Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage

Structure of AqpZ tetramer and location of mutations. The

Molecular dynamics simulations reveal the importance of amyloid

알츠하이머병 - AD 뇌의 신경세포 막에서 Aβ가 만드는 pore로 인해

Frontiers High Speed AFM and NanoInfrared Spectroscopy

The amyloid concentric β-barrel hypothesis: Models of amyloid beta

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ

Aβ(1-42) tetramer and octamer structures reveal edge conductivity

A β-barrel-like tetramer formed by a β-hairpin derived from Aβ

Flanking regions, amyloid cores, and polymorphism: the potential

βPFOAβ(1-42) samples can be enriched in either tetramers or

PDF] Alzheimer´s Disease-associated Aβ42 Peptide: Expression and

Frontiers Cholesterol as a key player in amyloid β-mediated

LinkedIn CovalX 페이지: Aβ(1-42) tetramer and octamer structures

Simulation model of Aβ42 pore-forming oligomers with the 6RHY fold

Journal of Cellular Biochemistry