Quantitative thermophoretic study of disease-related protein aggregates
about
Continuous Isotropic-Nematic Transition in Amyloid Fibril Suspensions Driven by Thermophoresis.Structure, Distribution, and Genetic Profile of α-Synuclein and Their Potential Clinical Application in Parkinson's Disease.Confinement effect on the dynamics of non-equilibrium concentration fluctuations far from the onset of convection.Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth.What Controls Thermo-osmosis? Molecular Simulations Show the Critical Role of Interfacial Hydrodynamics.Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism.
P2860
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P2860
Quantitative thermophoretic study of disease-related protein aggregates
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Quantitative thermophoretic study of disease-related protein aggregates
@ast
Quantitative thermophoretic study of disease-related protein aggregates
@en
type
label
Quantitative thermophoretic study of disease-related protein aggregates
@ast
Quantitative thermophoretic study of disease-related protein aggregates
@en
prefLabel
Quantitative thermophoretic study of disease-related protein aggregates
@ast
Quantitative thermophoretic study of disease-related protein aggregates
@en
P2093
P2860
P356
P1433
P1476
Quantitative thermophoretic study of disease-related protein aggregates
@en
P2093
Dieter Braun
Erwin De Genst
Judith J Mittag
Manuel Wolff
Therese W Herling
Tuomas P J Knowles
P2860
P2888
P356
10.1038/SREP22829
P407
P577
2016-03-17T00:00:00Z