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Nucleation mechanisms and morphologies in insulin amyloid fibril formation
Vito Foderà
, F Librizzi, V Vetri, V Militello, G Navarra, M Leone
1
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Keyphrases
Adverse Conditions
50%
Aggregation Behavior
50%
Alzheimer's Disease
50%
Amyloid Fibrillation
100%
Amyloid Fibrils
50%
Atomic Force Microscopy
50%
Biophysics
50%
Degenerative Pathology
50%
Disease-related Proteins
50%
Fibril Formation
50%
Fibril Morphology
50%
Fibrillation
50%
Fibrillation Kinetics
50%
Fluorescence Property
50%
Induced Aggregation
50%
Insulin
100%
Insulin Stability
50%
Light Scattering
50%
Medical Sciences
50%
Nucleation Mechanism
100%
Parkinson's Disease
50%
Pharmaceutical Science
50%
Physical Instability
50%
Protein Aggregation
50%
Protein Concentration
50%
Protein Drug
50%
Scientific Approach
50%
Spatial Heterogeneity
50%
Stochasticity
50%
Thermally Induced
50%
Thioflavin T
50%
Type 2 Diabetes Mellitus (T2DM)
50%
Chemistry
Amyloid Fibril
100%
Atomic Force Microscopy
33%
formation
100%
Light Scattering
33%
Nucleation
100%
Protein Aggregation
33%
stability
33%
Material Science
Atomic Force Microscopy
33%
Light Scattering
33%
Nucleation
100%
Protein Aggregation
33%
Surface (Surface Science)
33%
Biochemistry, Genetics and Molecular Biology
Amyloid Protein
100%
Atomic Force Microscopy
25%
Biochemistry
25%
Light Scattering
25%
Protein Aggregation
25%
Thioflavin
25%
Neuroscience
Alzheimer's Disease
25%
Amyloid Protein
100%
Light Scattering
25%
Parkinson's Disease
25%
Protein Aggregation
25%