C
Christian Lücke
Researcher at Max Planck Society
Publications - 74
Citations - 2140
Christian Lücke is an academic researcher from Max Planck Society. The author has contributed to research in topics: Protein structure & Fatty acid-binding protein. The author has an hindex of 27, co-authored 74 publications receiving 2020 citations. Previous affiliations of Christian Lücke include National Institutes of Health & Goethe University Frankfurt.
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Journal ArticleDOI
Structural Basis for High-Affinity Peptide Inhibition of Human Pin1
Yan Zhang,Sebastian Daum,Dirk Wildemann,Xiao Zhen Zhou,Mark A. Verdecia,Marianne E. Bowman,Christian Lücke,Tony Hunter,Kun Ping Lu,Gunter Fischer,Joseph P. Noel +10 more
TL;DR: Two high-resolution X-ray crystal structures of human Pin1 bound to non-natural peptide inhibitors identify a type-I beta-turn conformation for Pin1 prolyl peptide isomerase domain-peptide binding and an extensive molecular interface for high-affinity recognition.
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Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris.
TL;DR: The crystal structure of the D FPase from Loligo vulgaris is the first example of a structural characterization of a squid-type DFPase and the second crystal structureof a PTE determined to date, and may serve as a structural model for squid- type DFPases in general.
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The specific FKBP38 inhibitor N-(N',N'-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia.
Frank Edlich,Matthias Weiwad,Dirk Wildemann,Franziska Jarczowski,Susann Kilka,Marie-Christine Moutty,Günther Jahreis,Christian Lücke,Werner Schmidt,Frank Striggow,Gunter Fischer +10 more
TL;DR: It is demonstrated that FKBP38 inhibition by DM-CHX regulates neuronal cell death and proliferation, providing a promising strategy for the treatment of acute and/or chronic neurodegenerative diseases.
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Functional Tat transport of unstructured, small, hydrophilic proteins.
TL;DR: This study demonstrates for the first time Tat transport for fully unstructured proteins, using signal sequence fusions to naturally unfolded FG repeats from the yeast Nsp1p nuclear pore protein, and explains the observed restriction of the Tat system to folded globular proteins on a molecular level.
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TWISTED DWARF1 Mediates the Action of Auxin Transport Inhibitors on Actin Cytoskeleton Dynamics.
Jinsheng Zhu,Aurélien Bailly,Aurélien Bailly,Marta Zwiewka,Valpuri Sovero,Martin Di Donato,Pei Ge,Jacqueline Oehri,Jacqueline Oehri,Bibek Aryal,Pengchao Hao,Miriam Linnert,Noelia I. Burgardt,Christian Lücke,Matthias Weiwad,Max Michel,Oliver H. Weiergräber,Stephan Pollmann,Elisa Azzarello,Stefano Mancuso,Noel Ferro,Yoichiro Fukao,Céline Hoffmann,Roland Wedlich-Söldner,Jiří Friml,Clément Thomas,Markus Geisler,Markus Geisler +27 more
TL;DR: Evidence is provided that TWD1 determines downstream locations of auxin efflux transporters by adjusting actin filament debundling and dynamizing processes and mediating NPA action on the latter, which appears to be evolutionary conserved.