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HSPD1 gene

Known as: HEAT-SHOCK 60-KD PROTEIN 1, heat shock protein family D (Hsp60) member 1, GroEL 
This gene plays a role in protein folding.
National Institutes of Health

Related topics

Related topics

6 relations
60 kDa Heat Shock Protein, MitochondrialChaperonin 60cellular response to unfolded proteinintracellular protein transport

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HSPD1 wt Allele

Papers overview

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Highly Cited
2005
Highly Cited
2005
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well… 
Highly Cited
2002
Highly Cited
2002
Molecular mechanisms of chaperonin GroEL-GroES function.
The dynamics of the GroEL-GroES complex is investigated with a coarse-grained model. This model is one in which single-residue… 
Highly Cited
2002
Highly Cited
2002
Inhibition of Adjuvant Arthritis by a DNA Vaccine Encoding Human Heat Shock Protein 601
Adjuvant arthritis (AA) is an autoimmune disease inducible in rats involving T cell reactivity to the mycobacterial 65-kDa heat… 
Highly Cited
1997
Highly Cited
1997
Molecular chaperones: towards a characterization of the heat-shock protein 70 family.
Highly Cited
1993
Highly Cited
1993
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
Chaperonins are oligomeric protein complexes that play an essential role in the cell, mediating ATP-dependent polypeptide chain… 
Highly Cited
1992
Highly Cited
1992
Positive cooperativity in the functioning of molecular chaperone GroEL.
Highly Cited
1992
Highly Cited
1992
Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation
WHEN bacterial or enkaryotic cells are exposed to high temperatures or other harsh conditions, they respond by synthesis of a… 
Highly Cited
1991
Highly Cited
1991
Mycobacterial heat‐shock proteins as carrier molecules
We have previously shown that the priming of mice with live Mycobacterium tuberculosis var. bovis (Bacillus Calmette‐Guérin, BCG… 
Highly Cited
1990
Highly Cited
1990
Regulation and sequence of the Synechococcus sp. strain PCC 7942 groESL operon, encoding a cyanobacterial chaperonin
The molecular chaperonins such as GroEL are now widely regarded as essential components for the stabilization of integral… 
Highly Cited
1982
Highly Cited
1982
Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo
The Escherichia coli groEL and groES gene products are essential for both phage morphogenesis and bacterial growth. Although the… 
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