Publication for HSPD1 and HSPE1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	HSPD1	heat shock protein family D (Hsp60) member 1	3329			[link]
hsa	HSPE1	heat shock protein family E (Hsp10) member 1	3336

Pubmed ID	Priority	Text
29415503	0.98	HSP60/HSP10 (Figure 6).
	0.97	HSP10 binds to HSP60 in the presence of ATP, which increased the HSP60 double-ring formation.
	0.97	HSP60/HSP10 undergoes an ATP-dependent transition between the single- and double-rings in their system that is highly distinctive from the GroEL/GroES system particularly in the manner of complex formation and the roles of ATP binding and hydrolysis in the reaction cycle.
	0.97	HSP10 (at HSP10/HSP60 ratio = 0), suggesting that the double-ring HSP60 content was 50%.
	0.97	HSP10 and ATP to HSP60 further increased the I(0)/C value, and HSP60-containing molecules were estimated to be mostly double rings in the presence of HSP10 (at HSP10/HSP60 ratio = 1).
	0.97	HSP10 and ATP increased the value of HSP60 more than that of GroEL/GroES bullet complex.
	0.97	HSP60 and HSP10, a protease sensitivity assay was performed at a co-chaperone/chaperonin single-ring ratio of 1.0.
	0.97	HSP60 becomes competent to bind to HSP10 in the presence of ATP but not in the presence of ADP or the non-hydrolyzable analogues of ATP.
	0.97	HSP60 associates with HSP10 (step b).
	0.96	GroEL induces the formation of GroEL/GroES complex to form a cavity for encapsulation of substrates.
	0.96	HSP60/HSP10 which associated with HSP10 by ATP or AMP-PNP.
	0.95	HSP60 released the HSP10 and the dissociation of the double-ring to single-rings occurred.
	0.95	HSP60 double-ring formation and HSP60/HSP10 complex formation under more physiological conditions, we analyzed these complexes and GroEL/GroES complexes as a control in solution by SAXS (Figure 2A,B).
	0.95	GroEL/GroES by facilitating the dissociation of ADP from the trans-ring and overcoming the inter-ring negative cooperativity.
	0.95	GroES and ADP and the subsequent dissociation into two HSP60 single rings.
	0.95	GroEL/GroES, the reaction scheme of the HSP60/HSP10 system includes the transition between double-ring and single-ring.
	0.94	HSP60/HSP10 complex is similar to that of GroEL with two GroES, this result suggested that the HSP60/HSP10 complex forms the football complex.
	0.94	HSP60-HSP10 binding ratio in the presence of ATP was 86.8%, and this value was dramatically higher than that in the presence of the other nucleotides or the absence of nucleotides.
	0.94	HSP60/HSP10 Complex Dissociates after ATP Was Hydrolyzed
	0.94	HSP60 (upper) or HSP60/HSP10 (lower) in the presence (right) or absence (left) of 1 mM ATP.
	0.94	HSP60/HSP10 and GroEL/GroES complex under the various nucleotide conditions.
	0.93	HSP10 unlike the GroEL/GroES system.
	0.93	HSP60(D398A) showed that most of them readily formed football-type complexes with HSP10 in the presence of ATP without forming a single-ring (Figure 4D).
	0.93	GroEL/GroES bullet when the trans-ring is occupied by ADP, which results in the prevention of football complex formation.
	0.93	HSP60/HSP10 may be suitable in mammalian mitochondria in which nascent proteins are constantly produced unlike bacteria which could fall into a resting state by starvation or low temperature.
	0.92	GroEL/GroES also can be detected as football-type complexes under various non-physiological conditions.
	0.92	HSP60 alone (left) or HSP60/HSP10 (right) in the presence of 1 mM adenosine diphosphate (ADP).
	0.91	HSP10 and ADP did not significantly increase the I(0)/C value of HSP60 as well as the absence of nucleotides although the addition of GroES and ADP increased the value of GroEL.
