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@INPROCEEDINGS{Vickery:817958,
author = {Vickery, O. N. and Machtens, Jan-Philipp and Tamburrino, G.
and Seeliger, D. and Zachariae, U.},
title = {{I}nternal sodium in {GPCR}s strongly responds to
transmembrane voltage changes},
journal = {Biophysical journal},
volume = {110},
number = {3},
issn = {0006-3495},
address = {Cambridge, Mass.},
publisher = {Cell Press},
reportid = {FZJ-2016-04537},
pages = {425a-426a},
year = {2016},
abstract = {G protein-coupled receptors (GPCRs) are the largest
superfamily of membrane proteins in the human genome,
mediating the propagation of extracellular ligand binding
information into intracellular signal transduction cascades.
Crystal structures have revealed a water-filled hydrophilic
internal pocket within their transmembrane domain, extending
from the orthosteric ligand-binding site to regions near the
G protein binding site. Recent high-resolution structures
have identified a sodium ion near the base of this pocket,
coordinated by highly conserved residues (1,2).},
month = {Feb},
date = {2016-02-27},
organization = {60th Annual Meeting of the
Biophysical-Society, Los Angeles, CA
(USA), 27 Feb 2016 - 2 Mar 2016},
cin = {ICS-4},
ddc = {570},
cid = {I:(DE-Juel1)ICS-4-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16 / PUB:(DE-HGF)8},
UT = {WOS:000375142700079},
doi = {10.1016/j.bpj.2015.11.2300},
url = {https://juser.fz-juelich.de/record/817958},
}