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Claudin-4 Reconstituted in Unilamellar Vesicles is Sufficient to Form Tight Interfaces that Partition Membrane Proteins
Brian Belardi, Sungmin Son, Michael D. Vahey, Jinzhi Wang, Jianghui Hou, View ORCID ProfileDaniel A. Fletcher
doi: https://doi.org/10.1101/309856
Brian Belardi
1Department of Bioengineering and Biophysics Program, University of California, Berkeley, CA, 94720 USA
Sungmin Son
1Department of Bioengineering and Biophysics Program, University of California, Berkeley, CA, 94720 USA
Michael D. Vahey
1Department of Bioengineering and Biophysics Program, University of California, Berkeley, CA, 94720 USA
Jinzhi Wang
3Department of Internal Medicine & Center for Investigation of Membrane Excitability Disease, Washington University Medical School, St. Louis, MO 63110 USA
Jianghui Hou
3Department of Internal Medicine & Center for Investigation of Membrane Excitability Disease, Washington University Medical School, St. Louis, MO 63110 USA
Daniel A. Fletcher
1Department of Bioengineering and Biophysics Program, University of California, Berkeley, CA, 94720 USA
2Division of Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720 USA
4Chan Zuckerberg Biohub, San Francisco, CA 94158
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Posted April 27, 2018.
Claudin-4 Reconstituted in Unilamellar Vesicles is Sufficient to Form Tight Interfaces that Partition Membrane Proteins
Brian Belardi, Sungmin Son, Michael D. Vahey, Jinzhi Wang, Jianghui Hou, Daniel A. Fletcher
bioRxiv 309856; doi: https://doi.org/10.1101/309856
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