	0.91	HSP60 Stably Interacts with HSP10 and Forms a Football-Type Complex
	0.90	HSP10 with HSP60.
	0.90	HSP60, it also induced stabilization of the conformation by HSP10 binding which is required to form stable football-type complexes.
	0.89	HSP60 decreased by HSP10 as in the GroEL/GroES system (Figure 4A).
	0.89	HSP10 stably associated with HSP60(D398A) more than wild-type HSP60 (Figure 4B).
	0.88	HSP60/HSP10 complex easily forms a football complex in contrast to the GroEL/GroES complex.
	0.85	GroEL/GroES complexes, the molecular structure and function of the chaperonin homolog, heat shock protein, HSP60/HSP10, has remained unclear.
	0.85	HSP60/HSP10, GroES became resistant (~50%) to protease digestion in the presence of ADP, ATPgammaS and AMP-PNP (Figure 3A, lanes 10-12).
	0.85	GroEL/GroES and HSP60/HSP10.
	0.85	HSP60/HSP10 in the presence of various nucleotides including ATP, ADP, Adenosine-5'-(beta, gamma-imido)-triphosphate (AMP-PNP) and Adenosine 5'-(gamma-thio)-triphosphate (ATPgammaS); (D) I(0)/C values of HSP60 (solid circle) and GroEL (open circle) in the presence of various concentrations of co-chaperones under the nucleotide-free (Blue), 1 mM ATP (Red) or ADP (Green) conditions; (E) Rg values of HSP60 (solid circle) and GroEL (open circle) in the presence of various concentrations of co-chaperones under the conditions indicated were analyzed by a Guinier plot.
	0.83	HSP60 in the absence of nucleotides indicated that the addition of HSP10 had no effect on the overall structure (Figure 2A).
	0.83	HSP10 associates with HSP60 in the presence of ATP but not in the presence of ADP nor the non-hydrolyzable analogues of ATP.
	0.82	HSP60 did not bind HSP10 by AMP-PNP although porcine HSP60 bound HSP10 and a protein folding reaction was promoted.
	0.80	HSP60 stably interacts with HSP10 and forms the football-type complex.
	0.79	HSP60 exist as a significant number of double-ring complexes (football- and bullet-type complexes) and a small number of single-ring complexes in the presence of ATP and HSP10.
	0.79	HSP60/HSP10 forms the football-type complex much more easily than does GroEL/GroES.
	0.79	HSP10 and forms double-rings in the presence of ADP though wild type (WT) HSP60 did not, as shown in our study.
	0.74	HSP60 and HSP10 rings during dynamic interaction in solution, we employed a fluorescence cross correlation spectroscopy (FCCS) analysis in the presence of various nucleotides.
	0.72	HSP60 and subsequent release of HSP10, the equatorial domain changes its conformation and these interactions would be lost.
	0.67	HSP60, and co-chaperonin, HSP10, play an essential role in protein folding by capturing unfolded proteins in the HSP60/HSP10 complex.
	0.65	HSP60 were changed by the addition of ATP and HSP10.
	0.63	HSP60(D398A) also migrated as a single-ring in the presence of ATP, HSP60(D398A) migrated as a double-ring in the presence of ATP and HSP10 (Figure 4C, lane 4).
	0.62	HSP10/single ring HSP60 ratio = 2); (D) GroEL with GroES in the presence (right) and absence (left) of 1 mM ATP.
	0.61	HSP60 and HSP10 Was Induced by Only ATP
	0.60	GroEL/GroES.
	0.57	HSP60 and HSP10 purified from porcine formed football-type and bullet-type complexes in the presence of ATP.
	0.55	HSP60/HSP10 or GroEL/GroES under nucleotide-free, 1 mM ATP, ADP, AMP-PNP or ATPgammaS condition.
	0.54	HSP60-containing complexes possess the HSP60 double-ring structure and suggest that the ATP-dependent HSP60 double ring is stabilized by HSP10 binding.
	0.51	HSP60/HSP10 complex observed in the presence of 1 mM adenosine triphosphate (ATP).
26585937	0.98	GroEL and GroES.
