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Related Concept Videos

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...
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 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 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...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...

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Related Experiment Video

Updated: Jun 8, 2026

Cellular Redox Profiling Using High-content Microscopy
11:37

Cellular Redox Profiling Using High-content Microscopy

Published on: May 14, 2017

[Proteasome inhibitors].

Yasushi Saeki1, Keisuke Fukunaga, Keiji Tanaka

  • 1Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|October 20, 2010
PubMed
Summary
This summary is machine-generated.

The 26S proteasome is a key target for cancer therapy. This review covers bortezomib and newer proteasome inhibitors for treating multiple myeloma and other cancers.

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Last Updated: Jun 8, 2026

Cellular Redox Profiling Using High-content Microscopy
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Published on: May 14, 2017

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
10:44

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs

Published on: May 15, 2019

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Context:

  • The 26S proteasome regulates intracellular protein degradation.
  • Targeting proteasome activity offers a novel cancer therapeutic strategy.
  • Bortezomib, a proteasome inhibitor, is approved for multiple myeloma.

Purpose:

  • To review the clinical applications of bortezomib.
  • To discuss the role of proteasome inhibitors in cancer therapy.
  • To provide an overview of second-generation proteasome inhibitors.

Summary:

  • Bortezomib is a clinically effective proteasome inhibitor for multiple myeloma.
  • Proteasome inhibition induces cancer cell death and chemosensitization.
  • This review examines current bortezomib use and emerging proteasome inhibitors.

Impact:

  • Highlights the therapeutic potential of proteasome inhibition in oncology.
  • Informs clinical practice regarding bortezomib and combination therapies.
  • Guides future research in the development of novel proteasome inhibitors.