S
Sven O. Dahms
Researcher at Leibniz Association
Publications - 22
Citations - 750
Sven O. Dahms is an academic researcher from Leibniz Association. The author has contributed to research in topics: Amyloid precursor protein & Furin. The author has an hindex of 15, co-authored 20 publications receiving 653 citations. Previous affiliations of Sven O. Dahms include University of Salzburg & National Institutes of Health.
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Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein
TL;DR: The APP-based signal transduction, cell–cell- and/or cell–ECM interaction should depend on dimerization induced by heparin, as well as on pH, arguing that APP could fulfill different functions depending on its (sub)cellular localization.
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Metal binding dictates conformation and function of the amyloid precursor protein (APP) E2 domain
Sven O. Dahms,Ina Könnig,Dirk Roeser,Karl-Heinz Gührs,Magnus C. Mayer,Daniela Kaden,Gerd Multhaup,Manuel E. Than +7 more
TL;DR: A novel high-affinity binding site within the E2 domain that binds competitively to copper and zinc at physiological concentrations is characterized, most likely regulating the physiological function of APP and its processing in Alzheimer's disease.
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X-ray Structures of Human Furin in Complex with Competitive Inhibitors.
Sven O. Dahms,Kornelia Hardes,Gero L. Becker,Torsten Steinmetzer,Hans Brandstetter,Manuel E. Than +5 more
TL;DR: This work presents a novel preparation of human furin and the first crystal structures of this enzyme in complex with noncovalent inhibitors, and shows the inhibitor exchange by soaking, allowing the investigation of additional inhibitors and substrate analogues.
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Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism
TL;DR: Several structural states of the protein furin are described by X-ray crystallography and further characterize them by molecular dynamics simulations, suggesting essential elements underlying its unusually high substrate specificity.
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Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans
Izabela Sabala,Elżbieta Jagielska,Philip Bardelang,Honorata Czapinska,Sven O. Dahms,J.A. Sharpe,Richard James,Manuel E. Than,Neil R. Thomas,Matthias Bochtler,Matthias Bochtler +10 more
TL;DR: The first crystal structure of mature lysostaphin is reported and the structure of the mature active enzyme confirms its expected organization into catalytic and cell‐wall‐targeting domains and indicates that the domains are mobile with respect to each other because of the presence of a highly flexible peptide linker.