	0.98	GroEL-GroES.
	0.97	GroEL-GroES (Fig. 3a).
	0.97	GroEL-GroES significantly accelerated CCR5 folding as indicated above (Fig. 3c), the folding rate became considerably slower with the addition of both the chaperonin complex and DMPHBA (a value of 9.1 x 10-3 min-1 was estimated from the data) (Fig. 3d).
	0.97	GroEL-GroES, respectively, and these values changed to be 0.22 and 0.52 with supplied albumin (Fig. 4).
	0.97	GroEL-GroES and CCR5-rubredoxin are rendered at different scales.
	0.96	GroEL-GroES are typically defined by their ability to assist the folding and assembly of proteins in a catalytic and non-consumptive manner.
	0.96	GroEL-GroES to the cell-free reaction significantly accelerated the folding rate of CCR5 to 0.3 min-1, which is approximately 36 x faster (Fig. 3c).
	0.96	GroEL-GroES on the folding of newly translated CCR5, inhibition experiments were also performed with the addition of 5-(2,5-dimethyl-pyrrol-1-yl)-2-hydroxy-benzoic acid (DMPHBA), a chemical inhibitor of the GroEL-GroES-mediated protein folding, to the cell-free reaction mixture.
	0.96	GroEL-GroES in this cell-free system, if any, and its effect on the folding of CCR5 are negligible.
	0.96	GroEL alone can decrease the digestion rate by approximately 2x and that the addition of GroEL-GroES can further decrease the digestion rate by almost 4x.
	0.96	GroEL-GroES was added to the cell-free synthesis system.
	0.96	GroEL typically works with its lid GroES to mediate the folding of substrate proteins.
	0.96	GroEL-GroES chaperonin complex significantly promoted the efficiency and kinetics of the folding of newly translated CCR5.
	0.96	GroEL-GroES, the apparent rate constant increased 36x, requiring approximately 3 minutes to fold, which is much more reasonable for CCR5 to become functional.
	0.96	GroEL-GroES chaperonin complex and CCR5-rubredoxin.
	0.95	GroEL only and with the addition of GroEL-GroES, respectively.
	0.95	GroEL alone can be sufficient to assist the folding of proteins without the cooperation of GroES.
	0.95	GroEL-GroES suggest that the presence of GroES can further promote the folding of CCR5.
	0.95	GroEL-GroES indicates that the folded states are different in the absence of GroEL-GroES.
	0.95	GroEL-GroES inhibitor), (c) GroEL-GroES, or (d) GroEL-GroES and DMPHBA.
	0.94	GroEL-GroES may be implicated in the folding of membrane proteins.
	0.94	GroEL-GroES plays an important role in CCR5 folding and can significantly increase the rate and efficiency of folding.
	0.94	GroEL-GroES, proteolysis would be expected to be the same for the slow phase.
	0.94	GroEL-GroES folding time of CCR5 (~3 min) is an order of magnitude longer than that reported for water-soluble proteins (~10 s).
	0.92	GroEL-GroES on the folding rates of newly translated CCR5 was measured using a methodology developed by Mallam and Jackson.
	0.91	GroEL-GroES, with a low folding rate and yield, as well as a reduction in binding affinity and structural stability.
	0.91	GroEL-GroES on this process.
	0.91	GroEL-GroES, which corresponds to the amplitude of the fast phase of proteolysis, although the relative amount was considerably decreased.
	0.91	GroEL are shown in green and yellow, and GroES is shown in orange.
	0.90	GroEL-GroES displayed a lower binding affinity, assuming that some folding intermediates or partially folded CCR5 also bind the ligand but with a weaker affinity than that of the native receptor.
	0.88	GroEL-GroES is directly examined.
	0.88	GroEL-GroES.
	0.88	GroEL-GroES, folding was markedly accelerated and more efficient.
	0.87	GroEL-GroES can greatly facilitate the folding of nascent CCR5 chains by increasing the rate and yield of functional folding.
