位置：成果数据库 > 期刊 > 期刊详情页
Interactions of a water-soluble fullerene derivative with amyloid-beta protofibrils: dynamics, bindi
  • ISSN号：1089-5647
  • 期刊名称：Journal of Physical Chemistry B Materials
  • 时间：2014.6.19
  • 页码：6733-6741
  • 相关项目：多肽自组装的多尺度分子模拟研究（四）
作者： Xi, Wenhui|Luo, Yin|Cao, Siqin|Wei, Guanghong|
同期刊论文项目
多肽自组装的多尺度分子模拟研究（四）
期刊论文 24
同项目期刊论文
Aβ(16–22) Peptides Can Assemble into Ordered β-Barrels and Bilayer &
Influence of Au nanoparticles on the aggregation of amyloid-beta-(25-35) peptides.
Conformational distribution and alpha-helix to beta-sheet transition of human amylin fragment dimer.
Abeta(16-22) peptides can assemble into ordered beta-barrels and bilayer beta-sheets, while substitu
Hydrophobic Interaction Drives Surface-Assisted Epitaxial Assembly of Amyloid-like Peptides
STRUCTURAL INSIGHT INTO THE POLYMORPHISM OF NNQNTF PROTOFIBRIL: IMPORTANCE OF INTERFACIAL WATER, POL
Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer
Molecular mechanism of fullerene-inhibited aggregation of Alzheimer’s β-amyloid peptide fragment
Single Mutations in Tau Modulate the Populations of Fibril Conformers through Seed Selection
Effects of hydroxylated carbon nanotubes on the aggregation of Aβ(16-22) peptides: a combined simula
Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the na
Structural insight into tau protein’s paradox of intrinsically disordered behavior, self-acetylation
Aβ “Stretching-and-Packing” Cross-seeding Mechanism Can Trigger Tau Protein Aggregation
Distinct Helix Propensities and Membrane Interactions of Human and Rat IAPP1-19 Monomers in Anionic
Amphiphilic peptides A6K and V6K display distinct oligomeric structures and self-assembly dynamics:
Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier
Atomic-Level Study of the Effects of O4 Molecules on the Structural Properties of Protofibrillar Aβ
Interactions of a water-soluble fullerene derivative with amyloid-β protofibrils: dynamics, binding