
Cryo-EM structures of amyloid-β 42 filaments from human brains ...
2022年1月18日 · LCOs and cryo-EM do not similarly assess the structural features of polymerized Aβ. LCOs (particularly when used in combinations) largely show the arrangement and packing of Aβ-amyloid fibrils; the readout varies with the different Aβ40/42 ratios, and it also is sensitive to age-related changes in the aggregates ( Nyström et al., 2013 ).
Cryo-EM Unveils Distinct Aβ42 Fibril Structures for ... - ALZFORUM
2022年1月14日 · Cryo-EM of Aβ42 fibrils from 10 brains revealed two predominant filament structures. Type I and type II filaments comprised distinct, S-shaped protofilaments. Type I filaments predominated in sporadic AD; type II was found in familial AD, related diseases, and in APP knock-in mice.
Pretty in PINK1, Cryo-EM Reveals How Kinase Anchors to …
2025年3月14日 · This new cryo-EM structure represents a remarkable advance in our understanding of how human PINK1 is stabilized at the TOM complex, and Komander and his team deserve high praise for this work. Consistent with recent biochemical studies, including from our lab, the structure explains how TOM20 stabilizes PINK1 at the complex.
Cryo-EM Resolves Two Aβ40 Fibril Structures Amplified from
2023年1月20日 · Later, researchers led by Michel Goedert and Sjors Scheres of the MRC Laboratory of Molecular Biology, Cambridge, England, U.K., used cryo-EM to solve the structure of Aβ42 fibrils extracted from the brain parenchyma of people with AD (Jan 2022 news). That study identified two filament structures comprising distinct S-shaped protofilament cores.
Better than Crystal Clear? Cryo-EM Achieves Atomic Resolution
2020年10月23日 · Single-particle cryo-EM at atomic resolution. Nature. 2020 Oct 21; PubMed. Herzik MA Jr. Cryo-electron microscopy reaches atomic resolution. Nature. 2020 Oct 21; PubMed. Zhang K, Pintilie GD, Li S, Schmid MF, Chiu W. Resolving Individual-Atom of Protein Complex using Commonly Available 300-kV Cryo-electron Microscopes. bioRxiv. August 19, 2020.
Catch and Release: Cryo-EM Reveals How LRP2 Receptor
2023年2月10日 · Suspecting that changes in pH could drive the switch, first author Andrew Beenken and colleagues used cryo-EM to solve and compare the structures of LRP2 isolated from mouse kidney samples at a relatively neutral extracellular pH of 7.5, or an acidic endosomal pH of 5.2. Both structures emerged as homodimers with twofold symmetry. Open and Shut ...
Cryo-EM structures of tau filaments from Alzheimer's disease
2017年7月10日 · I am quite excited to see future cryo-EM-derived structures of tau fibrils obtained from postmortem tissues from patients with distinct tauopathies. Based on previous work from the Goedert, Lee/Trojanowski, and Diamond labs, it seems highly likely that distinct structures (or prion strains) will be associated with distinct diseases.
Cryo-EM structure of Alzheimer disease tau filaments with
2023年9月28日 · Cryo-EM structures of tau filaments from Alzheimer's disease with PET ligand APN-1607. Acta Neuropathol. 2021 May;141(5):697-708. Epub 2021 Mar 16 PubMed. Correction. Shi Y, Ghetti B, Goedert M, Scheres SH. Cryo-EM Structures of Chronic Traumatic Encephalopathy Tau Filaments with PET Ligand Flortaucipir. J Mol Biol. 2023 Jun 1;435(11):168025.
Molecular mechanism of substrate recognition and cleavage by
2024年6月7日 · Using cryo-EM of γ-secretase bound to APP-C99, Aβ49, Aβ46, and Aβ43, we are presented with the greatest insight yet of the sequential generation of Aβ species. The work confirms the established tripeptide cleavage pathway pattern of Aβ49>46>43>40 at a molecular resolution ( Matsumura et al., 2014 ; Takami et al., 2009 ).
Cryo-EM structures of tau filaments from Alzheimer's disease
2025年3月27日 · Cryo-EM structures of tau filaments from Alzheimer's disease with PET ligand APN-1607. Acta Neuropathol. 2021 May;141(5):697-708. Epub 2021 Mar 16 PubMed. Correction. Recommends. Please login to recommend the paper. Comments. No Available Comments. Make a Comment. To make a comment you must login or register.