	0.87	GroEL-GroES to the cell-free system, the half-life for the folding of newly translated CCR5 was determined to be approximately 85 min.
	0.87	GroEL-GroES requires further investigation.
	0.85	GroEL-GroES, but the slower phase is notably different.
	0.85	GroEL-GroES, which is consistent with the results of the CCR5 ligand-binding experiments.
	0.85	GroEL consists of fourteen identical subunits arranged in a pair of seven-membered rings that are stacked back-to-back to form a double doughnut-like cylindrical structure, and GroES consists of seven identical subunits arranged to form a domed disk (PDB 1SVT).
	0.84	GroEL-GroES, indicating full inhibition of the added chaperonin complex by DMPHBA.
	0.77	GroEL-GroES towards membrane proteins, which highlights the mechanistic flexibility and substrate diversity of GroEL-GroES.
	0.67	GroEL-GroES by measuring the kinetics of CCR5 proteolysis by subtilisin (Fig. 4).
	0.67	GroEL alone on the expression, folding kinetics, structural stability and biological activity of soluble CCR5 to assess the role of GroES in the folding of newly translated CCR5.
	0.65	GroEL was partially effective on its own, but for maximum efficiency both the GroEL and its GroES lid were necessary.
	0.55	GroEL-GroES added to the cell-free reaction were compared.
16253146	0.98	HSP60, in both primary tumour and lymph node metastasis, is correlated with the tumoral grade, while the HSP10 expression is not.
	0.98	HSP10 are commonly higher than the levels of HSP60.
	0.98	HSP60 and HSP10 in a series of LBC with lymph node metastases, and the immunolocalisation of these molecules in the different compartments of reactive lymph nodes.
	0.98	HSP60 and HSP10 in some carcinogenic models, in particular, both pre-tumoral (dysplastic) and neoplastic lesions of large bowel, as well as uterine exocervix and prostate gland has been investigated previously.
	0.98	HSP60, but not for HSP10, was correlated with the presence of lymph node metastasis and this data may have a histopathologic value.
	0.98	HSP60 and HSP10, in normal epithelia, are under the antibody detection threshold for immunohistochemical analyses, while neoplastic elements show a strong cytoplasmic expression of these proteins.
	0.97	HSP60 and HSP10 in a series of large bowel carcinomas and locoregional lymph nodes with and without metastases.
	0.97	HSP60 and HSP10.
	0.97	HSP60 and HSP10 in the secondary follicles, and for HSP10 in the medullary sinuses, when compared with hyperplastic lymph nodes.
	0.97	HSP60 and HSP10 may have diagnostic and prognostic significance in the management of this tumour and their overexpression in tumoral cells may be functionally related to tumoral progression.
	0.97	HSP60 and HSP10 in a series of carcinogenetic models, such as the "dysplasia-carcinoma" sequences of uterine exocervix, large bowel and prostate.
	0.97	HSP60 and HSP10 were studied in a series of advanced large bowel carcinomas (LBC) with lymph node metastases.
	0.97	HSP60 and HSP10 positivity in primitive versus metastatic tumours of different grade
	0.97	HSP60 in Ti and Ni was found to be dependent on the tumoral grade, while the expression of HSP10 was not.
	0.97	HSP60/HSP10 complex in preventing the activation of the apoptotic machinery.
	0.97	HSP10 in MS of MLN could support the hypothesis that this molecule, following unknown biological stimulations, acts independently from HSP60.
	0.96	HSP60 and HSP10 and that the release of mitochondrial HSP may also accelerate caspase activation in the cytoplasm of intact cells.
	0.96	HSP60 and/or HSP10 without any apparent metastasis should be examined in detail, since this observation may reflect an increased likelihood of finding a micrometastasis.
	0.96	HSP60 and HSP10 positivity may help to detect more aggressive tumors.
	0.95	HSP60 and HSP10 in large bowel carcinomas with lymph node metastase
	0.95	HSP60 and HSP10.
	0.95	HSP60 and HSP10 in a series of human lymph nodes were evaluated.
	0.95	HSP60 and HSP10 increased significantly in MLN, when compared to HLN.
	0.94	HSP60 positive cells was higher in the G3 group (mean: 70%) compared with the G1 (mean: 35%) (fig. 2a), while a similar number of HSP10 positive elements were present in both groups (mean: respectively 74% and 75%) (fig. 2b).
