L
Lutz Schmitt
Researcher at University of Düsseldorf
Publications - 202
Citations - 7303
Lutz Schmitt is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: ATP-binding cassette transporter & Secretion. The author has an hindex of 42, co-authored 182 publications receiving 6144 citations. Previous affiliations of Lutz Schmitt include University of Paris & University of Marburg.
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Journal ArticleDOI
The many facets of bile acids in the physiology and pathophysiology of the human liver.
Christoph G. W. Gertzen,Holger Gohlke,Holger Gohlke,Dieter Häussinger,Diran Herebian,Verena Keitel,Ralf Kubitz,Ertan Mayatepek,Lutz Schmitt +8 more
TL;DR: In this paper, the authors summarized the current knowledge of the physiology and pathophysiology of bile acids with an emphasis on recently established analytical approaches as well as the molecular mechanisms that underlie signaling and transport of Bile acids.
Journal ArticleDOI
Monomeric bile acids modulate the ATPase activity of detergent-solubilized ABCB4/MDR3.
TL;DR: In this paper, the authors investigated the modulation of ATP hydrolysis of ABC by different bile acids commonly present in humans and found that 24-nor-ursodeoxycholic acid was a distinct mode of regulation of ATPase activity.
Posted ContentDOI
A new twist in ABC transporter mediated multidrug resistance − Pdr5 is a drug/proton co-transporter
Manuel Wagner,Daniel Blum,Stefanie Raschka,Christoph G. W. Gertzen,Sander H. J. Smits,Richard Wagner,Lutz Schmitt +6 more
TL;DR: In this paper, the authors provide electrophysiological data on the reconstituted Pdr5 and demonstrate that this MDR efflux pump does not only actively translocate its substrates across the lipid bilayer, but also generates a proton motif force in the presence of Mg2+-ATP and substrates by acting as a drug co-transporter.
Posted ContentDOI
Mechanism of the secretion of the lanthipeptide nisin
TL;DR: In vivo secretion analysis of nisin, a ribosomally synthesized and post-translationally modified peptides containing dehydrated amino acids and (methyl-)lanthionine rings, demonstrated that the function of NisC is controlled, but the mere presence of NISB modulated the apparent secretion rates.
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Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli.
Iris Gawarzewski,Britta Tschapek,Astrid Hoeppner,Joachim Jose,Sander H. J. Smits,Lutz Schmitt +5 more
TL;DR: The purification, crystallization and preliminary X-ray crystallographic studies of the transport unit of AIDA-I are reported, which could provide new insights into the transport mechanism.