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Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)

Alzheimer’s plaques contain a high amount of Aβ fibrils and a high concentration of lipids. The authors determined structures of Aβ40 fibrils grown in the presence of lipids, revealing high-resolution details of potentially disease-relevant fibril-lipid interactions.

Benedikt Frieg
Mookyoung Han
Gunnar F. Schröder
ResearchOpen Access13 Feb 2024
Nature Communications

Volume: 15, P: 1-11
Cryo-EM of Aβ fibrils from mouse models find tg-APP_ArcSwe fibrils resemble those found in patients with sporadic Alzheimer’s disease

This study by Zielinski et al. used cryo-EM to compare Aβ fibril structures from mouse models to those from patients with Alzheimer’s disease. It revealed that tg-APP_ArcSwe mice exhibit fibrils resembling those predominantly found in sporadic Alzheimer’s disease cases.

Mara Zielinski
Fernanda S. Peralta Reyes
Gunnar F. Schröder
ResearchOpen Access16 Nov 2023
Nature Neuroscience

Volume: 26, P: 2073-2080
The 3D structure of lipidic fibrils of α-synuclein

Interactions between α-synuclein fibrils and lipids have been associated with the development of Parkinson’s disease. This cryo-EM study reveals structural details of these interactions and suggests a mechanism for fibril-induced lipid extraction.

Benedikt Frieg
Leif Antonschmidt
Gunnar F. Schröder
ResearchOpen Access10 Nov 2022
Nature Communications

Volume: 13, P: 1-10
Molecular interactions of FG nucleoporin repeats at high resolution

Proteins rich in phenylalanine-glycine (FG) repeats can phase separate through FG–FG interactions. The molecular interactions of an important FG-repeat protein, nucleoporin 98, have now been studied in liquid-like transient and amyloid-like cohesive states. These interactions underlie the behaviour of FG-repeat proteins and their function in physiological and pathological cell activities.

Alain Ibáñez de Opakua
James A. Geraets
Markus Zweckstetter
ResearchOpen Access22 Sept 2022
Nature Chemistry

Volume: 14, P: 1278-1285
The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils

Understanding how small molecules bind to pathological aggregates is of importance for therapeutic and diagnostic development in diseases such as Parkinson’s Disease. Here, the authors reveal a binding site of anle138b to lipid-induced α-synuclein fibrils.

Leif Antonschmidt
Dirk Matthes
Loren B. Andreas
ResearchOpen Access14 Sept 2022
Nature Communications

Volume: 13, P: 1-10
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Quaternary structure of α-synuclein fibrils characterized from human patients with Parkinson’s disease and Multiple System Atrophy modulates seeding in mouse primary oligodendroglial cultures.

Benedikt Frieg
James A. Geraets
Gunnar F. Schröder
ResearchOpen Access30 Sept 2022
Communications Biology

Volume: 5, P: 1-10
Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels

Interactions between opposite subunits of HCN channels are relevant for stabilizing the auto-inhibited state of the channel. Like cAMP-binding, K464E-mutation breaks these interactions to favor a channel’s pre-activated state.

Mahesh Kondapuram
Benedikt Frieg
Jana Kusch
ResearchOpen Access09 May 2022
Communications Biology

Volume: 5, P: 1-14
Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae

Sakshi Khosa
Benedikt Frieg
Sander H. J. Smits
ResearchOpen Access04 Jan 2016
Scientific Reports

Volume: 6, P: 1-13
Biophysical and pharmacokinetic characterization of a small-molecule inhibitor of RUNX1/ETO tetramerization with anti-leukemic effects

Mohanraj Gopalswamy
Tobias Kroeger
Holger Gohlke
ResearchOpen Access19 Aug 2022
Scientific Reports

Volume: 12, P: 1-18
Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses

Abhishek Cukkemane
Nina Becker
Oliver H. Weiergräber
ResearchOpen Access17 Dec 2021
Translational Psychiatry

Volume: 11, P: 1-13

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Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)

Cryo-EM of Aβ fibrils from mouse models find tg-APP_ArcSwe fibrils resemble those found in patients with sporadic Alzheimer’s disease

The 3D structure of lipidic fibrils of α-synuclein

Molecular interactions of FG nucleoporin repeats at high resolution

The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels

Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae

Biophysical and pharmacokinetic characterization of a small-molecule inhibitor of RUNX1/ETO tetramerization with anti-leukemic effects

Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses

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