Control of amyloid formation via beta-hairpin molecular recognition features

Informazioni relative al progetto

BETACONTROL

ID dell’accordo di sovvenzione: 726368

DOI

10.3030/726368

Progetto chiuso

Data della firma CE 16 Maggio 2017

Data di avvio 1 Giugno 2017

Data di completamento 28 Febbraio 2023

Finanziato da

• EXCELLENT SCIENCE - European Research Council (ERC)

Costo totale

€ 1 920 697,00

Contributo UE

€ 1 920 697,00

Coordinato da

HEINRICH-HEINE-UNIVERSITAET DUESSELDORF
Germany

CORDIS fornisce collegamenti ai risultati finali pubblici e alle pubblicazioni dei progetti ORIZZONTE.

I link ai risultati e alle pubblicazioni dei progetti del 7° PQ, così come i link ad alcuni tipi di risultati specifici come dataset e software, sono recuperati dinamicamente da .OpenAIRE .

Pubblicazioni

Peer reviewed articles (23)

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

Autori: 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
Pubblicato in: Biomolecules, Numero 12(3), 2022, Pagina/e 469, ISSN 2218-273X
Editore: 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

Autori: Emil Dandanell Agerschou, Marie P Schützmann, Nikolas Reppert, Michael M Wördehoff, Hamed Shaykhalishahi, Alexander K Buell, Wolfgang Hoyer
Pubblicato in: Biophysical Chemistry, Numero 269, 2021, Pagina/e 106519, ISSN 0301-4622
Editore: 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

Autori: 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
Pubblicato in: Frontiers in Neuroscience, Numero 15, 2021, Pagina/e 696440, ISSN 1662-453X
Editore: Frontiers Media
DOI: 10.3389/fnins.2021.696440

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

Autori: Emil Dandanell Agerschou, Vera Borgmann, Michael M Wördehoff, Wolfgang Hoyer
Pubblicato in: Chemical Science, Numero 11(41), 2020, Pagina/e 11331-11337, ISSN 2041-6539
Editore: 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

Autori: Anna S König, Nadine S Rösener, Lothar Gremer, Markus Tusche, Daniel Flender, Elke Reinartz, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold, Henrike Heise
Pubblicato in: Journal of Biological Chemistry, Numero 296, 2021, Pagina/e 100499, ISSN 0021-9258
Editore: 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

Autori: Asuka A. Orr, Hamed Shaykhalishahi, Ewa A. Mirecka, Sai Vamshi R. Jonnalagadda, Wolfgang Hoyer, Phanourios Tamamis
Pubblicato in: Computers & Chemical Engineering, Numero 116, 2018, Pagina/e 322-332, ISSN 0098-1354
Editore: 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

Autori: Nadine S. Rösener, Lothar Gremer, Elke Reinartz, Anna König, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
Pubblicato in: Journal of Biological Chemistry, Numero 293/41, 2018, Pagina/e 15748-15764, ISSN 0021-9258
Editore: 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

Autori: Michael M. Wördehoff, Hamed Shaykhalishahi, Luca Groß, Lothar Gremer, Matthias Stoldt, Alexander K. Buell, Dieter Willbold, Wolfgang Hoyer
Pubblicato in: Journal of Molecular Biology, Numero 429/20, 2017, Pagina/e 3018-3030, ISSN 0022-2836
Editore: Academic Press
DOI: 10.1016/j.jmb.2017.09.005

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

Autori: 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
Pubblicato in: Chemical Science, Numero 9/27, 2018, Pagina/e 5937-5948, ISSN 2041-6520
Editore: Royal Society of Chemistry
DOI: 10.1039/c8sc01479e

α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay

Autori: Michael Wördehoff, Wolfgang Hoyer
Pubblicato in: BIO-PROTOCOL, Numero 8/14, 2018, ISSN 2331-8325
Editore: Bio-protocol LLC
DOI: 10.21769/BioProtoc.2941

