Alexey G. Murzin

This study shows that chaperones shape the structural evolution of yeast prion amyloids during maturation, with Hsp104 inhibiting structural diversity.

This study reports cryo-EM structures of tau filaments from MAPT mutants, showing how specific mutations alter the Pick fold structure and enable reconstitution of variants.

The paper reports the structures of α-synuclein filaments from individuals with Parkinson's disease and dementia, revealing differences in dimerisation and twist reversal between pathogenic and non-pathogenic variants.

This study identifies distinct TAF15 amyloid filament structures in different FTLD-FET subtypes, leading to the renaming of the disease group as FTLD-TAF15.

The paper reports cryo-EM structures of tau filaments from individuals with P301L and P301T MAPT mutations, revealing distinct filament folds associated with FTDP-17.

The paper determines the structures of tau filaments in individuals with MAPT mutations V337M and R406W using cryo-EM, finding the Alzheimer fold in all cases and a new triple filament assembly.

This study identifies heteromeric amyloid filaments composed of ANXA11 and TDP-43 in FTLD-TDP Type C using cryo-EM, revealing a new pathological mechanism.

The paper determines cryo-EM structures of Aβ40 filaments from Alzheimer's and cerebral amyloid angiopathy samples, revealing structural differences at higher resolution.

The paper determines cryo-EM structures of Tau filaments from transgenic mice models and identifies differences compared to human Tau filaments.

This study uses cryo-EM to show that tau filaments in ALS/PDC share the CTE fold, suggesting environmental causes for the disease.

The paper reports cryo-EM structures of amyloid-beta filaments with the Arctic mutation from human and mouse brains, revealing structural differences and conformational changes.

The paper identifies a SNCA mutation causing juvenile-onset synucleinopathy and describes the structural features of α-synuclein filaments associated with the disease.

The paper reports cryo-EM structures of α-synuclein filaments from Parkinson's disease, PD dementia, and dementia with Lewy bodies, showing they are composed of a single protofilament distinct from those in multiple system atrophy.

This study identifies age-dependent formation of TMEM106B amyloid filaments in human brains using cryo-EM, showing they appear in older individuals but not younger ones.

This study reports in vitro assembly of recombinant tau into filaments structurally similar to those in Alzheimer's disease and chronic traumatic encephalopathy using cryo-EM.

Cryo-EM shows brain-derived Aβ42 filaments adopt two related S-shaped protofilament folds: Type I dominates sporadic Alzheimer's, Type II familial Alzheimer's, other disorders and App^NL-F knock-in mice.

Cryo-EM structures sort four-repeat tauopathies into three-layered (PSP, GGT, LNT) and four-layered (CBD, AGD, ARTAG, MAPT intron 10 mutations) tau folds, grounding a hierarchical structure-based classification.

This study determines the structure of α-synuclein filaments in multiple system atrophy using cryo-EM, revealing distinct filament types and conformers that differ from in vitro assemblies.

This paper reports the structure of tau filaments in corticobasal degeneration using cryo-EM, revealing a novel four-layered fold distinct from other tauopathies.

The paper determines the structure of tau filaments in Alzheimer's disease cases and finds they adopt a common fold across individuals.