Amyloid peptides and proteins in review
RS Harrison, PC Sharpe, Y Singh, DP Fairlie - Reviews of physiology …, 2007 - Springer
Amyloids are filamentous protein deposits ranging in size from nanometres to microns and
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …
Different species of α-synuclein oligomers induce calcium influx and seeding
KM Danzer, D Haasen, AR Karow… - Journal of …, 2007 - Soc Neuroscience
Aggregation of α-synuclein (α-syn) has been linked to the pathogenesis of Parkinson's
disease (PD) and other neurodegenerative diseases. Increasing evidence suggests that …
disease (PD) and other neurodegenerative diseases. Increasing evidence suggests that …
Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged α-synuclein
MJ Roberti, CW Bertoncini, R Klement… - Nature …, 2007 - nature.com
Abstract α-synuclein is a major component of intraneuronal protein aggregates constituting a
distinctive feature of Parkinson disease. To date, fluorescence imaging of dynamic …
distinctive feature of Parkinson disease. To date, fluorescence imaging of dynamic …
Role of different regions of α-synuclein in the assembly of fibrils
Z Qin, D Hu, S Han, DP Hong, AL Fink - Biochemistry, 2007 - ACS Publications
Elucidating the details of the assembly of amyloid fibrils is a key step to understanding the
mechanism of amyloid deposition diseases including Parkinson's disease. Although several …
mechanism of amyloid deposition diseases including Parkinson's disease. Although several …
Structural characterization of the intrinsically unfolded protein β-synuclein, a natural negative regulator of α-synuclein aggregation
CW Bertoncini, RM Rasia, GR Lamberto… - Journal of molecular …, 2007 - Elsevier
The synuclein family of intrinsically unfolded proteins is composed of three highly
homologous members, α-synuclein (αS), β-synuclein (βS) and γ-synuclein (γS), which are …
homologous members, α-synuclein (αS), β-synuclein (βS) and γ-synuclein (γS), which are …
[PDF][PDF] Copper-and iron-induced differential fibril formation in alpha-synuclein: TEM study
ISS Bharathi, KS Rao - Neurosci Lett, 2007 - academia.edu
Abstract α-Synuclein filaments are the central component of intracytoplasmic inclusion
bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the …
bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the …
DNA induces folding in α-synuclein: understanding the mechanism using chaperone property of osmolytes
α-Synuclein conformational modulation leading to fibrillation has been centrally implicated
in Parkinson's disease. Previously, we have shown that α-synuclein has DNA binding …
in Parkinson's disease. Previously, we have shown that α-synuclein has DNA binding …
Copper-and iron-induced differential fibril formation in α-synuclein: TEM study
SS Indi, KSJ Rao - Neuroscience letters, 2007 - Elsevier
α-Synuclein filaments are the central component of intracytoplasmic inclusion bodies
characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant …
characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant …
Photo‐activity induced by amyloidogenesis
O Tcherkasskaya - Protein science, 2007 - Wiley Online Library
Accumulation of chemically altered proteins is a noted characteristic of biological aging, and
increasing evidence suggests a variety of deleterious cellular developments associated with …
increasing evidence suggests a variety of deleterious cellular developments associated with …
Alpha-synuclein as a template for the synthesis of metallic nanowires
S Padalkar, J Hulleman, P Deb, K Cunzeman… - …, 2007 - iopscience.iop.org
Exploiting the concepts learnt from nature to build new nanomaterials from the bottom up is
critical for the efficient design of complex nanodevices. We demonstrate for the first time that …
critical for the efficient design of complex nanodevices. We demonstrate for the first time that …