A sensitive colorimetric strategy for monitoring cerebral ß-amyloid peptides in AD based on dual-functionalized gold nanoplasmonic particles.
Yu, Yan-yan; Zhang, Lin; Sun, Xiao-yu; Li, Cheng-lin; Qiu, Yu; Sun, Hao-peng; Tang, Dao-quan; Liu, Yao-wu; Yin, Xiao-xing.
Chem Commun (Camb)
; 51(42): 8880-3, 2015 May 25.
Artigo em Inglês | MEDLINE | ID: mdl-25925958
Molecular structure of ß-amyloid fibrils in Alzheimer's disease brain tissue.
Structural heterogeneity and intersubject variability of Aß in familial and sporadic Alzheimer's disease.
Towards an understanding of amyloid-ß oligomers: characterization, toxicity mechanisms, and inhibitors.
Aß propagation and strains: Implications for the phenotypic diversity in Alzheimer's disease.
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On the role of sidechain size and charge in the aggregation of A42 with familial mutations.
TREM2 lipid sensing sustains the microglial response in an Alzheimer's disease model.
Amyloid-ß oligomers are sequestered by both intracellular and extracellular chaperones.
Systematic development of small molecules to inhibit specific microscopic steps of Aß42 aggregation in Alzheimer's disease.
Distinct role of hydration water in protein misfolding and aggregation revealed by fluctuating thermodynamics analysis.