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Updated: May 15, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

パラダイムを混乱させる:アミロイド線維細胞核化の特異性

Dimo Kashchiev1, Raffaela Cabriolu, Stefan Auer

  • 1Institute of Physical Chemistry, Bulgarian Academy of Sciences, ul. Acad. G. Bonchev 11, Sofia 1113, Bulgaria.

Journal of the American Chemical Society
|January 12, 2013
PubMed
まとめ

アミロイド線維の核形成はユニークな方法で発生し,新しい理論が必要です. タンパク質濃度の値が存在し,それ以下では核形成が停止し,それ以上では加速し,治療戦略を導く.

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Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding01:22

Protein Folding

Overview