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Related Concept Videos

The Proteasome02:18

The Proteasome

10.1K
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...
10.1K
The Proteasome01:13

The Proteasome

1.6K
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...
1.6K
The Proteasome02:18

The Proteasome

4.4K
4.4K
Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor04:12

Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor

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In this video, we demonstrate a cell-based protein aggregation assay using proteasome inhibitors, which block proteasome activity, preventing misfolded, mutant proteins, fused to a fluorescent label, from undergoing ubiquitin-dependent proteasomal degradation, leading to their accumulation within the cell cytoplasm. The protein aggregates are then visualized and quantified by fluorescence...
814
Assaying Proteasomal Degradation in a Cell-free System in Plants07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

15.0K
Targeted protein degradation represents a major regulatory mechanism for cell function. It occurs via a conserved ubiquitin-proteasome pathway, which attaches polyubiquitin chains to the target protein that then serve as molecular “tags” for the 26S proteasome. Here, we describe a simple and reliable cell-free assay for proteasomal degradation of...
15.0K
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

7.0K
This protocol uses both subunit coexpression and postlysis subunit mixing for a more thorough examination of recombinant proteasome...
7.0K

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Related Experiment Video

Updated: Jan 20, 2026

The Ubiquitin-Proteasome Pathway
02:18

The Ubiquitin-Proteasome Pathway

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Proteasome Inhibitor Drugs.

Lloyd D Fricker1

  • 1Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA;

Annual Review of Pharmacology and Toxicology
|September 4, 2019
PubMed
Summary

Proteasome inhibitors are crucial cancer drugs, but their exact cell death mechanisms remain unclear. Research suggests their effects might involve pathways beyond direct proteasome inhibition at clinical concentrations.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Proteasomes are essential protein complexes for cellular protein degradation.
  • Distinct proteasome forms exist with varying subunits and associated proteins.
  • Proteasome inhibitors are established treatments for multiple myeloma and mantle cell lymphoma, with new agents under development.

Purpose of the Study:

  • To elucidate the downstream molecular events leading to cell death induced by proteasome inhibitors.
  • To investigate potential mechanisms of action beyond direct proteasome inhibition.

Main Methods:

  • Analysis of proteasome structure and function.
  • Pharmacological studies of proteasome inhibitors (e.g., bortezomib, carfilzomib, ixazomib).
  • Investigation of cellular responses to proteasome inhibitors at varying concentrations.
Keywords:
bortezomibcarfilzomibixazomibpeptideproteaseubiquitin

More Related Videos

Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor
04:12

Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor

814
Assaying Proteasomal Degradation in a Cell-free System in Plants
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Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

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Related Experiment Videos

Last Updated: Jan 20, 2026

The Ubiquitin-Proteasome Pathway
02:18

The Ubiquitin-Proteasome Pathway

10.1K
Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor
04:12

Protein Aggregate Formation Assay: A Method to Detect and Quantify Protein Aggregation in Cultured Cells upon Induction by Proteasome Inhibitor

814
Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

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Main Results:

  • Proteasome inhibitors demonstrate efficacy in treating specific hematological malignancies.
  • Observed effects on protein turnover occur at concentrations higher than clinically achieved.
  • The precise downstream signaling pathways mediating selective cell death are not fully understood.

Conclusions:

  • While proteasome inhibition is the primary action, other mechanisms may contribute to the therapeutic effects of these drugs.
  • Further research is needed to clarify the complete action of proteasome inhibitors at clinically relevant concentrations.