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

Autori: Boran Uluca, Thibault Viennet, Dušan Petrović, Hamed Shaykhalishahi, Franziska Weirich, Ayşenur Gönülalan, Birgit Strodel, Manuel Etzkorn, Wolfgang Hoyer, Henrike Heise
Pubblicato in: Biophysical Journal, Numero 114/7, 2018, Pagina/e 1614-1623, ISSN 0006-3495
Editore: Biophysical Society
DOI: 10.1016/j.bpj.2018.02.011

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

Autori: 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
Pubblicato in: Science, Numero 358/6359, 2017, Pagina/e 116-119, ISSN 0036-8075
Editore: 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

Autori: Thibault Viennet, Michael M. Wördehoff, Boran Uluca, Chetan Poojari, Hamed Shaykhalishahi, Dieter Willbold, Birgit Strodel, Henrike Heise, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Pubblicato in: Communications Biology, Numero 1/1, 2018, ISSN 2399-3642
Editore: 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

Autori: 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
Pubblicato in: eLife, Numero 8, 2019, ISSN 2050-084X
Editore: eLife Sciences Publications
DOI: 10.7554/elife.46112

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

Autori: Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar F. Schröder, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Pubblicato in: Chemistry and Physics of Lipids, Numero 220, 2019, Pagina/e 57-65, ISSN 0009-3084
Editore: Elsevier BV
DOI: 10.1016/j.chemphyslip.2019.02.009

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

Autori: Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder
Pubblicato in: Nature Communications, Numero 10/1, 2019, ISSN 2041-1723
Editore: 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

Autori: Carlos Perez, Tatiana Miti, Filip Hasecke, Georg Meisl, Wolfgang Hoyer, Martin Muschol, Ghanim Ullah
Pubblicato in: The Journal of Physical Chemistry B, Numero 123/27, 2019, Pagina/e 5678-5689, ISSN 1520-6106
Editore: American Chemical Society
DOI: 10.1021/acs.jpcb.9b02338

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

Autori: Christine Röder, Tatsiana Kupreichyk, Lothar Gremer, Luisa U. Schäfer, Karunakar R. Pothula, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Gunnar F. Schröder
Pubblicato in: Nature Structural & Molecular Biology, Numero 27/7, 2020, Pagina/e 660-667, ISSN 1545-9993
Editore: 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

Autori: Nadine S. Rösener, Lothar Gremer, Michael M. Wördehoff, Tatsiana Kupreichyk, Manuel Etzkorn, Philipp Neudecker, Wolfgang Hoyer
Pubblicato in: Communications Biology, Numero 3/1, 2020, ISSN 2399-3642
Editore: Nature Research
DOI: 10.1038/s42003-020-1085-z

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

Autori: Ricarda Törner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer, Jerome Boisbouvier
Pubblicato in: Nature Communications, Numero 13(1), 2022, Pagina/e 2363, ISSN 2041-1723
Editore: Nature Publishing Group
DOI: 10.1038/s41467-022-30042-y

The role of heat shock proteins in preventing amyloid toxicity

Autori: Ricarda Törner, Tatsiana Kupreichyk, Wolfgang Hoyer, Jerome Boisbouvier
Pubblicato in: Frontiers in Molecular Biosciences, Numero 9, 2022, Pagina/e 1045616, ISSN 2296-889X
Editore: Frontiers
DOI: 10.3389/fmolb.2022.1045616

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

Autori: Filip Hasecke, Chamani Niyangoda, Gustavo Borjas, Jianjun Pan, Garrett Matthews, Martin Muschol, Wolfgang Hoyer
Pubblicato in: Angewandte Chemie International Edition, Numero 60(6), 2021, Pagina/e 3016-3021, ISSN 1433-7851
Editore: 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

Autori: Marie P Schützmann, Filip Hasecke, Sarah Bachmann, Mara Zielinski, Sebastian Hänsch, Gunnar F Schröder, Hans Zempel, Wolfgang Hoyer
Pubblicato in: Nature Communications, Numero 12(1), 2021, Pagina/e 4634, ISSN 2041-1723
Editore: Nature Publishing Group
DOI: 10.1038/s41467-021-24900-4