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1 rates to cpn10 is possible in the absence of cpn60.
2 ubunit of the chloroplast chaperonin complex CPN60.
3  Plsp1 correlated with its dissociation from Cpn60.
4 by the equivalent region from the homologous cpn60-1 gene of Rhizobium leguminosarum.
5 le ring form in which both the GroEL and the Cpn60-1 proteins are found.
6 ng precise cross-over points, two regions in Cpn60-1 were defined which appeared to be critical for r
7  can complement for loss of the M. smegmatis cpn60.1 gene.
8 st that a peptide derived from mycobacterial Cpn60.1 has a long-lasting anti-inflammatory and immunom
9                             We show that the Cpn60.1 proteins, but not the Cpn60.2 proteins, can comp
10 cyte-stimulating activity of M. tuberculosis Cpn60.1 resides in the monomeric subunit and within this
11 tuberculosis expresses two chaperonins, one (Cpn60.1) dispensable and one (Cpn60.2) essential.
12 uberculosis heat shock protein 60 (Mtbhsp60, Cpn60.1, and Rv3417c) interacts with both TLR2 and TLR4
13                        We show here that the Cpn60.2 homologue from Mycobacterium smegmatis also fail
14               However, we also show that the Cpn60.2 proteins from both organisms can replace the ess
15   We investigated the oligomerization of the Cpn60.2 proteins using analytical ultracentrifugation an
16  show that the Cpn60.1 proteins, but not the Cpn60.2 proteins, can complement for loss of the M. smeg
17 peronins, one (Cpn60.1) dispensable and one (Cpn60.2) essential.
18        These results indicate cooperation of Cpn60 and cpSecA1 for proper membrane insertion of Plsp1
19 coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.
20  The deduced amino acid sequences of GroEL1 (cpn60) and GroES1 (cpn10) were in agreement with N-termi
21 a gene encoding one such protein, chaperonin CPN60, and have characterized its structure and expressi
22 al antibodies were developed to maize HSP70, cpn60, and HSP22.
23 we detected coimmunoprecipitation of IAP100, cpn60, and the imported mature form (S) of precursor.
24                      The molecular chaperone cpn60 binds many unfolded proteins and facilitates their
25                                              Cpn60 bound Plsp1 in the stroma.
26 dium falciparum mitochondrial chaperonin 60 (Cpn60) bound with ATP, which differs significantly from
27 ng Cpn60's obligate substrate RbcL displaced Cpn60-bound Plsp1; then, the released Plsp1 exhibited in
28 her, the binding of a hydrophobic surface to cpn60 can induce further exposure of complementary surfa
29 rgeting experiments support a model in which Cpn60 captures and then releases insertion-competent Pls
30 le 700-kDa complex that co-migrated with the Cpn60 complex before inserting into the membrane.
31 urther exposure of complementary surfaces on cpn60 complexes, thus amplifying interactions available
32  the higher plant chloroplast chaperonin 60 (cpn60) consist of roughly equal amounts of two divergent
33    A flexible region, known to interact with cpn60, extends from the lower rim of the dome.
34 investigated how the chloroplast chaperonin (Cpn60) facilitated the thylakoid integration of Plastidi
35 on (PCR) assays were developed targeting the cpn60 gene of species groups including G. vaginalis, G.
36 ous interpretation of these data is that the cpn60 gene was transferred from the endosymbiotic ancest
37  heat shock protein 70 and/or chaperonin 60 (cpn60) genes in trichomonads and microsporidia imply tha
38 tates substrate folding when in complex with cpn60 (GroEL in E. coli).
39                        Entamoeba histolytica CPN60 has an amino-terminal extension reminiscent of kno
40 his report, we describe a mitochondrial-like cpn60 homolog from the diplomonad parasite Giardia lambl
41 hylogenetic analyses position the G. lamblia cpn60 in a clade that includes mitochondrial and hydroge
42  provides new insights into the mechanism of Cpn60 in chaperonin assembly and function.
43 the exposed hydrophilic face did not bind to cpn60 in either the oxidized or reduced states.
44                             Thus, binding to cpn60 is favored by a secondary structure that organizes
45  Western blots reveal that the expression of cpn60 is independent of cellular stress and, except duri
46      Deletion of the first 15 amino acids of CPN60 leads to an accumulation of the truncated protein
47  have been used to probe the question of how cpn60 might recognize such a diverse set of unfolded pro
48 cloned the alpha and beta subunits of the ch-cpn60 of pea (Pisum sativum), expressed them individuall
49  envelope membrane (Toc159), stromal (hsp93, cpn60), or thylakoid (LHCP, OE23) proteins were not incr
50                               We show that a Cpn60 protein from the bacterium Rhizobium leguminosarum
51                                    Bacterial Cpn60 proteins (homologues to the Escherichia coli GroEL
52  (42 degrees C for 4 h), levels of HSP70 and cpn60 proteins did not change significantly.
53 nsduced into strains expressing heterologous Cpn60 proteins, to test for complementation at any tempe
54 at includes mitochondrial and hydrogenosomal cpn60 proteins.
55  E. histolytica organelle housing chaperonin CPN60 represents a mitochondrial remnant.
56 axonomic marker genes (e.g. 16S/18S/ITS/rpoB/cpn60) represents the leading method for identifying a w
57  seven housekeeping genes, gltA, gdhB, recA, cpn60, rpoD, gyrB, and gpi, with that of sequence-based
58                                  Introducing Cpn60's obligate substrate RbcL displaced Cpn60-bound Pl
59 he 16S rRNA-encoding gene and chaperonin-60 (cpn60) showed that the plants were infected with phytopl
60 that Aacpn10 has molecular interactions with cpn60 similar to other cpn10s.
61  pathogen in Mexico, we designed an array of cpn60-targeted molecular diagnostic assays for SbGP/MPV
62 100 was identified as stromal chaperonin 60 (cpn60); the association of IAP100 and cpn60 was specific
63 ein, we have localized native E. histolytica CPN60 to a previously undescribed organelle of putative
64 ane proteins in the stroma can interact with Cpn60 to shield themselves from the aqueous environment.
65 o attach to the corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to facilitate its
66 molecular chaperones DnaK (HSP70) and GroEL (cpn60) using two-dimensional sodium dodecyl sulfate-poly
67 ferentiating it from other known phytoplasma cpn60 UT sequences, while identifying a double infection
68                      These results suggested Cpn60 was an intermediate in thylakoid targeting of Plsp
69 ids, the integration of Plsp1 decreased when Cpn60 was present in excess of cpSecA1, the stromal moto
70 in 60 (cpn60); the association of IAP100 and cpn60 was specific and was abolished when immunoprecipit
71 When the Plsp1 residues that interacted with Cpn60 were removed, Plsp1 did not integrate into the mem
72 duce the exposure of hydrophobic surfaces on cpn60, whereas the same peptide in its random coil form
73 Kd = approximately 106 microM for binding to cpn60, whereas there was no detectable binding of the re