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GroEL-GroES complex

Known as: GroEL-GroES complex location 
Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The… Expand
National Institutes of Health

Papers overview

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2014
2014
Protease from Serratia proteamaculans (PSP) is the first known psychrophilic oligopeptidase B. The gene of S. proteamaculans 94… Expand
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2012
2012
BackgroundD-phenylglycine aminotransferase (D-PhgAT) of Pseudomonas stutzeri ST-201 catalyzes the reversible stereo-inverting… Expand
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2009
2009
Human phospholipid scramblase 1(hPLSCR1), when expressed in E. coli (BL-21 DE3), forms inclusion bodies that are functionally… Expand
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2007
2007
SummarySome (perhaps all) plant viruses transmitted in a circulative manner by their insect vectors avoid destruction in the… Expand
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2007
2007
Chaperonins cpn60 and cpn10 are essential proteins involved in cellular protein folding. Plant chloroplasts contain a unique… Expand
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2006
2006
Bacterial chaperonin GroEL with a molecular mass of 800 kDa was studied by (13)C NMR spectroscopy. Carbonyl carbons of GroEL were… Expand
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2004
2004
The appropriate conditions to switch on the heat shock promoters in Corynebacterium glutamicum were defined by Northern blot… Expand
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2003
2003
The GroES protein from Escherichia coli is a well-known member of the molecular chaperones. GroES consists of seven identical 10… Expand
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1997
1997
The interaction of GroEL with urea-unfolded dihydrofolate reductase (DHFR) has been studied in the presence of DHFR substrates by… Expand
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