Control of amyloid formation via beta-hairpin molecular recognition features

Información del proyecto

BETACONTROL

Identificador del acuerdo de subvención: 726368

DOI

10.3030/726368

Proyecto cerrado

Fecha de la firma de la CE 16 Mayo 2017

Fecha de inicio 1 Junio 2017

Fecha de finalización 28 Febrero 2023

Financiado con arreglo a

• EXCELLENT SCIENCE - European Research Council (ERC)

Coste total

€ 1 920 697,00

Aportación de la UE

€ 1 920 697,00

Coordinado por

HEINRICH-HEINE-UNIVERSITAET DUESSELDORF
Germany

CORDIS proporciona enlaces a los documentos públicos y las publicaciones de los proyectos de los programas marco HORIZONTE.

Los enlaces a los documentos y las publicaciones de los proyectos del Séptimo Programa Marco, así como los enlaces a algunos tipos de resultados específicos, como conjuntos de datos y «software», se obtienen dinámicamente de OpenAIRE .

Publicaciones

Peer reviewed articles (23)

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

Autores: 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
Publicado en: Biomolecules, Edición 12(3), 2022, Página(s) 469, ISSN 2218-273X
Editor: 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

Autores: Emil Dandanell Agerschou, Marie P Schützmann, Nikolas Reppert, Michael M Wördehoff, Hamed Shaykhalishahi, Alexander K Buell, Wolfgang Hoyer
Publicado en: Biophysical Chemistry, Edición 269, 2021, Página(s) 106519, ISSN 0301-4622
Editor: 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

Autores: 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
Publicado en: Frontiers in Neuroscience, Edición 15, 2021, Página(s) 696440, ISSN 1662-453X
Editor: Frontiers Media
DOI: 10.3389/fnins.2021.696440

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

Autores: Emil Dandanell Agerschou, Vera Borgmann, Michael M Wördehoff, Wolfgang Hoyer
Publicado en: Chemical Science, Edición 11(41), 2020, Página(s) 11331-11337, ISSN 2041-6539
Editor: 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

Autores: Anna S König, Nadine S Rösener, Lothar Gremer, Markus Tusche, Daniel Flender, Elke Reinartz, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold, Henrike Heise
Publicado en: Journal of Biological Chemistry, Edición 296, 2021, Página(s) 100499, ISSN 0021-9258
Editor: 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

Autores: Asuka A. Orr, Hamed Shaykhalishahi, Ewa A. Mirecka, Sai Vamshi R. Jonnalagadda, Wolfgang Hoyer, Phanourios Tamamis
Publicado en: Computers & Chemical Engineering, Edición 116, 2018, Página(s) 322-332, ISSN 0098-1354
Editor: 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

Autores: Nadine S. Rösener, Lothar Gremer, Elke Reinartz, Anna König, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
Publicado en: Journal of Biological Chemistry, Edición 293/41, 2018, Página(s) 15748-15764, ISSN 0021-9258
Editor: 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

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

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

Autores: 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
Publicado en: Chemical Science, Edición 9/27, 2018, Página(s) 5937-5948, ISSN 2041-6520
Editor: Royal Society of Chemistry
DOI: 10.1039/c8sc01479e

α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay

Autores: Michael Wördehoff, Wolfgang Hoyer
Publicado en: BIO-PROTOCOL, Edición 8/14, 2018, ISSN 2331-8325
Editor: Bio-protocol LLC
DOI: 10.21769/BioProtoc.2941

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

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

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

Autores: 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
Publicado en: Science, Edición 358/6359, 2017, Página(s) 116-119, ISSN 0036-8075
Editor: 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

Autores: Thibault Viennet, Michael M. Wördehoff, Boran Uluca, Chetan Poojari, Hamed Shaykhalishahi, Dieter Willbold, Birgit Strodel, Henrike Heise, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Publicado en: Communications Biology, Edición 1/1, 2018, ISSN 2399-3642
Editor: 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

Autores: 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
Publicado en: eLife, Edición 8, 2019, ISSN 2050-084X
Editor: eLife Sciences Publications
DOI: 10.7554/elife.46112

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

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

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

Autores: Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder
Publicado en: Nature Communications, Edición 10/1, 2019, ISSN 2041-1723
Editor: 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

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

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

Autores: Christine Röder, Tatsiana Kupreichyk, Lothar Gremer, Luisa U. Schäfer, Karunakar R. Pothula, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Gunnar F. Schröder
Publicado en: Nature Structural & Molecular Biology, Edición 27/7, 2020, Página(s) 660-667, ISSN 1545-9993
Editor: 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

Autores: Nadine S. Rösener, Lothar Gremer, Michael M. Wördehoff, Tatsiana Kupreichyk, Manuel Etzkorn, Philipp Neudecker, Wolfgang Hoyer
Publicado en: Communications Biology, Edición 3/1, 2020, ISSN 2399-3642
Editor: Nature Research
DOI: 10.1038/s42003-020-1085-z

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

Autores: Ricarda Törner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer, Jerome Boisbouvier
Publicado en: Nature Communications, Edición 13(1), 2022, Página(s) 2363, ISSN 2041-1723
Editor: Nature Publishing Group
DOI: 10.1038/s41467-022-30042-y

The role of heat shock proteins in preventing amyloid toxicity

Autores: Ricarda Törner, Tatsiana Kupreichyk, Wolfgang Hoyer, Jerome Boisbouvier
Publicado en: Frontiers in Molecular Biosciences, Edición 9, 2022, Página(s) 1045616, ISSN 2296-889X
Editor: Frontiers
DOI: 10.3389/fmolb.2022.1045616

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

Autores: Filip Hasecke, Chamani Niyangoda, Gustavo Borjas, Jianjun Pan, Garrett Matthews, Martin Muschol, Wolfgang Hoyer
Publicado en: Angewandte Chemie International Edition, Edición 60(6), 2021, Página(s) 3016-3021, ISSN 1433-7851
Editor: 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

Autores: Marie P Schützmann, Filip Hasecke, Sarah Bachmann, Mara Zielinski, Sebastian Hänsch, Gunnar F Schröder, Hans Zempel, Wolfgang Hoyer
Publicado en: Nature Communications, Edición 12(1), 2021, Página(s) 4634, ISSN 2041-1723
Editor: Nature Publishing Group
DOI: 10.1038/s41467-021-24900-4