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1 ficantly from any known crystal structure of chaperonin 60.
2 n with cell wall LPS but also with cytosolic chaperonin 60.
3 ng we found that recombinant M. tuberculosis chaperonin 60.1 fails to form the prototypic tetradecame
4                    We have demonstrated that chaperonin 60.1 from this bacterium is a very active sti
5  demonstrated that Mycobacteria tuberculosis chaperonin 60.1 inhibits leucocyte diapedesis and bronch
6 at the signaling activity of M. tuberculosis chaperonin 60.1 resides in the equatorial domain.
7 etermine structure/function relationships of chaperonin 60.1 we have cloned and expressed the apical,
8 ric ring Plasmodium falciparum mitochondrial chaperonin 60 (Cpn60) bound with ATP, which differs sign
9 preparations of the higher plant chloroplast chaperonin 60 (cpn60) consist of roughly equal amounts o
10 ochondrial-like heat shock protein 70 and/or chaperonin 60 (cpn60) genes in trichomonads and microspo
11  in general also attach to the corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to
12 itated with IAP100 was identified as stromal chaperonin 60 (cpn60); the association of IAP100 and cpn
13 PCR targeting the 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infect
14  is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitoc
15 nd endocytosis of Escherichia coli, LPS, and chaperonin 60 (GroEL) as revealed by both FACS analysis
16 emonstrate that alpha-crystallin, along with chaperonin 60 (GroEL), was able to provide statistically
17                The major heat shock protein, chaperonin 60, has been established to have intercellula
18  form whose accumulation requires a specific chaperonin 60 isoform.
19 , the formation of which requires a specific chaperonin 60-kDa isoform.
20 m the prototypic tetradecameric structure of chaperonin 60 proteins under the conditions tested and o
21 a small proportion of bacteria to encode two chaperonin 60 proteins.
22 ished phylogenetic analyses of beta-tubulin, chaperonin 60, valyl-tRNA synthetase, and EF-1alpha, sug
23 hondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins a
24 l distending toxin (CDT); and (c) a secreted chaperonin 60 with potent leukocyte-activating and bone