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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

Papers overview

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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… Expand
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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… Expand
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Review
2004
Review
2004
Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many… Expand
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Review
2004
Review
2004
The availability of a large number of complete genome sequences raises the question of how many genes are essential for cellular… Expand
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Review
2000
Review
2000
A large variety of stress conditions including physicochemical factors induce the synthesis of more than 20 heat shock proteins… Expand
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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… Expand
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Review
1993
Review
1993
T URNOVER OF AB ERR ANT PROT EINS IN E. COLI . . . . . . . . . . . . . . . . . 445 The Lon Protease… Expand
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Highly Cited
1992
Highly Cited
1992
The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70… Expand
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Highly Cited
1990
Highly Cited
1990
By analysis of a temperature-sensitive yeast mutant, a heat-shock protein in the matrix of mitochondria, mitochondrial hsp70… Expand
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Highly Cited
1989
Highly Cited
1989
The products of the groES and groEL genes of Escherichia coli, constituting the groE operon, are known to be required for growth… Expand
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