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Showing 1–5 of 5 results
Advanced filters: Author: Diana Arseni Clear advanced filters

  • 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.

    • Manuel Schweighauser
    • Diana Arseni
    • Sjors H. W. Scheres
    ResearchOpen Access
    Nature
    Volume: 605, P: 310-314

  • 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.

    • Diana Arseni
    • Takashi Nonaka
    • Benjamin Ryskeldi-Falcon
    ResearchOpen Access
    Nature
    Volume: 634, P: 662-668

  • 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.

    • Stephan Tetter
    • Diana Arseni
    • Benjamin Ryskeldi-Falcon
    ResearchOpen Access
    Nature
    Volume: 625, P: 345-351

  • 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.

    • Diana Arseni
    • Renren Chen
    • Benjamin Ryskeldi-Falcon
    ResearchOpen Access
    Nature
    Volume: 620, P: 898-903

  • 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.

    • Diana Arseni
    • Masato Hasegawa
    • Benjamin Ryskeldi-Falcon
    Research
    Nature
    Volume: 601, P: 139-143