Control of amyloid formation via beta-hairpin molecular recognition features

Publikacje

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

Autorzy: 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
Opublikowane w: Biomolecules, Numer 12(3), 2022, Strona(/y) 469, ISSN 2218-273X
Wydawca: 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

Autorzy: Emil Dandanell Agerschou, Marie P Schützmann, Nikolas Reppert, Michael M Wördehoff, Hamed Shaykhalishahi, Alexander K Buell, Wolfgang Hoyer
Opublikowane w: Biophysical Chemistry, Numer 269, 2021, Strona(/y) 106519, ISSN 0301-4622
Wydawca: 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

Autorzy: 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
Opublikowane w: Frontiers in Neuroscience, Numer 15, 2021, Strona(/y) 696440, ISSN 1662-453X
Wydawca: Frontiers Media
DOI: 10.3389/fnins.2021.696440

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

Autorzy: Emil Dandanell Agerschou, Vera Borgmann, Michael M Wördehoff, Wolfgang Hoyer
Opublikowane w: Chemical Science, Numer 11(41), 2020, Strona(/y) 11331-11337, ISSN 2041-6539
Wydawca: 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

Autorzy: Anna S König, Nadine S Rösener, Lothar Gremer, Markus Tusche, Daniel Flender, Elke Reinartz, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold, Henrike Heise
Opublikowane w: Journal of Biological Chemistry, Numer 296, 2021, Strona(/y) 100499, ISSN 0021-9258
Wydawca: 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

Autorzy: Asuka A. Orr, Hamed Shaykhalishahi, Ewa A. Mirecka, Sai Vamshi R. Jonnalagadda, Wolfgang Hoyer, Phanourios Tamamis
Opublikowane w: Computers & Chemical Engineering, Numer 116, 2018, Strona(/y) 322-332, ISSN 0098-1354
Wydawca: 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

Autorzy: Nadine S. Rösener, Lothar Gremer, Elke Reinartz, Anna König, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
Opublikowane w: Journal of Biological Chemistry, Numer 293/41, 2018, Strona(/y) 15748-15764, ISSN 0021-9258
Wydawca: 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

Autorzy: Michael M. Wördehoff, Hamed Shaykhalishahi, Luca Groß, Lothar Gremer, Matthias Stoldt, Alexander K. Buell, Dieter Willbold, Wolfgang Hoyer
Opublikowane w: Journal of Molecular Biology, Numer 429/20, 2017, Strona(/y) 3018-3030, ISSN 0022-2836
Wydawca: Academic Press
DOI: 10.1016/j.jmb.2017.09.005

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

Autorzy: 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
Opublikowane w: Chemical Science, Numer 9/27, 2018, Strona(/y) 5937-5948, ISSN 2041-6520
Wydawca: Royal Society of Chemistry
DOI: 10.1039/c8sc01479e

α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay

Autorzy: Michael Wördehoff, Wolfgang Hoyer
Opublikowane w: BIO-PROTOCOL, Numer 8/14, 2018, ISSN 2331-8325
Wydawca: Bio-protocol LLC
DOI: 10.21769/BioProtoc.2941

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

Autorzy: Boran Uluca, Thibault Viennet, Dušan Petrović, Hamed Shaykhalishahi, Franziska Weirich, Ayşenur Gönülalan, Birgit Strodel, Manuel Etzkorn, Wolfgang Hoyer, Henrike Heise
Opublikowane w: Biophysical Journal, Numer 114/7, 2018, Strona(/y) 1614-1623, ISSN 0006-3495
Wydawca: Biophysical Society
DOI: 10.1016/j.bpj.2018.02.011

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

Autorzy: 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
Opublikowane w: Science, Numer 358/6359, 2017, Strona(/y) 116-119, ISSN 0036-8075
Wydawca: 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

