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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
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The Proteasome Structure01:17

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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.
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Nanosensors to Detect Protease Activity In Vivo for Noninvasive Diagnostics
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Published on: July 16, 2018

Targeting proteases: successes, failures and future prospects.

Boris Turk1

  • 1Department of Biochemistry and Molecular Biology, J. Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia. boris.turk@ijs.si

Nature Reviews. Drug Discovery
|September 7, 2006
PubMed
Summary

Proteases, once viewed as simple protein degraders, are now recognized as vital signaling molecules. Dysregulation of these molecules is linked to diseases, driving the development of targeted protease drugs.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Proteases were historically considered solely as protein-degrading enzymes.
  • Emerging research highlights proteases as crucial signaling molecules in numerous biological processes.
  • Dysregulation of protease activity is implicated in various pathologies, including cancer and cardiovascular diseases.

Purpose of the Study:

  • To review the current understanding of human protease research.
  • To discuss the role of proteases in signaling pathways and disease.
  • To examine the prospects for future protease-targeted drug development.

Main Methods:

  • Literature review of protease research.
  • Analysis of protease signaling pathways.
  • Case studies of successful and failed protease-targeted drugs.

Main Results:

  • Proteases are now understood to be critical signaling molecules.
  • Protease dysregulation contributes to significant human diseases.
  • Several protease-targeting drugs are approved, with many more in development.

Conclusions:

  • Protease research has evolved significantly, revealing their complex roles.
  • Targeting proteases offers a promising therapeutic strategy for various diseases.
  • Future drug development requires careful consideration of protease functions and dysfunctions.