関連する実験動画

Updated: Sep 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

18.5K

SpectraSageは,神経変性に関与するモノウビキチラ化タウタンパク質に20Sの特定のタンパク質分解パターンを明らかにした

Gabriele Antonio Zingale1, Irene Pandino1, Daniele Trivellato2

  • 1IRCCS Fondazione Bietti Rome Italy gabriele.zingale@fondazionebietti.it diego.sbardella@fondazionebietti.it.

Chemical science
|August 29, 2025
PubMed
まとめ

ユビキチンプロテアソーム系が神経変性に影響する この研究は,タウタンパク質のユビキティレーション位置が20Sプロテアソームによる分解にどのように影響し,特定の酵素メカニズムを明らかにすることを明らかにしています.

さらに関連する動画

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain09:35

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

12.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.0K

関連する概念動画

The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among 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. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.1K
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
958
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,...
9.8K