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

Topic mentions per year

Topic mentions per year

1984-2017
05010019842017

Papers overview

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Highly Cited
2010
Highly Cited
2010
We report a new vector, pEVOL, for the incorporation of unnatural amino acids into proteins in Escherichia coli using evolved… (More)
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Highly Cited
2009
Highly Cited
2009
Most protein mutations, and mutations that alter protein functions in particular, undermine stability and are therefore… (More)
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Highly Cited
2007
Highly Cited
2007
The microRNAs miR-1 and miR-133 are preferentially expressed in cardiac and skeletal muscles and have been shown to regulate… (More)
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Highly Cited
2005
Highly Cited
2005
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like… (More)
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Highly Cited
2002
Highly Cited
2002
The Archaeon Methanosarcina mazei and related species are of great ecological importance as they are the only organisms… (More)
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Highly Cited
2001
Highly Cited
2001
Heat shock proteins (HSPs) require no adjuvant to confer immunogenicity to bound peptides, as if they possessed an intrinsic… (More)
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Highly Cited
2000
Highly Cited
2000
Heat shock proteins (HSP), highly conserved across species, are generally viewed as intracellular proteins thought to serve… (More)
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Highly Cited
2000
Highly Cited
2000
BACKGROUND Work from our laboratory has proven that increased titers of anti-heat shock protein 60 (HSP60) antibodies are… (More)
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Highly Cited
1999
Highly Cited
1999
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that… (More)
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Highly Cited
1994
Highly Cited
1994
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally… (More)
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