2010
Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy.

Philipp Neudecker , Markus Tusche , Henrike Heise , Henrike Heise
Journal of Biological Chemistry 296 100499 -100499

1
2021
Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus.

Nadine S. Rösener , Lothar Gremer , Michael M. Wördehoff , Tatsiana Kupreichyk
Communications Biology 3 ( 1) 1 -12

3
2020
A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments.

Wolfgang Hoyer , Kathrin Ramm , Andreas Plückthun
Biophysical Chemistry 96 ( 2) 273 -284

21
2002
What Does Solid‐State NMR Tell Us about Amyloid Structures?

Wolfgang Hoyer , Henrike Heise
Amyloid Fibrils and Prefibrillar Aggregates: Molecular and Biological Properties 39 -61

2
2013
Dependence of α-synuclein aggregate morphology on solution conditions

Wolfgang Hoyer , Thomas Antony , Dmitry Cherny , Gudrun Heim
Journal of Molecular Biology 322 ( 2) 383 -393

373
2002
Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils.

Christine Röder , Tatsiana Kupreichyk , Lothar Gremer , Luisa U. Schäfer
Nature Structural & Molecular Biology 27 ( 7) 660 -667

96
2020
Protofibril-Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation.

Filip Hasecke , Chamani Niyangoda , Gustavo Borjas , Jianjun Pan
Angewandte Chemie 60 ( 6) 3016 -3021

2021
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Lothar Gremer , Daniel Schölzel , Carla Schenk , Elke Reinartz
Science 358 ( 6359) 116 -119

373
2017
Transcriptome-wide analysis uncovers the targets of the RNA-binding protein MSI2 and effects of MSI2's RNA-binding activity on IL-6 signaling.

Sujitha Duggimpudi , Andreas Kloetgen , Sathish Kumar Maney , Philipp C. Münch
Journal of Biological Chemistry 293 ( 40) 15359 -15369

11
2018
A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein

Nadine S. Rösener , Lothar Gremer , Elke Reinartz , Anna König
Journal of Biological Chemistry 293 ( 41) 15748 -15764

11
2018
An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils.

Emil Dandanell Agerschou , Patrick Flagmeier , Theodora Saridaki , Céline Galvagnion
eLife 8

26
2019
Uncovering the Binding and Specificity of β-Wrapins for Amyloid-β and α-Synuclein

Asuka A. Orr , Michael M. Wördehoff , Wolfgang Hoyer , Phanourios Tamamis
Journal of Physical Chemistry B 120 ( 50) 12781 -12794

15
2016
Steuerung der α‐Synuclein‐Aggregation durch Bindung einer β‐Haarnadel

Ewa A. Mirecka , Hamed Shaykhalishahi , Aziz Gauhar , Şerife Akgül
Angewandte Chemie 126 ( 16) 4311 -4314

4
2014
Sensitive Electrochemical Detection of Native and Aggregated α-Synuclein Protein Involved in Parkinson's Disease

Michal Masařík , Agata Stobiecka , René Kizek , František Jelen
Electroanalysis 16 ( 1314) 1172 -1181

72
2004
Origin of metastable oligomers and their effects on amyloid fibril self-assembly

Filip Hasecke , Tatiana Miti , Carlos Perez , Jeremy Barton
Chemical Science 9 ( 27) 5937 -5948

31
2018
A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

Thibault Viennet , Michael M. Wördehoff , Boran Uluca , Chetan Poojari
bioRxiv 173724

2
2017
Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide

Ewa Agnieszka Mirecka , Lothar Gremer , Stephanie Schiefer , Filipp Oesterhelt
Journal of Biotechnology 191 221 -227

15
2014
NMR of α-synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation

Claudio O Fernández , Wolfgang Hoyer , Markus Zweckstetter , Elizabeth A Jares-Erijman
The EMBO Journal 23 ( 10) 2039 -2046

190
2004