	0.94	HSP60 and HSP10 positive elements in secondary follicles could also be considered diagnostic to predict the presence of lymph node metastases.
	0.93	HSP60 and HSP10 might be considered as new diagnostic and prognostic tools for these cancers, being involved in the molecular steps of carcinogenesis, analogously to what has already been demonstrated with other tumours.
	0.93	HSP60 and HSP10.
	0.93	HSP10, but not HSP60, positive cells, when compared to the MS of HLN, we could assume that HSP10 in this site is under unknown stimulation inducing its overexpression, for functional roles, i.e. cell proliferation.
	0.93	HSP60 and HSP10, working together, could protect mitochondrial function and prevent apoptotic cell death although some studies have shown that these molecules do not always act as a single functional unit in vivo.
	0.92	HSP60 and HSP10 should be functionally correlated, HSP10 is present in a higher number of specimens and with a higher expression than HSP60.
	0.90	HSP10 and HSP60 was investigated in a series of normal human bone marrows, similar data were found.
	0.89	HSP60 and 13% for HSP10.
	0.89	HSP60 and HSP10 are up-regulated in cancer for extramitochondrial functions, i.e. in the block of the apoptotic machinery that usually takes place during cancer development and progression.
	0.87	HSP60 and HSP10 are two chaperones that interact in a two-step folding mechanism in the mitochondria of prokaryotic and eukaryotic cells.
	0.81	HSP60 positive cells in G1 and G3 LBC was significant (p < 0.0005), while statistic difference was not found in HSP10 positivity (p > 0.05).
	0.77	HSP60 (p > 0.05) and HSP10 (p > 0.1).
	0.71	HSP60 (p < 0.005) and HSP10 (p < 0.001) in lymph nodes.
	0.62	HSP60 (fig. 6a) and HSP10 (fig. 6b) in the cells of all reactive lymph node compartments was commonly localised in the cytoplasm.
	0.56	HSP60 (a) and HSP10 (b) show cytoplasmic positivity.
23875653	0.98	GroES alignment and 505 sequences based GroEL alignment, representing the 6 major bacterial groups.
	0.97	groES and groEL were performed building pairs of files for each group of bacteria, both of which included the same bacterial strains.
	0.97	GroES and GroEL are the most central in the coevolution network (Additional file 1: Figure S1a to c).
	0.97	GroES and GroEL is essential to induce the conformational changes needed for the folding cycle.
	0.96	GroEL, GroES and between both these proteins.
	0.96	GroEL and GroES, we first conducted a coevolutionary analysis to determine the network of residues dependencies in all bacteria.
	0.96	GroES and GroEL.
	0.96	GroEL (c) identifies amino acid sites which are involved in the interaction with GroES and protein substrates (blue spheres in the structure of GroEL: d) sites involved in the inter-subunit GroEL contacts and and substrate folding in the ring cavity (red spheres), residues with a role in ATP hydrolysis (green sphere) and those mapping to the inter-ring interfaces (black spheres).
	0.96	GroES and GroEL.
	0.95	GroES is shown using the three-letter amino acid code (a) Sites coevolving within GroES were divided into two main structure clusters (b) One cluster includes two amino acid sites (blue spheres), which are involved in the interaction with GroEL.
	0.95	GroES-L. Functional shifts in GroEL have been previously documented and linked to events of GroEL gene duplication and to changes in the organismal lifestyle.
	0.93	GroES and GroEL in the different bacterial clades (colour coded circles) and compared involved residues with those identified across the entire bacterial phylogeny (stars).
	0.93	GroES and GroEL provide information on the structural consequences of their interaction
	0.92	GroEL, according to which changes in the amino acid composition of its co-chaperonin GroES can determine GroEL functioning as a single instead of double ring.
