All Comments by Brigita Urbanc

  1. Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.
  2. Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation.
  3. The Toxic Fold? Aβ Dodecamers, Tetramers Show Their Conformations
  4. Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure.
  5. A molecular dynamics study of the interaction of D-peptide amyloid inhibitors with their target sequence reveals a potential inhibitory pharmacophore conformation.
  6. Low-power laser irradiation inhibiting Abeta25-35-induced PC12 cell apoptosis via PKC activation.
  7. Affibodies—Putting the β in Aβ?
  8. Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity.
  9. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.
  10. Linking folding with aggregation in Alzheimer's beta-amyloid peptides.
  11. Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus.
  12. Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models.
  13. Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
  14. Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides.
  15. Messing with the Membrane—An Alternative Interpretation of the Amyloid-β Hypothesis