Autorzy: Thibault Viennet, Michael M. Wördehoff, Boran Uluca, Chetan Poojari, Hamed Shaykhalishahi, Dieter Willbold, Birgit Strodel, Henrike Heise, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Opublikowane w: Communications Biology, Numer 1/1, 2018, ISSN 2399-3642
Wydawca: 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

Autorzy: 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
Opublikowane w: eLife, Numer 8, 2019, ISSN 2050-084X
Wydawca: eLife Sciences Publications
DOI: 10.7554/elife.46112

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

Autorzy: Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar F. Schröder, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Opublikowane w: Chemistry and Physics of Lipids, Numer 220, 2019, Strona(/y) 57-65, ISSN 0009-3084
Wydawca: Elsevier BV
DOI: 10.1016/j.chemphyslip.2019.02.009

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

Autorzy: Christine Röder, Nicola Vettore, Lena N. Mangels, Lothar Gremer, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Alexander K. Buell, Gunnar F. Schröder
Opublikowane w: Nature Communications, Numer 10/1, 2019, ISSN 2041-1723
Wydawca: 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

Autorzy: Carlos Perez, Tatiana Miti, Filip Hasecke, Georg Meisl, Wolfgang Hoyer, Martin Muschol, Ghanim Ullah
Opublikowane w: The Journal of Physical Chemistry B, Numer 123/27, 2019, Strona(/y) 5678-5689, ISSN 1520-6106
Wydawca: American Chemical Society
DOI: 10.1021/acs.jpcb.9b02338

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

Autorzy: Christine Röder, Tatsiana Kupreichyk, Lothar Gremer, Luisa U. Schäfer, Karunakar R. Pothula, Raimond B. G. Ravelli, Dieter Willbold, Wolfgang Hoyer, Gunnar F. Schröder
Opublikowane w: Nature Structural & Molecular Biology, Numer 27/7, 2020, Strona(/y) 660-667, ISSN 1545-9993
Wydawca: 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

Autorzy: Nadine S. Rösener, Lothar Gremer, Michael M. Wördehoff, Tatsiana Kupreichyk, Manuel Etzkorn, Philipp Neudecker, Wolfgang Hoyer
Opublikowane w: Communications Biology, Numer 3/1, 2020, ISSN 2399-3642
Wydawca: Nature Research
DOI: 10.1038/s42003-020-1085-z

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

Autorzy: Ricarda Törner, Tatsiana Kupreichyk, Lothar Gremer, Elisa Colas Debled, Daphna Fenel, Sarah Schemmert, Pierre Gans, Dieter Willbold, Guy Schoehn, Wolfgang Hoyer, Jerome Boisbouvier
Opublikowane w: Nature Communications, Numer 13(1), 2022, Strona(/y) 2363, ISSN 2041-1723
Wydawca: Nature Publishing Group
DOI: 10.1038/s41467-022-30042-y

The role of heat shock proteins in preventing amyloid toxicity

Autorzy: Ricarda Törner, Tatsiana Kupreichyk, Wolfgang Hoyer, Jerome Boisbouvier
Opublikowane w: Frontiers in Molecular Biosciences, Numer 9, 2022, Strona(/y) 1045616, ISSN 2296-889X
Wydawca: Frontiers
DOI: 10.3389/fmolb.2022.1045616

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

Autorzy: Filip Hasecke, Chamani Niyangoda, Gustavo Borjas, Jianjun Pan, Garrett Matthews, Martin Muschol, Wolfgang Hoyer
Opublikowane w: Angewandte Chemie International Edition, Numer 60(6), 2021, Strona(/y) 3016-3021, ISSN 1433-7851
Wydawca: 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

Autorzy: Marie P Schützmann, Filip Hasecke, Sarah Bachmann, Mara Zielinski, Sebastian Hänsch, Gunnar F Schröder, Hans Zempel, Wolfgang Hoyer
Opublikowane w: Nature Communications, Numer 12(1), 2021, Strona(/y) 4634, ISSN 2041-1723
Wydawca: Nature Publishing Group
DOI: 10.1038/s41467-021-24900-4

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