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関連する概念動画

Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
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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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

20.5K
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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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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Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

1.8K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
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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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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関連する実験動画

Updated: Jul 9, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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病気特有のタウ線維は,ポリモルフな中間体によって組み合わされる.

Sofia Lövestam1, David Li1, Jane L Wagstaff1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

Nature
|November 29, 2023
PubMed
まとめ

研究者らはタウタンパク質の組み立てにおける 初期の中間アミロイドフィラメント構造を発見し アルツハイマー病のような 神経退行性疾患を理解し 新しい治療戦略を策定する上で 決定的な役割を果たしました

さらに関連する動画

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

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関連する実験動画

Last Updated: Jul 9, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.4K
In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

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科学分野:

  • 神経科学
  • 生物化学
  • 構造生物学

背景:

  • アミロイド繊維組の中間種は神経変性疾患に関与している.
  • これらの中間物質に関する構造データは限られており,アミロイド組成機構の理解を妨げています.

研究 の 目的:

  • 切断されたタウタンパク質をアミロイドフィラメントに組み立てることを in vitro で調査する.
  • 繊維の形成過程における中間種の構造的特徴を決定する.

主な方法:

  • 時間の解像度を持つ冷凍電子顕微鏡 (cryo-EM) を使って,タウの組立を研究した.
  • 核磁共振 (NMR) を用いて,単体タウ構造を分析した.

主要な成果:

  • オーダーされたコア (残留物302-316) を有する共有の初期中間アミロイドフィラメントが特定された.
  • このコア構造は単体タウでも観察され,固いベータ鎖のような形状を採用した.
  • その後の時間点は,反応条件に依存する多様な中間構造を明らかにし,そのほとんどは反応の終わりまでに消失した.
  • 最終的な繊維は人間の脳サンプルと一致する オーダーされた核を保持した.

結論:

  • この研究は,アミロイド組成における初次および二次核形成に関する構造的洞察を提供します.
  • 神経退行性疾患の新たな治療法を開発するための潜在的標的となる.