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Chaperonins Summary

Description: A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.

Also Known As: Chaperonin Complexes; Chaperonin Family; Chaperonin Protein Complex

Networked: 38 relevant articles (0 outcomes, 5 trials/studies) for this Bio-Agent

Key Diseases for which Chaperonins is Relevant

  1. Shock : 2 studies in 10 results
  2. Reperfusion Injury : 1 study in 2 results
  3. Neurodegenerative Diseases (Neurodegenerative Disease) : 1 study in 1 result
  4. Polyps : 1 study in 1 result
  5. Neoplasms (Cancer) : 1 study in 1 result
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Drugs Related to Chaperonins

  1. Chaperonin 60
  2. Luciferases
  3. Proteins (Proteins, Gene)
  4. Heat-Shock Proteins (Heat-Shock Protein)
  5. Adenosine Triphosphate (ATP)
  6. Proteasome Endopeptidase Complex (Proteasome)
  7. Calreticulin
  8. Protein Disulfide-Isomerases
  9. Molecular Chaperones (Chaperone, Molecular)
  10. Nitrogen
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Therapies Related to Chaperonins

  1. Warm Ischemia

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