The expanding amyloid family: Structure, stability, function, and pathogenesis
The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …
Imaging modes of atomic force microscopy for application in molecular and cell biology
Atomic force microscopy (AFM) is a powerful, multifunctional imaging platform that allows
biological samples, from single molecules to living cells, to be visualized and manipulated …
biological samples, from single molecules to living cells, to be visualized and manipulated …
Disease-specific tau filaments assemble via polymorphic intermediates
Intermediate species in the assembly of amyloid filaments are believed to play a central role
in neurodegenerative diseases and may constitute important targets for therapeutic …
in neurodegenerative diseases and may constitute important targets for therapeutic …
Implications of peptide assemblies in amyloid diseases
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …
quality of life of millions worldwide, with profound social and economic implications. Despite …
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
R Kayed, E Head, JL Thompson, TM McIntire… - Science, 2003 - science.org
Soluble oligomers are common to most amyloids and may represent the primary toxic
species of amyloids, like the Aβ peptide in Alzheimer's disease (AD). Here we show that all …
species of amyloids, like the Aβ peptide in Alzheimer's disease (AD). Here we show that all …
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
WB Stine, KN Dahlgren, GA Krafft, MJ LaDu - Journal of Biological …, 2003 - ASBMB
Extensive research causally links amyloid-β peptide (Aβ) to Alzheimer's disease, although
the pathologically relevant Aβ conformation remains unclear. Aβ spontaneously aggregates …
the pathologically relevant Aβ conformation remains unclear. Aβ spontaneously aggregates …
Amyloid fibrils: abnormal protein assembly
RN Rambaran, LC Serpell - Prion, 2008 - Taylor & Francis
Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs
and tissues. Amyloid is insoluble and is structurally dominated by β‑sheet structure. Unlike …
and tissues. Amyloid is insoluble and is structurally dominated by β‑sheet structure. Unlike …
Amyloid fibrillogenesis: themes and variations
JC Rochet, PT Lansbury Jr - Current opinion in structural biology, 2000 - Elsevier
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both
'natively unfolded'and globular proteins have been shown to initiate fibrillization by adopting …
'natively unfolded'and globular proteins have been shown to initiate fibrillization by adopting …
Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR
JJ Balbach, Y Ishii, ON Antzutkin, RD Leapman… - Biochemistry, 2000 - ACS Publications
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …
and representing residues 16− 22 of the full-length β-amyloid peptide associated with …
Amyloid cross-seeding: Mechanism, implication, and inhibition
Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …
disease, etc. are caused by inclusions and plaques containing misfolded protein …