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Related Concept Videos

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 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.
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Caspases01:24

Caspases

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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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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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Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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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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Related Experiment Video

Updated: Dec 14, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
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In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

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Using specificity to strategically target proteases.

Mark D Lim1, Charles S Craik

  • 1Department of Pharmaceutical Chemistry, University of California, School of Pharmacy, 513 Parnassus Avenue Room S-926, San Francisco, CA 94158, USA.

Bioorganic & Medicinal Chemistry
|April 25, 2008
PubMed
Summary
This summary is machine-generated.

Protease dysregulation links to disease. Activity-based methods, including positional scanning, synthetic combinatorial libraries, and substrate activity screening, help characterize proteases and their substrates for disease detection.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Proteases are enzymes crucial for biological functions.
  • Dysregulated protease activity is linked to various diseases and cancers.
  • Protease substrates offer potential for disease detection and biomarker development.

Purpose of the Study:

  • To review the development of activity-based methodologies for protease characterization.
  • To highlight the application of positional scanning, synthetic combinatorial libraries (PS-SCL's), and substrate activity screening (SAS) assays.
  • To discuss the understanding of natural protease substrates and emerging technologies.

Main Methods:

  • Focus on activity-based profiling techniques.
  • Utilizes positional scanning, synthetic combinatorial libraries (PS-SCL's).
  • Employs substrate activity screening (SAS) assays.

Main Results:

  • Characterization of protease activity and specificity.
  • Identification of protease-specific substrates.
  • Advancement in understanding protease function in disease.

Conclusions:

  • Activity-based methods offer powerful tools for protease research.
  • PS-SCL's and SAS assays enhance the study of protease-substrate interactions.
  • These methodologies contribute to the development of novel diagnostics and therapeutics.