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Related Concept Videos

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...
The Proteasome02:18

The Proteasome

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...
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 (ubiquitin...

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Related Experiment Video

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Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

A panel of subunit-selective activity-based proteasome probes.

Martijn Verdoes1, Lianne I Willems, Wouter A van der Linden

  • 1Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands.

Organic & Biomolecular Chemistry
|May 8, 2010
PubMed
Summary

Researchers developed fluorescent probes to specifically target beta1 and beta5 sites of the mammalian proteasome. These probes aid in understanding the roles of active proteasome subunits in cellular functions like antigen presentation.

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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
09:45

Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples

Published on: May 10, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Mammals possess seven catalytically active proteasome subunits.
  • Understanding the specific roles of these subunits in processes like antigen presentation is crucial.
  • Targeted inhibitors and probes are needed to investigate individual subunit functions.

Purpose of the Study:

  • To develop novel fluorescent activity-based probes.
  • To achieve selective targeting of the beta1 and beta5 active sites of the constitutive proteasome.

Main Methods:

  • Design and synthesis of fluorescent activity-based probes.
  • Characterization of probe selectivity for specific proteasome active sites.

Main Results:

  • Successful development of fluorescent probes.
  • Demonstrated selective targeting of the beta1 and beta5 proteasome sites.

Conclusions:

  • The developed probes are valuable tools for studying proteasome function.
  • These probes will facilitate research into the roles of specific proteasome subunits in cellular processes.