Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.
about
Global structural motions from the strain of a single hydrogen bondSolid-state NMR studies of metal-free SOD1 fibrillar structures.Physicochemical code for quinary protein interactions in Escherichia coli.Identification of human monoclonal antibodies specific for human SOD1 recognizing distinct epitopes and forms of SOD1.Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregationStructural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mappingZinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.SOD1 aggregation in ALS mice shows simplistic test tube behavior.Thermodynamics of protein destabilization in live cellsLow autophagy capacity implicated in motor system vulnerability to mutant superoxide dismutaseUnderstanding protein aggregation from the view of monomer dynamicsStructural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomerTargeting mitochondrial metal dyshomeostasis for the treatment of neurodegeneration.Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediatesUnderstanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells
P2860
Q27676522-26DABFF4-E1DE-42C8-94A7-9C820D1CA830Q30153414-538C456A-3F60-48EC-BE22-2FE773A67C42Q33790747-94B54B5E-53E3-4434-9E00-E65057D3097DQ34684165-61D93F78-BE5F-4F16-964D-72E90C649460Q35021849-90FBA5AB-7BEF-4F51-8522-DD757988379EQ35377964-CABDD5AA-7D15-49BA-BF03-2B06267D8536Q35566949-05958FB7-4F90-4475-B738-1BA1305E8110Q35961208-D32141C4-3497-4AF7-B08A-A69F87CDBC5CQ36155123-AF48B504-2912-408D-B754-75924C0366B8Q36503560-1D1FDA1E-1B99-4644-B8DC-CAF99B167D8EQ36806901-8B70F5A2-7215-44C3-A12D-0E91B333B587Q36991027-9B649A85-C268-4C87-8829-4D627909FE68Q37017713-0FC25483-A018-4632-A7EF-ED6BEAFC6FA8Q38570991-D1D5A6E4-7090-41B8-B2DC-3AEEC3312ADFQ42065939-0A5FB4FB-1EC6-4083-AEDD-07138E963A93Q42667951-11909B2D-5BFB-4259-BC8F-D4CCA1A2BCF3Q46851121-6A05C392-2F78-4B0C-A9F6-FEBEDB06BC69Q47127143-800A4CCE-E108-4BB9-BBBB-49795A3E6379Q47985099-BF5E51CE-D3D7-470A-A31E-1CD5250F6DBCQ57805726-F76EE016-93B1-4A58-8B31-F1C741DFE097
P2860
Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@ast
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@en
type
label
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@ast
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@en
prefLabel
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@ast
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@en
P2860
P356
P1476
Fibrillation precursor of supe ...... e protein-folding equilibrium.
@en
P2093
Mikael Oliveberg
P2860
P304
17868-17873
P356
10.1073/PNAS.1201795109
P407
P577
2012-07-13T00:00:00Z