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Amyloid Fibrils03:03

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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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Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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Rapid Generation of Amyloid from Native Proteins In vitro
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拡大するアミロイド族:構造,安定性,機能,病原性

Michael R Sawaya1, Michael P Hughes1, Jose A Rodriguez1

  • 1Departments of Chemistry and Biochemistry and Biological Chemistry, UCLA, Los Angeles, CA 90095, USA; Howard Hughes Medical Institute, UCLA, Los Angeles, CA 90095, USA; UCLA-DOE Institute, UCLA, Los Angeles, CA 90095, USA; Molecular Biology Institute, UCLA, Los Angeles, CA 90095, USA.

Cell
|September 17, 2021
PubMed
まとめ

アミロイドタンパク質は様々な構造を持つ線維を形成し,病気と機能に影響を与えます. 構造的な挫折は 形状の変化性と適応性を説明します

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科学分野:

  • 生物化学
  • 構造生物学
  • 分子生物学

背景:

  • アミロイドタンパク質は アルツハイマー病のような病気に 起因することが知られています
  • これらのタンパク質は,球状タンパク質と異なるユニークな繊維構造を採用しています.
  • 単一のタンパク質配列は,異なるアミロイド構造 (ポリモルフ) を形成することができる.

研究 の 目的:

  • 様々なアミロイド繊維の 原子レベルの構造を調べるため
  • アミロイドの機能と病原性の構造的基礎と構造的変動性を理解する.
  • アミロイドの行動における 構造的挫折の役割を調査する

主な方法:

  • 80以上のアミロイド繊維の 高解像度構造分析
  • 病原性および機能性アミロイド構造の比較分析
  • タンパク質の配列,形状,および繊維の性質の関係に関する調査.

主要な成果:

  • 多くのアミロイドタンパク質繊維の詳細な原子構造が解明されている.
  • 病原性および機能的なタイプを含む80以上の異なるアミロイド繊維構造を特定しました.
  • 構造的な挫折によって引き起こされる形状の変動がアミロイドの機能と病気の鍵であることを示した.

結論:

  • アミロイド構造は高度な可塑性があり,単一の配列で多様な繊維ポリモルフを形成することができる.
  • 構造的挫折は,アミロイド線維の安定性,敏感性,および生物学的機能を決定する重要な要因である.
  • アミロイドの形状の多様性を理解することは,健康と病気における役割を解読するために不可欠です.