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.
Papers
More filters
Journal ArticleDOI
Evidence for a credit-card-swipe mechanism in the human PC floppase ABCB4.
Martin Prescher,Michele Bonus,Jan Stindt,Verena Keitel-Anselmino,Sander H. J. Smits,Holger Gohlke,Holger Gohlke,Lutz Schmitt +7 more
TL;DR: ABCB4 as discussed by the authors is described as an ATP-binding cassette (ABC) transporter that primarily transports lipids of the phosphatidylcholine (PC) family but is also capable of translocating a subset of typical multidrug-resistance-associated drugs.
Journal ArticleDOI
Addendum to "A structural classification of substrate-binding proteins" [FEBS Lett. 584 (2010) 2606-2617]
TL;DR: A DALI search in addition to the FFAS server and PSI-BLAST detected 7 new pro-tein structures and identified four proteins belonging to the TAXI and TTT families of TRAP-transporters, which are miss-ing from the authors' analysis.
Journal ArticleDOI
A phospholipase B from Pseudomonas aeruginosa with activity towards endogenous phospholipids affects biofilm assembly.
Andrea J. Weiler,Olivia Spitz,Mirja Gudzuhn,Stephan Schott-Verdugo,Michael Kamel,Björn Thiele,Wolfgang R. Streit,Alexej Kedrov,Lutz Schmitt,Holger Gohlke,Filip Kovacic +10 more
TL;DR: In this article , the authors demonstrate that the hypothetical gene pa2927 of Pseudomonas aeruginosa encodes a novel phospholipase B named PaPlaB.
Journal ArticleDOI
Secretion of slow-folding proteins by a Type 1 secretion system.
TL;DR: Taking together, theses two studies suggest that the introduction of slow-folding mutations into a protein sequence might be the key to use Type 1 secretion systems for the biotechnological production of proteins.
Journal ArticleDOI
Water-mediated protein–fluorophore interactions modulate the affinity of an ABC-ATPase/TNP–ADP complex
TL;DR: The crystal structure of the TNP-ADP/HlyB-NBD complex is determined and in silico approaches such as docking or modeling cannot directly be applied to generate 'affinity-adopted' ADP- or ATP-analogs for ABC-ATPases.