The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.

The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.

Item
http://www.wikidata.org/entity/Q36638623
Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein proteinThe Dependence of Amyloid-β Dynamics on Protein Force Fields and Water Models.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Effects of the Pathogenic Mutation A117V and the Protective Mutation H111S on the Folding and Aggregation of PrP106-126: Insights from Replica Exchange Molecular Dynamics Simulations.Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics.Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.Arginine and disordered amyloid-β peptide structures: molecular level insights into the toxicity in Alzheimer's diseaseDivalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms.Effects of Zn2+ binding on the structural and dynamic properties of amyloid β peptide associated with Alzheimer's disease: Asp1 or Glu11?Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42Effect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.The folding mechanism and key metastable state identification of the PrP127-147 monomer studied by molecular dynamics simulations and Markov state model analysis.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
P2860

The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.

Item
http://www.wikidata.org/entity/Q36638623
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@ast
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@en
type
label
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@ast
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@en
prefLabel
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@ast
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
The structures of the E22Δ mut ...... wild-type amyloid-β alloforms
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932