α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay

Por Wördehoff, Michael M., Hoyer, Wolfgang
Publicado no Bio Protoc (2018)

Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation

Por Hoyer, Wolfgang, Grönwall, Caroline, Jonsson, Andreas, Ståhl, Stefan, Härd, Torleif
Publicado em 2008

Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR

Por Heise, Henrike, Hoyer, Wolfgang, Becker, Stefan, Andronesi, Ovidiu C., Riedel, Dietmar, Baldus, Marc
Publicado em 2005

Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core

Por Weirich, Franziska, Gremer, Lothar, Mirecka, Ewa A., Schiefer, Stephanie, Hoyer, Wolfgang, Heise, Henrike
Publicado no PLoS One (2016)

Recombinant amyloid beta-peptide production by coexpression with an affibody ligand

Por Macao, Bertil, Hoyer, Wolfgang, Sandberg, Anders, Brorsson, Ann-Christin, Dobson, Christopher M, Härd, Torleif
Publicado em 2008

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

Por Perez, Carlos, Miti, Tatiana, Hasecke, Filip, Meisl, Georg, Hoyer, Wolfgang, Muschol, Martin, Ullah, Ghanim
Publicado no J Phys Chem B (2019)

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

Por Hasecke, Filip, Niyangoda, Chamani, Borjas, Gustavo, Pan, Jianjun, Matthews, Garrett, Muschol, Martin, Hoyer, Wolfgang
Publicado no Angew Chem Int Ed Engl (2020)

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

Por Rösener, Nadine S., Gremer, Lothar, Wördehoff, Michael M., Kupreichyk, Tatsiana, Etzkorn, Manuel, Neudecker, Philipp, Hoyer, Wolfgang
Publicado no Commun Biol (2020)

β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor

Por Mirecka, Ewa A., Feuerstein, Sophie, Gremer, Lothar, Schröder, Gunnar F., Stoldt, Matthias, Willbold, Dieter, Hoyer, Wolfgang
Publicado no Sci Rep (2016)

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

Por Orr, Asuka A., Shaykhalishahi, Hamed, Mirecka, Ewa A., Jonnalagadda, Sai Vamshi R., Hoyer, Wolfgang, Tamamis, Phanourios
Publicado no Comput Chem Eng (2018)

NMR of α-synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation

Por Fernández, Claudio O, Hoyer, Wolfgang, Zweckstetter, Markus, Jares-Erijman, Elizabeth A, Subramaniam, Vinod, Griesinger, Christian, Jovin, Thomas M
Publicado em 2004

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Por Bertoncini, Carlos W., Jung, Young-Sang, Fernandez, Claudio O., Hoyer, Wolfgang, Griesinger, Christian, Jovin, Thomas M., Zweckstetter, Markus
Publicado em 2005

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

Por Wördehoff, Michael M., Shaykhalishahi, Hamed, Groß, Luca, Gremer, Lothar, Stoldt, Matthias, Buell, Alexander K., Willbold, Dieter, Hoyer, Wolfgang
Publicado no J Mol Biol (2017)

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

Por Rösener, Nadine S., Gremer, Lothar, Reinartz, Elke, König, Anna, Brener, Oleksandr, Heise, Henrike, Hoyer, Wolfgang, Neudecker, Philipp, Willbold, Dieter
Publicado no J Biol Chem (2018)

Alternative Conformations of the Tau Repeat Domain in Complex with an Engineered Binding Protein

Por Grüning, Clara S. R., Mirecka, Ewa A., Klein, Antonia N., Mandelkow, Eckhard, Willbold, Dieter, Marino, Stephen F., Stoldt, Matthias, Hoyer, Wolfgang
Publicado em 2014

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

Por Uluca, Boran, Viennet, Thibault, Petrović, Dušan, Shaykhalishahi, Hamed, Weirich, Franziska, Gönülalan, Ayşenur, Strodel, Birgit, Etzkorn, Manuel, Hoyer, Wolfgang, Heise, Henrike
Publicado no Biophys J (2018)

The Off-rate of Monomers Dissociating from Amyloid-β Protofibrils

Por Grüning, Clara S. R., Klinker, Stefan, Wolff, Martin, Schneider, Mario, Toksöz, Küpra, Klein, Antonia N., Nagel-Steger, Luitgard, Willbold, Dieter, Hoyer, Wolfgang
Publicado em 2013

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

Por Falke, Marcel, Victor, Julian, Wördehoff, Michael M., Peduzzo, Alessia, Zhang, Tao, Schröder, Gunnar F., Buell, Alexander K., Hoyer, Wolfgang, Etzkorn, Manuel
Publicado no Chem Phys Lipids (2019)

Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

Por Rasia, Rodolfo M., Bertoncini, Carlos W., Marsh, Derek, Hoyer, Wolfgang, Cherny, Dmitry, Zweckstetter, Markus, Griesinger, Christian, Jovin, Thomas M., Fernández, Claudio O.
Publicado em 2005

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

Por Röder, Christine, Vettore, Nicola, Mangels, Lena N., Gremer, Lothar, Ravelli, Raimond B. G., Willbold, Dieter, Hoyer, Wolfgang, Buell, Alexander K., Schröder, Gunnar F.
Publicado no Nat Commun (2019)