1 GST moiety and removal of tightly associated GroEL protein.

2 ng for an important functional region of the GroEL protein.

3 ied that annexin A2 possibly interacted with GroEL protein.

4 pable of producing more than 100 mg/L mutant GroEL protein.

5                                              GroEL protein and groEL mRNA transcript were up-regulate

6                                              GroEL protein and mRNA levels were elevated in cells exp

7 nd, most notably, the amounts of DnaK and of GroEL protein are reduced.

8 proteins (homologues to the Escherichia coli GroEL protein) are often examined for function by testin

9 on of a diffraction pattern from an isolated GroEL protein complex Ekeberg T et al. (Light Sci Appl 1

10  Coimmunoprecipitation assays confirmed that GroEL proteins could bind to annexin A2, and confocal an

11 ene, the effects of progressive depletion of GroEL protein from E. coli cells can also be monitored a

12             In this study, we found that the GroEL protein (heat shock protein 60) of Mycoplasma gall

13 n was significantly induced by a recombinant GroEL protein in PBMCs, and knocking down annexin A2 exp

14                                          The groEL protein is part of the groESL operon and enables a

15 isation of an active single-ring form of the GroEL protein (SR-A92T), which has an exceptionally low

16 e, we show using computational analysis that GroEL protein substrates have a bimodal distribution of

17                                 The purified GroEL protein was shown to adhere to peripheral blood mo