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関連する概念動画

Amyloid Fibrils03:03

Amyloid Fibrils

10.1K
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,...
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Amyloid Fibrils03:03

Amyloid Fibrils

5.2K
5.2K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

3.1K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.7K

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Updated: Apr 22, 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

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アミロイドアセンブリにおける運動中介物質

Chen Liang1, Rong Ni, Jillian E Smith

  • 1Departments of Chemistry and Biology, Emory University , Atlanta, Georgia 30322, United States.

Journal of the American Chemical Society
|October 15, 2014
PubMed
まとめ

アルツハイマー病のアミロイドペプチドアセンブリは,オストワルドの成熟ではなく,構成的移行によって形成されます. アルツハイマー病の核形成経路の新たなメカニズムは,高度な構造的方法を使用して発見されました.

科学分野:

  • バイオケミストリー バイオケミストリー
  • 構造生物学 構造生物学とは
  • 神経科学は神経科学である.

背景:

  • アミロイド組成は,アルツハイマー病の病原性に関与しています.
  • アミロイドの成長の典型的なモデルは,オストワルドのような成熟です.

研究 の 目的:

  • アルツハイマー病におけるオランダの変異性Aβペプチドの核化メカニズムを調査する.
  • アミロイド組立中の構造的中間物質を明らかにする.

主な方法:

  • イソトープ編集型赤外線 (IR) スペクトロスコピー
  • 固体核磁気共鳴 (NMR) スペクトロスコーピーの固体核磁気共鳴 (NMR) スペクトロスコーピーは,固体核磁気共鳴 (NMR) スペクトロスコーピーの固体核磁気共鳴 (NMR) スペクトロスコーピーの固体核磁気共鳴 (NMR) の固体核磁気共鳴 (NMR) の固体核磁気共鳴 (NMR) の固体核磁気共鳴 (NMR) の固体核磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR) の固体磁気共鳴 (NMR)

主要な成果:

  • 核形成の過程で一連の形状的移行が観察され,オストワルド型の成熟と対照的であった.
  • インターメディエア・アセンブリで予期せぬストランド・オリエンテーションを特定しました.

さらに関連する動画

Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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関連する実験動画

Last Updated: Apr 22, 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

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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  • アミロイド核の漸進的組み立て経路を特徴づけた.

    • 結論:

    • オランダの変異性Aβペプチドの核形成には,明確な形状的移行が含まれています.
    • これらの発見は,アルツハイマー病におけるアミロイド形成のための新しい核化のメカニズムを示唆しています.
    • 漸進的組み立て経路は,アミロイド構造に関する新しい洞察を提供します.