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Related Concept Videos

The Proteasome01:13

The Proteasome

1.9K
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 Proteasome02:18

The Proteasome

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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...
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The Proteasome02:18

The Proteasome

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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

9.1K
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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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Related Experiment Video

Updated: Feb 27, 2026

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

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Turning-ON Proteasomes.

Jan Henrik Krahn1, Farnusch Kaschani1, Markus Kaiser1

  • 1Chemical Biology, University of Duisburg-Essen, ZMB, Faculty of Biology, Universitätsstraße 2, 45117 Essen, Germany.

Cell Chemical Biology
|June 24, 2017
PubMed
Summary
This summary is machine-generated.

Researchers identified a p38 mitogen-activated protein kinase (MAPK) inhibitor that activates proteasomes. This discovery offers new therapeutic avenues for neurodegenerative diseases by enhancing protein aggregate clearance.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Neuroscience

Background:

  • Proteasome inhibitors are established tools, but proteasome activators remain underexplored.
  • Understanding proteasome function is crucial for developing new therapeutic strategies.

Purpose of the Study:

  • To identify novel proteasome activators using a chemical screen.
  • To investigate the therapeutic potential of proteasome activators in neurodegenerative diseases.

Main Methods:

  • A chemical screen was employed to identify compounds that modulate proteasome activity.
  • The identified compound's effect on proteasome activity and protein aggregate clearance was assessed.

Main Results:

  • A p38 mitogen-activated protein kinase (MAPK) inhibitor was identified as a proteasome activator.
  • The compound demonstrated enhanced clearance of protein aggregates in cellular models.

Conclusions:

  • The study highlights a novel class of proteasome activators.
  • This finding suggests potential new chemotherapeutic strategies for neurodegenerative conditions.