Emma Morrison - Publications
Affiliations: | 2008-2014 | Biochemistry | Medical College of Wisconsin, Milwaukee, WI, United States |
Year | Citation | Score | |||
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2018 | Thomas NE, Wu C, Morrison EA, Robinson AE, Werner JP, Henzler-Wildman K. The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release. The Journal of Biological Chemistry. PMID 30287687 DOI: 10.1074/jbc.RA118.005430 | 0.691 | |||
2017 | Robinson AE, Thomas NE, Morrison EA, Balthazor BM, Henzler-Wildman KA. New free-exchange model of EmrE transport. Proceedings of the National Academy of Sciences of the United States of America. PMID 29114048 DOI: 10.1073/pnas.1708671114 | 0.707 | |||
2015 | Morrison EA, Robinson AE, Liu Y, Henzler-Wildman KA. Asymmetric protonation of EmrE. The Journal of General Physiology. PMID 26573622 DOI: 10.1085/jgp.201511404 | 0.665 | |||
2014 | Dutta S, Morrison EA, Henzler-Wildman KA. Blocking dynamics of the SMR transporter EmrE impairs efflux activity. Biophysical Journal. 107: 613-20. PMID 25099800 DOI: 10.1016/J.Bpj.2014.06.030 | 0.689 | |||
2014 | Dutta S, Morrison EA, Henzler-Wildman KA. EmrE dimerization depends on membrane environment. Biochimica Et Biophysica Acta. 1838: 1817-22. PMID 24680655 DOI: 10.1016/J.Bbamem.2014.03.013 | 0.658 | |||
2014 | Morrison EA, Henzler-Wildman KA. Transported substrate determines exchange rate in the multidrug resistance transporter EmrE. The Journal of Biological Chemistry. 289: 6825-36. PMID 24448799 DOI: 10.1074/jbc.M113.535328 | 0.698 | |||
2012 | Morrison EA, Henzler-Wildman KA. Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile. Biochimica Et Biophysica Acta. 1818: 814-20. PMID 22226849 DOI: 10.1016/j.bbamem.2011.12.020 | 0.593 | |||
2012 | Morrison EA, DeKoster GT, Dutta S, Vafabakhsh R, Clarkson MW, Bahl A, Kern D, Ha T, Henzler-Wildman KA. Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature. 481: 45-50. PMID 22178925 DOI: 10.1038/Nature10703 | 0.705 | |||
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