K
Kornelius Zeth
Researcher at Max Planck Society
Publications - 74
Citations - 5097
Kornelius Zeth is an academic researcher from Max Planck Society. The author has contributed to research in topics: Protein structure & Bacterial outer membrane. The author has an hindex of 38, co-authored 74 publications receiving 4776 citations. Previous affiliations of Kornelius Zeth include Spanish National Research Council & University of the Basque Country.
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Journal ArticleDOI
Structure of the human voltage-dependent anion channel
Monika Bayrhuber,Thomas Meins,Michael Habeck,Stefan Becker,Karin Giller,Saskia Villinger,Clemens Vonrhein,Christian Griesinger,Markus Zweckstetter,Kornelius Zeth +9 more
TL;DR: The 3D structure of human VDAC1 was solved conjointly by NMR spectroscopy and x-ray crystallography in this paper, which is the most abundant protein in the mitochondrial outer membrane (MOM).
Structure of the Human Voltage Dependent Anion Channel and Its Potential Role in Apoptosis
MA Bayrhuber,T Meins,Michael Habeck,C Vonrhein,Vijayan,S. Villinger,Stefan Becker,Christian Griesinger,Kornelius Zeth,Markus Zweckstetter +9 more
TL;DR: The 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography, is presented, showing a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore.
Journal ArticleDOI
Crystal structure of human β2‐glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome
Robert Schwarzenbacher,Kornelius Zeth,Kay Diederichs,Anna Gries,Gerhard M. Kostner,Peter Laggner,Ruth Prassl +6 more
TL;DR: The β2GPI structure reveals potential autoantibody‐binding sites and supports mutagenesis studies where Trp316 and CKNKEKKC have been found to be essential for the phospholipid‐binding capacity of β2 GPI.
Journal ArticleDOI
Substrate recognition by the AAA+ chaperone ClpB.
Christian Schlieker,Jimena Weibezahn,Holger Patzelt,Peter Tessarz,Christine Strub,Kornelius Zeth,Annette H. Erbse,Jens Schneider-Mergener,Jason W. Chin,Peter G. Schultz,Bernd Bukau,Axel Mogk +11 more
TL;DR: This work has identified a substrate-binding site of ClpB that is located at the central pore of the first AAA domain that contributes to substrate binding and its crucial role was confirmed by mutational analysis and direct crosslinking to substrates.
Journal ArticleDOI
AAA+ proteins and substrate recognition, it all depends on their partner in crime
TL;DR: The AAA+ superfamily has been identified in all organisms studied to date as mentioned in this paper, and members of this superfamily are involved in functions as diverse as transcription and protein degradation and play an important role in the protein quality control network.