Control of amyloid formation via beta-hairpin molecular recognition features

Project Information

BETACONTROL

Grant agreement ID: 726368

DOI

10.3030/726368

Project closed

EC signature date 16 May 2017

Start date 1 June 2017

End date 28 February 2023

Funded under

• EXCELLENT SCIENCE - European Research Council (ERC)

Total cost

€ 1 920 697,00

EU contribution

€ 1 920 697,00

Coordinated by

HEINRICH-HEINE-UNIVERSITAET DUESSELDORF
Germany

CORDIS provides links to public deliverables and publications of HORIZON projects.

Links to deliverables and publications from FP7 projects, as well as links to some specific result types such as dataset and software, are dynamically retrieved from OpenAIRE .

Publications

Peer reviewed articles (23)

Alpha-Synuclein-Specific Naturally Occurring Antibodies Inhibit Aggregation In Vitro and In Vivo

Author(s): Anne K. Braczynski, Marc Sevenich, Ian Gering, Tatsiana Kupreichyk, Emil D. Agerschou, Yannick Kronimus, Pardes Habib, Matthias Stoldt, Dieter Willbold, Jörg B. Schulz, Jan-Philipp Bach, Björn H. Falkenburger, Wolfgang Hoyer
Published in: Biomolecules, Issue 12(3), 2022, Page(s) 469, ISSN 2218-273X
Publisher: MDPI
DOI: 10.3390/biom12030469

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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 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, Issue 3/1, 2020, ISSN 2399-3642
Publisher: Nature Research
DOI: 10.1038/s42003-020-1085-z

Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin

Author(s): Ricarda Törner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer, Jerome Boisbouvier
Published in: Nature Communications, Issue 13(1), 2022, Page(s) 2363, ISSN 2041-1723
Publisher: Nature Publishing Group
DOI: 10.1038/s41467-022-30042-y

The role of heat shock proteins in preventing amyloid toxicity

Author(s): Ricarda Törner, Tatsiana Kupreichyk, Wolfgang Hoyer, Jerome Boisbouvier
Published in: Frontiers in Molecular Biosciences, Issue 9, 2022, Page(s) 1045616, ISSN 2296-889X
Publisher: Frontiers
DOI: 10.3389/fmolb.2022.1045616

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, Issue 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, Issue 12(1), 2021, Page(s) 4634, ISSN 2041-1723
Publisher: Nature Publishing Group
DOI: 10.1038/s41467-021-24900-4