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Chaperonins

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)

Bio-Agent Context: Research Results

Experts

1. Qamra, Rohini: 2 articles (09/2005 - 09/2004)
2. Mande, Shekhar C: 2 articles (09/2005 - 09/2004)
3. Henderson, B: 2 articles (05/2004 - 09/2000)
4. Carcoforo, Paolo: 1 article (05/2013)
5. Cervellati, Carlo: 1 article (05/2013)
6. Lanzara, Vincenzo: 1 article (05/2013)
7. De Laureto, Patrizia Polverino: 1 article (05/2013)
8. Agostinelli, Enzo: 1 article (05/2013)
9. Portinari, Mattia: 1 article (05/2013)
10. Frare, Erica: 1 article (05/2013)

Related Diseases

1. Shock
2. Reperfusion Injury
3. Neurodegenerative Diseases (Neurodegenerative Disease)
4. Polyps
5. Neoplasms (Cancer)

Related Drugs and Biologics

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

Related Therapies and Procedures

1. Warm Ischemia