Control of amyloid formation via beta-hairpin molecular recognition features

Publications

Peer reviewed articles (20)

β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation

Author(s): Emil Dandanell Agerschou, Marie P Schützmann, Nikolas Reppert, Michael M Wördehoff, Hamed Shaykhalishahi, Alexander K Buell, Wolfgang Hoyer
Published in: Biophysical Chemistry, 269, 2021, Page(s) 106519, ISSN 0301-4622
Publisher: Elsevier BV
DOI: 10.1016/j.bpc.2020.106519

A β-Wrapin Targeting the N-Terminus of α-Synuclein Monomers Reduces Fibril-Induced Aggregation in Neurons

Author(s): Éva M Szegő, Fabian Boß, Daniel Komnig, Charlott Gärtner, Lennart Höfs, Hamed Shaykhalishahi, Michael M Wördehoff, Theodora Saridaki, Jörg B Schulz, Wolfgang Hoyer, Björn H Falkenburger
Published in: Frontiers in Neuroscience, 15, 2021, Page(s) 696440, ISSN 1662-453X
Publisher: Frontiers Media
DOI: 10.3389/fnins.2021.696440

Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein

Author(s): Emil Dandanell Agerschou, Vera Borgmann, Michael M Wördehoff, Wolfgang Hoyer
Published in: Chemical Science, 11(41), 2020, Page(s) 11331-11337, ISSN 2041-6539
Publisher: Royal Society of Chemistry
DOI: 10.1039/d0sc04051g

Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy

Author(s): Anna S König, Nadine S Rösener, Lothar Gremer, Markus Tusche, Daniel Flender, Elke Reinartz, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold, Henrike Heise
Published in: Journal of Biological Chemistry, 296, 2021, Page(s) 100499, ISSN 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology Inc.
DOI: 10.1016/j.jbc.2021.100499

Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins

Author(s): Asuka A. Orr, Hamed Shaykhalishahi, Ewa A. Mirecka, Sai Vamshi R. Jonnalagadda, Wolfgang Hoyer, Phanourios Tamamis
Published in: Computers & Chemical Engineering, 116, 2018, Page(s) 322-332, ISSN 0098-1354
Publisher: Pergamon Press Ltd.
DOI: 10.1016/j.compchemeng.2018.02.013

A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein

Author(s): Nadine S. Rösener, Lothar Gremer, Elke Reinartz, Anna König, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
Published in: Journal of Biological Chemistry, 293/41, 2018, Page(s) 15748-15764, ISSN 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology Inc.
DOI: 10.1074/jbc.RA118.003116

Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth

Author(s): Michael M. Wördehoff, Hamed Shaykhalishahi, Luca Groß, Lothar Gremer, Matthias Stoldt, Alexander K. Buell, Dieter Willbold, Wolfgang Hoyer
Published in: Journal of Molecular Biology, 429/20, 2017, Page(s) 3018-3030, ISSN 0022-2836
Publisher: Academic Press
DOI: 10.1016/j.jmb.2017.09.005

Origin of metastable oligomers and their effects on amyloid fibril self-assembly

Author(s): Filip Hasecke, Tatiana Miti, Carlos Perez, Jeremy Barton, Daniel Schölzel, Lothar Gremer, Clara S. R. Grüning, Garrett Matthews, Georg Meisl, Tuomas P. J. Knowles, Dieter Willbold, Philipp Neudecker, Henrike Heise, Ghanim Ullah, Wolfgang Hoyer, Martin Muschol
Published in: Chemical Science, 9/27, 2018, Page(s) 5937-5948, ISSN 2041-6520
Publisher: Royal Society of Chemistry
DOI: 10.1039/c8sc01479e

α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay

Author(s): Michael Wördehoff, Wolfgang Hoyer
Published in: BIO-PROTOCOL, 8/14, 2018, ISSN 2331-8325
Publisher: Bio-protocol LLC
DOI: 10.21769/BioProtoc.2941

DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α -Synuclein in Different States

Author(s): Boran Uluca, Thibault Viennet, Dušan Petrović, Hamed Shaykhalishahi, Franziska Weirich, Ayşenur Gönülalan, Birgit Strodel, Manuel Etzkorn, Wolfgang Hoyer, Henrike Heise
Published in: Biophysical Journal, 114/7, 2018, Page(s) 1614-1623, ISSN 0006-3495
Publisher: Biophysical Society
DOI: 10.1016/j.bpj.2018.02.011

Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Author(s): Lothar Gremer, Daniel Schölzel, Carla Schenk, Elke Reinartz, Jörg Labahn, Raimond B. G. Ravelli, Markus Tusche, Carmen Lopez-Iglesias, Wolfgang Hoyer, Henrike Heise, Dieter Willbold, Gunnar F. Schröder
Published in: Science, 358/6359, 2017, Page(s) 116-119, ISSN 0036-8075
Publisher: American Association for the Advancement of Science
DOI: 10.1126/science.aao2825

Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation

Author(s): Thibault Viennet, Michael M. Wördehoff, Boran Uluca, Chetan Poojari, Hamed Shaykhalishahi, Dieter Willbold, Birgit Strodel, Henrike Heise, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Published in: Communications Biology, 1/1, 2018, ISSN 2399-3642
Publisher: Nature Publishing Group
DOI: 10.1038/s42003-018-0049-z

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils

Author(s): Emil Dandanell Agerschou, Patrick Flagmeier, Theodora Saridaki, Céline Galvagnion, Daniel Komnig, Laetitia Heid, Vibha Prasad, Hamed Shaykhalishahi, Dieter Willbold, Christopher M Dobson, Aaron Voigt, Bjoern Falkenburger, Wolfgang Hoyer, Alexander K Buell
Published in: eLife, 8, 2019, ISSN 2050-084X
Publisher: eLife Sciences Publications
DOI: 10.7554/elife.46112

α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation

Author(s): Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar F. Schröder, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Published in: Chemistry and Physics of Lipids, 220, 2019, Page(s) 57-65, ISSN 0009-3084
Publisher: Elsevier BV
DOI: 10.1016/j.chemphyslip.2019.02.009

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

Author(s): Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder
Published in: Nature Communications, 10/1, 2019, ISSN 2041-1723
Publisher: Nature Publishing Group
DOI: 10.1038/s41467-019-11320-8

Mechanism of Fibril and Soluble Oligomer Formation in Amyloid Beta and Hen Egg White Lysozyme Proteins

Author(s): Carlos Perez, Tatiana Miti, Filip Hasecke, Georg Meisl, Wolfgang Hoyer, Martin Muschol, Ghanim Ullah
Published in: The Journal of Physical Chemistry B, 123/27, 2019, Page(s) 5678-5689, ISSN 1520-6106
Publisher: American Chemical Society
DOI: 10.1021/acs.jpcb.9b02338

Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

Author(s): Christine Röder, Tatsiana Kupreichyk, Lothar Gremer, Luisa U. Schäfer, Karunakar R. Pothula, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Gunnar F. Schröder
Published in: Nature Structural & Molecular Biology, 27/7, 2020, Page(s) 660-667, ISSN 1545-9993
Publisher: Nature Publishing Group
DOI: 10.1038/s41594-020-0442-4

Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus

Author(s): Nadine S. Rösener, Lothar Gremer, Michael M. Wördehoff, Tatsiana Kupreichyk, Manuel Etzkorn, Philipp Neudecker, Wolfgang Hoyer
Published in: Communications Biology, 3/1, 2020, ISSN 2399-3642
Publisher: Nature Research
DOI: 10.1038/s42003-020-1085-z

Protofibril–Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation

Author(s): Filip Hasecke, Chamani Niyangoda, Gustavo Borjas, Jianjun Pan, Garrett Matthews, Martin Muschol, Wolfgang Hoyer
Published in: Angewandte Chemie International Edition, 60(6), 2021, Page(s) 3016-3021, ISSN 1433-7851
Publisher: John Wiley & Sons Ltd.
DOI: 10.1002/anie.202010098

Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting

Author(s): Marie P Schützmann, Filip Hasecke, Sarah Bachmann, Mara Zielinski, Sebastian Hänsch, Gunnar F Schröder, Hans Zempel, Wolfgang Hoyer
Published in: Nature Communications, 12(1), 2021, Page(s) 4634, ISSN 2041-1723
Publisher: Nature Publishing Group
DOI: 10.1038/s41467-021-24900-4