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
Type I secretion systems - a story of appendices.
TL;DR: The function of the appendix and the differences that might exist among the three families of T1SS are compared and the current knowledge of these one-step transport machineries are summarized with emphasis on the N-terminal extensions found in many Type I-specific ABC transporters.
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Crystal Structures of the Choline/Acetylcholine Substrate-binding Protein ChoX from Sinorhizobium meliloti in the Liganded and Unliganded-Closed States
Christine Oswald,Sander H. J. Smits,Marina Höing,Linda Sohn-Bösser,Laurence Dupont,Daniel Le Rudulier,Lutz Schmitt,Erhard Bremer +7 more
TL;DR: Fluorescence-based ligand binding assays used to quantitate substrate binding by the periplasmic ligand-binding protein ChoX confirmed that ChoX recognizes choline and acetylcholine with high and medium affinity, respectively, and solved the crystal structures of ChoX in a closed, substrate-free conformation.
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Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter.
Jelena Zaitseva,Stefan Jenewein,Alexander Wiedenmann,Houssain Benabdelhak,I. Barry Holland,Lutz Schmitt +5 more
TL;DR: Experimental data showed that both the nature and pH of an assay buffer influenced the level of protein activity, and comparative analysis of protein stability and ATPase activity in various buffers suggests an inverse relationship between the two.
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Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids.
TL;DR: By synthesis of a class of chelator lipids, this concept represents a powerful technique for orientation and organization of proteins at lipid interfaces with applications in biosensing, biofunctionalization of nanostructured interfaces, two-dimensional crystallization, and studies of lipid-anchored proteins.
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Sequencing of FIC1, BSEP and MDR3 in a large cohort of patients with cholestasis revealed a high number of different genetic variants.
Carola Dröge,Michele Bonus,Ulrich Baumann,Caroline Klindt,Elke Lainka,Simone Kathemann,Florian Brinkert,Enke Grabhorn,Eva-Doreen Pfister,Daniel Wenning,Alexander Fichtner,Daniel Gotthardt,Karl Heinz Weiss,Patrick J McKiernan,Ratna Dua Puri,I. C. Verma,Stefanie Kluge,Holger Gohlke,Lutz Schmitt,Ralf Kubitz,Dieter Häussinger,Verena Keitel +21 more
TL;DR: In patients without a disease-causing mutation, common genetic variants were detected in a high number of cases, indicating that these common variants may contribute to cholestasis development.