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HSPE1 gene

Known as: CPN10, HSP10, heat shock protein family E (Hsp10) member 1 
National Institutes of Health

Related topics

Related topics

2 relations
Chaperonin 10

Broader (1)

early pregnancy factor

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2005
Review
2005
The unusual chaperonins of Mycobacterium tuberculosis.
Highly Cited
2000
Highly Cited
2000
Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding*
Unlike the GroEL homologs of eubacteria and mitochondria, oligomer preparations of the higher plant chloroplast chaperonin 60… 
Highly Cited
1998
Highly Cited
1998
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
The ATPase cycle of GroE chaperonins has been examined by transient kinetics to dissect partial reactions in complexes where… 
Highly Cited
1997
Highly Cited
1997
Correlates of extra-pair fertilization success in hooded warblers
Abstract We examined correlates of extra-pair fertilization (EPF) success in the hooded warbler (Wilsonia citrina), a species… 
Highly Cited
1996
Highly Cited
1996
A synthetic 10‐kD heat shock protein (hsp10) from Mycobacterium tuberculosis modulates adjuvant arthritis
The heat shock protein, hsp10, is an abundant protein in Mycobacterium tuberculosis (Mtb), its nucleotide sequence encoding a… 
Highly Cited
1994
Highly Cited
1994
The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding
Highly Cited
1993
Highly Cited
1993
Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES
Highly Cited
1993
Highly Cited
1993
Refolding of barnase in the presence of GroE.
The refolding of barnase in the presence of GroEL has been monitored on the millisecond to seconds time scale using stopped-flow… 
Highly Cited
1993
Highly Cited
1993
GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
Highly Cited
1992
Highly Cited
1992
Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.
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