1 n with cell wall LPS but also with cytosolic chaperonin 60.

2 ng we found that recombinant M. tuberculosis chaperonin 60.1 fails to form the prototypic tetradecame

3                    We have demonstrated that chaperonin 60.1 from this bacterium is a very active sti

4 at the signaling activity of M. tuberculosis chaperonin 60.1 resides in the equatorial domain.

5 etermine structure/function relationships of chaperonin 60.1 we have cloned and expressed the apical,

6 preparations of the higher plant chloroplast chaperonin 60 (cpn60) consist of roughly equal amounts o

7 ochondrial-like heat shock protein 70 and/or chaperonin 60 (cpn60) genes in trichomonads and microspo

8  in general also attach to the corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to

9 itated with IAP100 was identified as stromal chaperonin 60 (cpn60); the association of IAP100 and cpn

10 PCR targeting the 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infect

11  is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitoc

12 nd endocytosis of Escherichia coli, LPS, and chaperonin 60 (GroEL) as revealed by both FACS analysis

13 emonstrate that alpha-crystallin, along with chaperonin 60 (GroEL), was able to provide statistically

14                The major heat shock protein, chaperonin 60, has been established to have intercellula

15  form whose accumulation requires a specific chaperonin 60 isoform.

16 , the formation of which requires a specific chaperonin 60-kDa isoform.

17 m the prototypic tetradecameric structure of chaperonin 60 proteins under the conditions tested and o

18 a small proportion of bacteria to encode two chaperonin 60 proteins.

19 ished phylogenetic analyses of beta-tubulin, chaperonin 60, valyl-tRNA synthetase, and EF-1alpha, sug

20 hondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins a

21 l distending toxin (CDT); and (c) a secreted chaperonin 60 with potent leukocyte-activating and bone