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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

Related topics

Related topics

50 relations

Narrower (37)

BAG6 protein, ArabidopsisBAG6 protein, humanCDC37L1 protein, humanCesT protein, E coli

Broader (1)

Carrier Proteins
HSP40 Heat-Shock ProteinsHeat Shock Protein Beta-8Heat shock proteinsHeat-Shock Proteins 70

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2007
Highly Cited
2007
Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.
Highly Cited
2006
Highly Cited
2006
MUC1 oncoprotein is targeted to mitochondria by heregulin-induced activation of c-Src and the molecular chaperone HSP90
The MUC1 heterodimeric transmembrane glycoprotein is aberrantly overexpressed by most human carcinomas. The MUC1 C-terminal… 
Highly Cited
2006
Highly Cited
2006
Hydrophilic iminosugar active‐site‐specific chaperones increase residual glucocerebrosidase activity in fibroblasts from Gaucher patients
Gaucher disease is an autosomal recessive lysosomal storage disorder caused by the deficient activity of glucocerebrosidase… 
Highly Cited
2001
Highly Cited
2001
The chloroplastic GrpE homolog of Chlamydomonas: two isoforms generated by differential splicing.
In eubacteria and mitochondria, Hsp70 chaperone activity is controlled by the nucleotide exchange factor GrpE. We have identified… 
Highly Cited
2000
Highly Cited
2000
Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest.
The ansamycin antibiotics, herbimycin A (HA) and geldanamycin (GM), bind to a conserved pocket in heat shock protein 90 (Hsp90… 
Highly Cited
2000
Highly Cited
2000
Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone*
p23 is a co-chaperone for the heat shock protein, hsp90. This protein binds hsp90 and participates in the folding of a number of… 
Highly Cited
1997
Highly Cited
1997
Differential N-Glycan Patterns of Secreted and Intracellular IgG Produced in Trichoplusia ni Cells*
Structures of the N-linked oligosaccharide attached to the heavy chain of a heterologous murine IgG2a produced from Trichoplusia… 
Highly Cited
1995
Highly Cited
1995
Is NSF a fusion protein?
Highly Cited
1994
Highly Cited
1994
Hsp47 and the translation-translocation machinery cooperate in the production of alpha 1(I) chains of type I procollagen.
Highly Cited
1993
Highly Cited
1993
ATP induces large quaternary rearrangements in a cage-like chaperonin structure
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