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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Molecular insights into type I secretion systems
TL;DR: This review will provide a detailed view of the components of the translocator and will summarize structural as well as functional data.
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Kinetic isomers of a class II MHC-peptide complex.
TL;DR: It is demonstrated that a water-soluble version of the murine class II MHC molecule I-Ek complexed with an antigenic peptide derived from pigeon cytochrome c (PCC) displays monophasic as well as biphasic dissociation kinetics, demonstrating that the isomers interconvert and exist in a pH-sensitive equilibrium.
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An aeroplysinin-1 specific nitrile hydratase isolated from the marine sponge Aplysina cavernicola.
TL;DR: The enzymes were shown to be manganese dependent, although cobalt and nickel ions were also able to recover the activity of the nitrile hydratases, and showed high substrate specificity towards the physiological substrate aeroplysinin-1.
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Mass spectrometry‐based abundance atlas of ABC transporters in human liver, gut, kidney, brain and skin
Zubida M. Al-Majdoub,Brahim Achour,Narciso Couto,Martyn Howard,Yasmine Elmorsi,Daniel Scotcher,Sarah Alrubia,Sarah Alrubia,Eman El-Khateeb,Eman El-Khateeb,Areti-Maria Vasilogianni,Noura Alohali,Noura Alohali,Sibylle Neuhoff,Lutz Schmitt,Amin Rostami-Hodjegan,Jill Barber +16 more
TL;DR: Interestingly, this atlas unveiled that ABCB2/TAP1 may have TAP2‐independent functions in the brain and that biliary atresia (BA) and control livers have quite different ABC transporter profiles.
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Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation.
TL;DR: The crystal structure of ChoX is reported in an unusual, ligand-free conformation that represents a semi-closed form of ChoZ, and comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.