All Stories

  1. P4‐213: REDUCTION OF β‐AMYLOID AND PHOSPHO‐TAU IN TRANSGENIC MICE BY A NOVEL FUSION PROTEIN BIVALENT FOR A GENERAL AMYLOID INTERACTION MOTIF (GAIM)
  2. P2‐067: IMMUNOGLOBULIN‐GENERAL AMYLOID INTERACTION MOTIF (IG‐GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO
  3. A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies
  4. P2–050: A novel mechanism that targets misfolded protein assemblies
  5. P4–290: Novel fusion protein bivalent for a general amyloid interaction motif reduces beta‐amyloid aggregates in transgenic mice
  6. Conserved features of intermediates in amyloid assembly determine their benign or toxic states
  7. P4‐412: NPT001: A candidate therapeutic for clearance of beta‐amyloid and tau aggregates in Alzheimer's disease
  8. P2‐456: NPT001: A candidate therapeutic for clearance of β‐amyloid and tau aggregates in Alzheimer's disease
  9. Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins
  10. The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication
  11. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
  12. Structural insights into a yeast prion illuminate nucleation and strain diversity
  13. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on thede novoformation of the [PSI+] prion in yeast and aggregation of Sup35in vitro
  14. Interaction of human recombinant αA‐ and αB‐crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation
  15. Structural perturbation of α-crystallin and its chaperone-like activity
  16. Molten-Globule State of Carbonic Anhydrase Binds to the Chaperone-like  -Crystallin