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Molecular Chaperones

Known as: Chaperone, Chaperone, Molecular, Molecular Chaperones [Chemical/Ingredient] 
Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport… 
National Institutes of Health

Papers overview

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Highly Cited
2004
Highly Cited
2004
Heat shock (HS) proteins (Hsps) function in tissue protection through their chaperone activity and by interacting with cell… 
Highly Cited
2001
Highly Cited
2001
One of the central tenets in neuroscience has been that the protein constituents of distal compartments of the neuron (e.g., the… 
Highly Cited
2000
Highly Cited
2000
The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90… 
Highly Cited
1999
Highly Cited
1999
Hsp70 family members together with their Hsp40 cochaperones function as molecular chaperones, using an ATP-controlled cycle of… 
Highly Cited
1997
Highly Cited
1997
Structures of the N-linked oligosaccharide attached to the heavy chain of a heterologous murine IgG2a produced from Trichoplusia…