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Stabilize partially unfolded proteins, preventing aggregation; found in the cytoplasm and in organelles like mitochondria.

Works to disaggregate and reactivate aggregated proteins, often functioning in tandem with the Hsp70 system.

Facilitate protein folding and quality control in the endoplasmic reticulum; BiP (Binding immunoglobulin Protein) is an example.

A prokaryotic molecular chaperone system that assists in protein folding, with DnaK as the Hsp70 homolog.

Enhances the import of proteins into mitochondria by interacting with mitochondrial chaperones.

Chaperonin found in eukaryotes that assists in the folding of actin, tubulin, and other cytosolic proteins.

Assist the main chaperones by modulating their activity and specificity; Hop (Hsp70-Hsp90 organizing protein) is an example.

Facilitates the stabilization and proper folding of proteins involved in signal transduction; present in the cytosol of eukaryotic cells.

Not a chaperone itself but a prokaryotic heat shock transcription factor that increases the synthesis of heat shock proteins, including chaperones.

Facilitate the folding of glycoproteins in the endoplasmic reticulum by binding to carbohydrate moieties.

ATPase associated with various cellular activities, involved in the extraction of misfolded proteins from the ER for degradation.

Captures and stabilizes unfolded proteins, delivering them to a larger chaperonin for folding.

Assists in protein folding and prevents aggregation; found across various cellular compartments such as the cytosol and endoplasmic reticulum.

Provide an isolated environment for proper protein folding; an example is GroEL/GroES in bacteria.