	0.92	GroES coevolving with GroEL (Figure 2a).
	0.91	GroES and GroEL, we searched groE sequences amongst the major bacterial Phyla and found that Actinobacteria, Cyanobacteria, Bacteroidetes and Chlorobi, Firmicutes, Proteobacteria, and Spirochaetes comprised a number of groE homologs that would allow accurate inference of coevolution.
	0.91	GroEL is shown in the X-axis, while this distribution in GroES is shown in the Y-axis.
	0.91	GroES amino acid regions coevolving with residues from GroEL are all located in the interface between the GroES subunits.
	0.90	GroES, GroEL and between both these proteins.
	0.90	GroEL residues coevolving with GroES are distributed among the three domains, apical, intermediate and equatorial.
	0.88	GroEL subunits, with each subunit being divided into three domains: the apical, which binds unfolded proteins and GroES, the intermediate, which acts as a hinge allowing the movement of the apical domain as well as the transition between trans and cis conformations needed for GroEL function, and the equatorial which is responsible for the ATPase and the folding activities that take place in the central cavity of the ringed complex.
	0.88	GroEL, and its co-chaperonin GroES, offer a unique system to test this hypothesis because, despite its essentiality to the cell, this protein has evolved many alternative functions in other bacteria.
	0.84	GroES and GroEL from the same set of bacterial strains (381 sequences for GroES and GroEL).
	0.80	GroES and GroEL, coevolving amino acids formed structural clusters within GroESL (Figure 2b).
	0.77	GroES and GroEL as well as between both these interacting proteins uncover a complex network of evolutionary dependencies among amino acid sites.
	0.76	GroES and GroEL.
	0.73	GroES and GroEL, also known as cpn10 and cpn60 respectively, are expressed at constitutive levels under physiological conditions and their expression increases at high temperatures, allowing the growth and survival of bacteria at a broad range of temperatures.
	0.71	GroES and GroEL for each of the bacterial groups examined in this study.
	0.69	GroEL sites, Ala260 and Arg268, are involved in the binding of substrates and overlap with sites involved in GroES binding as well.
	0.68	GroES and GroEL.
	0.66	GroES and GroEL in bacteria
	0.61	groES genes, and 12 and 278 for groEL genes belonging to Spirochaetes and Proteobacteria groups, respectively (Table 1).
	0.61	GroES and GroEL, respectively).
	0.61	GroEL coevolving with sites from GroES were centred in the apical and equatorial domains (Figure 3).
	0.58	GroES is heavily involved in determining the function of GroEL as a single or as a double ring, the coevolution of Glu461 from GroEL with GroES amino acid sites may have implications in the structural stability of the double ring, and thus, GroES-GroEL folding cycle.
	0.58	GroES and GroEL (Additional file 5: Figure S5) were not detected in intra-protein coevolution analyses, and thus, were not the result of indirect evolutionary dependencies.
	0.58	GroEL and GroES.
	0.54	GroES and GroEL identifies 7 residues from GroES and 8 from GroEL (a) Structural mapping of coevolving residues reveals the functional importance of coevolving residues (b) residues coevolving between both proteins belong to substrate binding regions, inter-subunit and inter-ring contacts.
27493521	0.98	GroEL binds to GroES.
	0.98	GroES binding to SR1, which enables SR1 to fold substrate proteins in an iterative manner as GroEL does.
	0.98	GroEL is compacted upon GroES binding and is subsequently extended by folding into its native state.
	0.97	GroEL, GroEL binds GroES and undergoes conformational changes to form a large hydrophilic cavity (the chaperonin cage) in which a denatured protein is encapsulated (Fig. 1B).
	0.97	GroEL for DMMBP, even though about 90% of denatured DMMBP escaped out of the SR1 cage, suggesting that the recapture of denatured DMMBP by GroEL and the subsequent binding of GroES on the DMMBP-bound GroEL ring are very rapid and do not accelerate or decelerate the folding rate.
