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相关概念视频

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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Overview
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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基于氨的纤维状系统.

Soumen Kuila1, Sukantha Dey1, Pijush Singh1,2

  • 1Department of Chemistry, University of North Bengal, Raja Rammohanpur, Siliguri 734013, West Bengal, India. jayanta@nbu.ac.in.

Chemical communications (Cambridge, England)
|November 21, 2023
PubMed
概括

基尿症 (PKU) 涉及氨 (Phe) 形成有毒的粉样纤维,导致智力障碍. 这篇评论详细介绍了Phe纤维素的形成,其毒性和抑制策略,提供了针对PKU的数据库.

科学领域:

  • 生物化学 生化学
  • 神经科学是一个神经科学.
  • 分子生物学分子生物学

背景情况:

  • 基尿症 (PKU) 是一种由氨积累引起的代谢障碍.
  • 过多的氨形成有毒的粉样蛋白纤维,导致神经退行.
  • 了解纤维细胞的形成对于开发PKU疗法至关重要.

研究的目的:

  • 审查基于氨氨酸的粉样蛋白纤维的形成.
  • 讨论影响纤维细胞形成动态的因素.
  • 探索抑制策略,并将毒性与其他神经退行性进行比较.

主要方法:

  • 关于Phe纤维素形成研究的文献综述.
  • 分析用于自组装的光谱和显微技术.
  • 将Phe-fibril的毒性与其他氨基原蛋白的毒性进行比较.

主要成果:

  • 纤维细胞的形成受到溶剂,pH值,度和温度的影响.
  • 基于Phe的纤维素具有毒性,可以诱导其他蛋白质形成纤维素.
  • 包括多,药物和纳米粒子在内的各种化合物抑制纤维的形成.

结论:

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  • 乳腺纤维的形成是一个复杂的过程,受多种因素的影响.
  • 抑制Phe纤维素的形成是PKU的一个有前途的治疗策略.
  • 这项工作为PKU研究和治疗开发提供了一个全面的数据库.