Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.
about
Contrasting effects of nanoparticle-protein attraction on amyloid aggregationSolid-state NMR studies of metal-free SOD1 fibrillar structures.Direct observation of a single nanoparticle-ubiquitin corona formationAggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesCu,Zn-superoxide dismutase without Zn is folded but catalytically inactive.Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and propertiesApplications of Discrete Molecular Dynamics in biology and medicineCompetitive binding of natural amphiphiles with graphene derivativesIntrinsically semi-disordered state and its role in induced folding and protein aggregationComputational approaches to understanding protein aggregation in neurodegeneration.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates.Inhibition of IAPP aggregation by insulin depends on the insulin oligomeric state regulated by zinc ion concentration.A hidden aggregation-prone structure in the heart of hypoxia inducible factor prolyl hydroxylase.NanoEHS beyond Toxicity - Focusing on Biocorona.Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.A structural modeling approach for the understanding of initiation and elongation of ALS-linked superoxide dismutase fibrils.Study of mutation and misfolding of Cu-Zn SOD1 protein.Folding 19 proteins to their native state and stability of large proteins from a coarse-grained model.Cholesterol secosterol aldehyde adduction and aggregation of Cu,Zn-superoxide dismutase: Potential implications in ALS
P2860
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P2860
Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@ast
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@en
type
label
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@ast
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@en
prefLabel
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@ast
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@en
P2860
P50
P1476
Local unfolding of Cu, Zn supe ...... ology of fibrillar aggregates.
@en
P2093
Nobuyuki Nukina
P2860
P304
P356
10.1016/J.JMB.2011.12.029
P407
P577
2011-12-21T00:00:00Z