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The light-driven sodium ion pump: A new player in rhodopsin research.
- Published in:
- BioEssays, 2016, v. 38, n. 12, p. 1274, doi. 10.1002/bies.201600065
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Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin.
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- Scientific Reports, 2015, p. 8545, doi. 10.1038/ncomms9545
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- Article
Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin.
- Published in:
- Nature Communications, 2015, v. 6, n. 10, p. 8545, doi. 10.1038/ncomms9545
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- Article
Structural insights into µ-opioid receptor activation.
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- Nature, 2015, v. 524, n. 7565, p. 315, doi. 10.1038/nature14886
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- Article
Molecular Dynamics of Channelrhodopsin at the Early Stages of Channel Opening.
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- PLoS ONE, 2015, v. 10, n. 6, p. 1, doi. 10.1371/journal.pone.0131094
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Structural basis for Na<sup>+</sup> transport mechanism by a light-driven Na<sup>+</sup> pump.
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- Nature, 2015, v. 521, n. 7550, p. 48, doi. 10.1038/nature14322
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- Article
Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK.
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- Nature Communications, 2015, v. 6, n. 5, p. 7097, doi. 10.1038/ncomms8097
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- Article
Atomistic design of microbial opsin-based blue-shifted optogenetics tools.
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- Nature Communications, 2015, v. 6, n. 5, p. 7177, doi. 10.1038/ncomms8177
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- Article
Crystallization and preliminary X-ray diffraction analysis of YidC, a membrane-protein chaperone and insertase from Bacillus halodurans.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2014, v. 70, n. 8, p. 1056, doi. 10.1107/S2053230X14012540
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Structural basis for the drug extrusion mechanism by a MATE multidrug transporter.
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- Nature, 2013, v. 496, n. 7444, p. 247, doi. 10.1038/nature12014
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- Article
Crystal structure of channelrhodopsin, a light-gated cation channel - all cations lead through the monomer.
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- Biophysics (13492942), 2013, v. 9, p. 57, doi. 10.2142/biophysics.9.57
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- Article
Crystal structure of the channelrhodopsin light-gated cation channel.
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- Nature, 2012, v. 482, n. 7385, p. 369, doi. 10.1038/nature10870
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- Article