Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.
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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregationManganese exposure induces α-synuclein aggregation in the frontal cortex of non-human primatesConformational Entropy of Intrinsically Disordered Proteins from Amino Acid TriadsA zebrafish model of manganism reveals reversible and treatable symptoms that are independent of neurotoxicity.Resveratrol and Alzheimer's disease: message in a bottle on red wine and cognition.Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress.Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disordersFairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.In Vivo MRI Mapping of Brain Iron Deposition across the Adult Lifespan.Concentration Dependent Ion-Protein Interaction Patterns Underlying Protein Oligomerization BehavioursStructures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics.Advances in electrochemical detection for study of neurodegenerative disorders.Heavy metals and metalloids as a cause for protein misfolding and aggregation.The use of metabolomics in the study of metals in biological systems.Reactivity of U-associated osteopontin with lactoferrin: a one-to-many complex.Brain biometals and Alzheimer's disease - boon or bane?Human predisposition to cognitive impairment and its relation with environmental exposure to potentially toxic elements.Progress of elemental anomalies of hippocampal formation in the pilocarpine model of temporal lobe epilepsy--an X-ray fluorescence microscopy studyEffect of acidic pH on the stability of α-synuclein dimers.Ruthenium complexes as novel inhibitors of human islet amyloid polypeptide fibril formation.Characterization of UO2(2+) binding to osteopontin, a highly phosphorylated protein: insights into potential mechanisms of uranyl accumulation in bones.Study of interactions between metal ions and protein model compounds by energy decomposition analyses and the AMOEBA force field.The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.Phosphorylated α-Synuclein-Copper Complex Formation in the Pathogenesis of Parkinson's Disease.Electroanalysis of the interaction between (-)-epigallocatechin-3-gallate (EGCG) and amyloid-β in the presence of copper.Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein.
P2860
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P2860
Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.
description
article científic
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article scientifique
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articol științific
@ro
articolo scientifico
@it
artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@en
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@nl
type
label
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@en
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@nl
prefLabel
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@en
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@nl
P2860
P356
P1433
P1476
Role of metal ions in aggregat ...... in neurodegenerative diseases.
@en
P2093
Leonid Breydo
P2860
P304
P356
10.1039/C1MT00106J
P577
2011-08-25T00:00:00Z