Molecular chaperone

Introduction: Molecular chaperone

Description of Molecular chaperone

Molecular chaperone: diverse family of prokaryotic and eukaryotic intracellular proteins involved in the assembly and transmembrane translocation of other proteins; seem to function by stabilizing partially unfolded states; includes certain heat shock proteins.
Source: CRISP

Molecular chaperone: A family of cellular proteins that mediate the correct assembly or disassembly of other polypeptides, and in some cases their assembly into oligomeric structures, but which are not components of those final structures. It is believed that chaperone proteins assist polypeptides to self-assemble by inhibiting alternative assembly pathways that produce nonfunctional structures. Some classes of molecular chaperones are the nucleoplasmins, the CHAPERONINS, the HEAT-SHOCK PROTEINS 70, and the HSP90 HEAT-SHOCK PROTEINS.
Source: MeSH 2007

Molecular chaperone: Related Topics

These medical condition or symptom topics may be relevant to medical information for Molecular chaperone:

• Molecular
• Molecular disease
• Chaperone
• Family
• Prokaryotic
• Eukaryotic
• Intracellular
• Proteins
• Transmembrane
• Translocation

Terms associated with Molecular chaperone:

More specific terms for Molecular chaperone:

• calnexin

Source - CRISP

Broader terms for Molecular chaperone

• transport protein

Source - CRISP

The term Molecular chaperone can be used for:

• chaperonin
• GroEL protein
• SecB protein
• unfoldase

Source: CRISP

Other terms that may be related to Molecular chaperone:

• protein folding
• stress protein

Source: CRISP

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• Medical Acronymns/Abbreviations

More Medical Dictionary Topics

Leukon

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