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| 001 | 817958 | ||
| 005 | 20210129224048.0 | ||
| 024 | 7 | _ | |a 10.1016/j.bpj.2015.11.2300 |2 doi |
| 024 | 7 | _ | |a WOS:000375142700079 |2 WOS |
| 037 | _ | _ | |a FZJ-2016-04537 |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Vickery, O. N. |0 P:(DE-HGF)0 |b 0 |
| 111 | 2 | _ | |a 60th Annual Meeting of the Biophysical-Society |c Los Angeles, CA |d 2016-02-27 - 2016-03-02 |w USA |
| 245 | _ | _ | |a Internal sodium in GPCRs strongly responds to transmembrane voltage changes |
| 260 | _ | _ | |a Cambridge, Mass. |c 2016 |b Cell Press |
| 300 | _ | _ | |a 425a-426a |
| 336 | 7 | _ | |a CONFERENCE_PAPER |2 ORCID |
| 336 | 7 | _ | |a Conference Paper |0 33 |2 EndNote |
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| 520 | _ | _ | |a 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). |
| 536 | _ | _ | |a 551 - Functional Macromolecules and Complexes (POF3-551) |0 G:(DE-HGF)POF3-551 |c POF3-551 |f POF III |x 0 |
| 700 | 1 | _ | |a Machtens, Jan-Philipp |0 P:(DE-Juel1)156429 |b 1 |u fzj |
| 700 | 1 | _ | |a Tamburrino, G. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Seeliger, D. |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Zachariae, U. |0 P:(DE-HGF)0 |b 4 |
| 773 | _ | _ | |a 10.1016/j.bpj.2015.11.2300 |0 PERI:(DE-600)1477214-0 |n 3 |p 425a-426a |t Biophysical journal |v 110 |y 2016 |x 0006-3495 |
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| 914 | 1 | _ | |y 2016 |
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