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Schweighauser, Shi, Murzin and colleagues report cryo-EM structures of tau filaments from individuals with P301L or P301T MAPT mutations. P301L tau filaments adopted a distinct three-lobed fold, while P301T filaments had either a variant of the three-lobed fold or a V-shaped fold.

A novel common fold observed in the structures of elongation factor G, DNA gyrase B and ribosomal protein S5 displays a rare topological feature suggesting the high probability of an evolutionary relationship

Qi et al. used cryo-electron microscopy to determine the structures of tau filaments from the brains of individuals with MAPT mutants V337M and R406W, known to give rise to frontotemporal dementias. They showed that the tau filaments adopted the Alzheimer fold.

Using cryo-electron microscopy, heteromeric amyloid filaments composed of TDP-43 and ANXA11 in the brains of patients with frontotemporal lobar degeneration type C are discovered.

Cryogenic electron microscopy structures of amyloid filaments extracted from patient brains reveal that the protein TAF15 forms filaments that characterize certain cases of frontotemporal lobar degeneration.

A time-resolved cryogenic electron microscopy analysis provides structural information on the processes of primary and secondary nucleation of tau amyloid formation, with implications for the development of new therapies.

Cryo-electron microscopy structures and mass spectrometry analyses show that TAR DNA-binding protein 43 (TDP-43) forms amyloid filaments with a distinct fold in type A frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP) compared with TDP-43 filaments in type B FTLD-TDP and amyotrophic lateral sclerosis.

A study using structure determination by cryogenic electron microscopy identifies and characterizes TMEM106B amyloid filaments in human brain, and suggests that their formation is age dependent, with no obvious association with disease.

The authors report on the structures of α-synuclein filaments from the brains of individuals with Parkinson's disease, Parkinson's disease dementia and dementia with Lewy bodies and how they differ from those seen in multiple system atrophy.

Cryo-electron microscopy of aggregated TDP-43 from postmortem brain tissue of individuals who had ALS with FTLD reveals a filament structure with distinct features to other neuropathological protein filaments, such as those of tau and α-synuclein.

Cryo-electron microscopy structures of tau filaments from progressive supranuclear palsy and other tauopathies reveal new filament conformations, and suggest that tauopathies can be classified on several different levels according to their filament folds.

Cryo-electron microscopy reveals the structures of α-synuclein filaments from the brains of individuals with multiple system atrophy.

Cyro-electron microscopy of tau filaments from people with corticobasal degeneration reveals a previously unseen four-layered fold, distinct from the filament structures seen in Alzheimer’s disease, Pick’s disease and chronic traumatic encephalopathy.

High-resolution structures of tau filaments shed light on the ultrastructure of neurofibrillary lesions in Alzheimer’s disease.

The series of four CASP experiments has helped to transform the field of protein structure prediction. The state of the art in protein structure prediction has undoubtedly changed, but has there been progress over the years?

The structures of tau filaments from patients with the neurodegenerative disorder Pick’s disease show that the filament fold is different from that of the tau filaments found in Alzheimer’s disease.

Cryo-electron microscopy structures of tau filaments from the brains of three individuals with chronic traumatic encephalopathy reveal distinct assembled tau conformers, with a novel protofilament fold enclosing hydrophobic molecules.