関連する実験動画

Updated: Jun 19, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 14, 2010

プロテイン・ディスルファイド・イソメラーゼは,アミロイドβペプチドのオリゴメア集合体を溶解し,解毒する

Antonio Mele1, Albert Serrano1, Maria C Zabala-Rodriguez1

  • 1Burnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.

FEBS letters
|February 20, 2026
PubMed
まとめ

タンパク質ジスルファイドイソメラーゼ (PDI) は有毒なアミロイドβ (Aβ) オリゴーマーを溶解し,アルツハイマー病に対する神経保護を提供します. この分解活性は,繊維ではなく,初期のAβ集積を標的にし,治療の可能性を示唆しています.

キーワード:
アルツハイマー病 (Alzheimer's disease) とは,アルツハイマー病 (Alzheimer's disease) を意味する.チャプロン (Chaperone) とは条件付き障害である.デザグレーゲージを分解する.タンパク質ジスルファイドイソメラーゼ

さらに関連する動画

Purification of Hsp104, a Protein Disaggregase07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

関連する概念動画

Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Folding01:25

Protein Folding

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...
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...