	0.97	GroEL by ATP hydrolysis without GroES cannot fold rapidly.
	0.96	GroES, a lid of the cavity, has seven mobile loops that interact with the hydrophobic surfaces of GroEL.
	0.96	GroES binding and release from GroEL, coupled with ATP hydrolysis, complicates the analysis of the folding reaction in the chaperonin cage.
	0.94	GroEL upon GroES/ATP binding.
	0.94	GroES/polypeptide binding surfaces of three GroEL subunits could be reserved for the binding of the denatured protein, since GroEL or GroES oligomers containing up to three binding-defective subunits, whose residues interacting with the GroES/polypeptide binding surface are mutated, can mediate protein folding.
	0.91	GroEL and GroES binding.
	0.90	GroES and ATP binding to the complex formed between GroEL and the denatured protein, the denatured protein is encapsulated inside the chaperonin cage and the protein folding reaction starts.
	0.90	GroEL (left, PDB:1OEL) and GroEL-GroES-ADP complex (right, PDB:1AOL).
	0.90	GroEL and GroES are colored as Fig. 1.
	0.54	GroEL (left) and GroEL-GroES-ADP complex (right, the chaperonin cage).
31963896	0.98	HSP60/HSP10 + ATP, Substrate + HSP60 + ATP + 25 microM curcumin, Substrate + HSP10 + ATP + 25 microM curcumin, and Substrate only; no heat shock treatment).
	0.97	HSP60/HSP10 complex, most probably stabilizing the complex by interacting with the folding site of the protein and promoting the folding activity (Figure 4).
	0.97	HSP60/HSP10.
	0.97	HSP60/HSP10 + ATP + 25 microM curcumin) and in the absence of HSP10 (Substrate + HSP60 + ATP + 25 microM curcumin) or HSP60 (Substrate + HSP10 + ATP + 25 microM curcumin), when compared with the reaction without curcumin (Substrate + HSP60/HSP10 + ATP, at 30 min).
	0.96	HSP10 to HSP60 subunits helps promote the refolding of the substrate (Figure 4).
	0.96	HSP60/HSP10 complex or for client protein ligation.
	0.96	HSP60 inhibitors is well established, the binding site of curcumin for HSP60/HSP10 folding machine is unknown, and, to the best of our knowledge, this is the first case of enhancer of this CS.
	0.96	HSP60/HSP10 complex after 60 min of reaction (* p < 0.01 vs. Substrate + HSP60/HSP10 + ATP, Substrate + HSP60 + ATP + 25 microM curcumin, Substrate + HSP10 + ATP + 25 microM curcumin, and Substrate only; no heat shock treatment).
	0.96	HSP10 and HSP60.
	0.87	HSP60/HSP10 complex has any consequences for its folding activity.
	0.86	HSP60, its protein-folding process occurs in cooperation with the co-chaperonin HSP10, as demonstrated by the assay.
	0.76	HSP60/HSP10 folding machinery.
	0.56	HSP60 chaperone activity in the absence of HSP10 (Figure 4).
22140545	0.98	Hsp10, Hsp40 and Hsp60 levels were increased in COPD
	0.98	Hsp10, Hsp40, and Hsp60 levels were increased in the bronchial epithelium of severe/very severe COPD compared to control non-smokers (Mann Whitney: p = 0.007, 0.020, and 0.006, respectively) (Figures 1 and 2).
	0.97	Hsp10, Hsp40, and Hsp60 were increased during progression of disease.
	0.96	Hsp10 (A, B), Hsp40 (C, D), and Hsp60 (E, F).
	0.94	Hsp10, Hsp40, and Hsp60 immunopositive cells in the epithelium (top panels A, C, E) and in the lamina propria (bottom panels B, D, F) of the four groups studied: Control non Smokers, Control Smokers, Mild/Moderate COPD, and Severe/Very Severe COPD.
	0.93	Hsp10, Hsp27, Hsp40, Hsp60, Hsp70, Hsp90, and HSF-1, along with levels of inflammatory markers.
	0.91	Hsp10 - the Hsp60 intramitochondrial co-chaperonin, also known as Early Pregnancy Factor - has a potent immunosuppressive activity both in vivo and in vitro .
