynamic interplay
between ligands, receptors, and G proteins. The development of Forster
resonance energy transfer and bioluminescence resonance energy transfer-based
methods has now permitted the kinetic analysis of initial steps involved
in G protein-coupled receptor-mediated signaling in live cells and
in systems as diverse as neurotransmitter and hormone signaling.
The direct measurement of ligand efficacy at the level of the receptor
by Forster resonance energy transfer is also now possible and allows
intrinsic efficacies of clinical drugs to be linked with the effect
of receptor polymorphisms.},
added-at = {2010-12-14T18:12:02.000+0100},
author = {Vilardaga, J. P. and Bunemann, M. and Feinstein, T. N. and Lambert, N. and Nikolaev, V. O. and Engelhardt, S. and Lohse, M. J. and Hoffmann, C.},
biburl = {https://www.bibsonomy.org/bibtex/24cf9dab41bd86283832820574f5c57fd/pharmawuerz},
endnotereftype = {Journal Article},
interhash = {792b03d6c2ebbdffe8b3f5bc18e04809},
intrahash = {4cf9dab41bd86283832820574f5c57fd},
issn = {1944-9917 (Electronic) 1944-9917 (Linking)},
journal = {Mol Endocrinol},
keywords = {Animals Biological Energy Fluorescence G-Protein-Coupled/chemistry/*metabolism GTP-Binding Humans Kinetics Luminescent Measurements Models, Proteins/chemistry/*metabolism Resonance Signal Transduction/*physiology Transfer Receptor},
month = May,
note = {Vilardaga, Jean-Pierre Bunemann, Moritz Feinstein, Timothy N Lambert,
Nevin Nikolaev, Viacheslav O Engelhardt, Stefan Lohse, Martin J Hoffmann,
Carsten Research Support, Non-U.S. Gov't Review United States Molecular
endocrinology (Baltimore, Md.) Mol Endocrinol. 2009 May;23(5):590-9.
Epub 2009 Feb 5.},
number = 5,
pages = {590-9},
shorttitle = {GPCR and G proteins: drug efficacy and activation in live cells},
timestamp = {2010-12-14T18:20:09.000+0100},
title = {GPCR and G proteins: drug efficacy and activation in live cells},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19196832},
volume = 23,
year = 2009
}