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Related Concept Videos

The Proteasome01:13

The Proteasome

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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...
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The Proteasome Structure01:17

The Proteasome Structure

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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...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Early recovery of proteasome activity in cells pulse-treated with proteasome inhibitors is independent of DDI2.

eLife·2024
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Early recovery of proteasome activity in cells pulse-treated with proteasome inhibitors is independent of DDI2.

bioRxiv : the preprint server for biology·2023
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Related Experiment Video

Updated: Oct 6, 2025

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Site-Specific Proteasome Inhibitors.

Alexei F Kisselev1

  • 1Department of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, AL 36849, USA.

Biomolecules
|January 21, 2022
PubMed
Summary
This summary is machine-generated.

New proteasome inhibitors offer precise targeting of individual active sites. These site-specific drugs advance research into protein homeostasis and disease treatment, moving beyond broad-spectrum proteasome inhibition.

Keywords:
immunoproteasomeubiquitin-proteasome system

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • The proteasome is a critical cellular machine for protein degradation and homeostasis.
  • Existing proteasome inhibitors target multiple active sites, impacting various cellular functions.
  • Approved drugs like bortezomib treat multiple myeloma, highlighting proteasome inhibition's therapeutic potential.

Purpose of the Study:

  • To review the development and application of site-specific proteasome inhibitors.
  • To explore the use of these inhibitors in understanding proteasome active site biology.
  • To discuss their potential as drug targets for various diseases.

Main Methods:

  • Literature review of site-specific proteasome inhibitors.
  • Analysis of studies utilizing selective proteasome inhibitors.
  • Discussion of drug development strategies for proteasome-targeted therapies.

Main Results:

  • Development of highly specific inhibitors for individual proteasome active sites (β5, β2, β1).
  • Emergence of inhibitors targeting the immunoproteasome's distinct active sites.
  • Demonstration of site-specific inhibitors as valuable tools in biological research.

Conclusions:

  • Site-specific proteasome inhibitors represent a significant advancement over traditional broad-spectrum agents.
  • These selective inhibitors enable detailed study of proteasome active site function.
  • Targeted proteasome inhibition holds promise for novel therapeutic strategies in diverse diseases.