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Amyloid Fibrils03:03

Amyloid Fibrils

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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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Protein Folding01:22

Protein Folding

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Protein Organization01:13

Protein Organization

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Formation of Intermediate Filaments00:57

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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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Formation of Higher-order Actin Filaments01:11

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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Assembly of Cytoskeletal Filaments01:18

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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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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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アミロイド組成中の繊維ポリモルフの構造進化

Martin Wilkinson1, Yong Xu1, Dev Thacker1

  • 1Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.

Cell
|December 22, 2023
PubMed
まとめ
この要約は機械生成です。

アミロイド線維の構造は,組み立ての過程で時間とともに変化します. クリオ電子顕微鏡では,ヒトの島アミロイドポリペプチド動中に形成され,消失する異なった構造を明らかにし,新しい病気の洞察を提供しました.

キーワード:
アミロイドアミロイド多形化クリオエム糖尿病運動学タンパク質の集積タンパク質繊維タンパク質構造構造生物学

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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科学分野:

  • 生物化学
  • 構造生物学
  • 分子生物物理学

背景:

  • クリオ電子顕微鏡 (cryo-EM) は,しばしば疾患に関連した静的アミロイド線維の構造を明らかにした.
  • これらの決定された構造は,組み立ての終点を表し,初期段階の繊維と潜在的な構造的多形性との関係を未知のままにします.
  • 繊維の形成のダイナミックな性質を理解することは,病気のメカニズムを解読するために不可欠です.

研究 の 目的:

  • アミロイド線維の構造的多様性を in vitro 線維の異なる段階で調査する.
  • 組み立ての過程で繊維構造が時間とともに進化するかどうかを判断する.
  • 病気の進行に対する動的線維形成の影響を調査する.

主な方法:

  • アミロイド線維の構造を分析するために,冷凍電子顕微鏡 (cryo-EM) を利用した.
  • ヒト・アイレット・アミロイド・ポリペプチド (IAPP-S20G) の疾患に関連する変異体によるin vitroフィブリレーションの様々な時間点で形成された繊維を調べた.
  • 概括性を評価するために,ワイルド型ヒトアミロイドポリペプチド (hIAPP) でタイムコース分析を行った.

主要な成果:

  • IAPP-S20G線維の遅延,成長,平原相に対応する明確な線維構造が観察されました.
  • 組み立ての過程で特定の繊維の出現と消失を記録した.
  • 野生型のhIAPPも繊維構造の時間依存の変化を示し,一般的な現象を示しています.

結論:

  • アミロイド繊維の組み立ては,一時的に人口化された構造の形成と消失を含むダイナミックなプロセスです.
  • 線維構造は静的ではなく,時間とともに進化し,病理学的性質に影響を与える可能性があります.
  • これらの発見は,アミロイドの組み立てメカニズムと病気の進行に関する新しい洞察を提供します.