	0.90	Hsp60 and Hsp10 levels in patients with COPD could help in the identification of a subclass of patients (i.e., those in which Hsp60 and Hsp10 levels suddenly decrease) which would have a higher risk for cancer development.
	0.86	Hsp60 and Hsp10 levels decrease during carcinogenic steps in airways, i.e., from normal through dysplastic to neoplastic mucosa.
	0.85	Hsp60 and its co-chaperonin Hsp10, and Hsp40 are significantly increased in patients with severe/very severe stable COPD compared to non-smokers with normal lung function.
	0.80	Hsp60 and Hsp10 have been reported during bronchial carcinogenesis, one of the most severe complications for COPD patients, participation of Hsps in COPD pathogenesis and progression has not, to our knowledge, been examined in any detail.
	0.74	Hsp10, Hsp40, and Hsp60 positive cells when compared with COPD patients without chronic bronchitis (not shown).
22312474	0.98	GroEL/GroES complex is necessary for protecting them from aggregation.
	0.98	GroES, which is essential for GroEL-mediated protein folding.
	0.97	GroEL in ATP-bound and -unbound formed and that of GroES has identified an ATP binding domain encompassing N- and C-terminus of GroEL subunits.
	0.96	GroES to GroEL occurs upon ATP binding to equatorial domain of the GroEL subunits whereas the lid formation in eukaryotic and archaeal chaperonins is triggered by the transition state of ATP hydrolysis, suggesting nucleotide cycle dependent mechanistic difference of lid closure.
	0.95	GroES also promotes ATP hydrolysis and the protein substrate gets folded in the "Anfinsen cage" of the GroEL-GroES-ADP complex.
	0.93	GroEL system, CCT also binds ATP and hydrolyses it during protein folding cycle, the CCT does not have detachable GroES-like cochaperonin, rather, a flexible protrusions located in the apical domain in each CCT subunit acts as a lid and is responsible for closing the central cavity.
	0.87	GroEL, followed by the binding of GroES to the same end.
	0.84	GroEL has a cofactor GroES which is used as a "lid" for the closure of central cavity essential for protein folding.
27014702	0.98	GroEL/S variants surface in the first intermediate domain (int.) and second equatorial domain of GroEL, and throughout GroES (Wang et al.,).
	0.98	GroES variant that surfaced from the screening showed that increasing the overall polarity of the GroEL/S folding chamber is important for improved GFP folding activity (Wang et al.,).
	0.97	GroEL, and upon binding of ATP and GroES to the same ring, substrate is moved into the chamber.
	0.97	GroEL and co-chaperone GroES that showed enhanced ability to fold green fluorescent protein (GFP; Wang et al.,).
	0.97	GroES, which is critical in the allosteric regulation of the GroEL system (Kawe and Plukthun,).
	0.97	GroEL activity increased the ATPase activity of GroEL, and improved the ability of GroES to inhibit GroEL ATPase activity (Figures 1A,B; Wang et al.,).
	0.97	GroEL/S chaperonin highlights a fascinating theme in chaperone engineering: very slight modifications (here, only two missense mutations to GroEL, and one to GroES, were required for optimized activity) to chaperone sequence can translate to highly improved folding machines for specific substrates.
	0.68	GroEL is found in a large number of bacteria, and together with its co-chaperone GroES is extremely well characterized (Castanie-Cornet et al.,).
18974836	0.98	GroES-ATP7-(single-ring)GroEL complex.
	0.98	GroES makes contact with the central void of the GroEL trans ring.
	0.97	GroEL/GroES chaperonin complex is a molecular machine whose components assembly and disassembly upon ATP binding and hydrolysis is accompanied by conformation changes.
	0.94	GroES-ATP7-GroEL/GroES-ATP7-(single-ring)GroEL is higher than in most other tested cases (see Table 2).
	0.62	GroEL consists of two 7-subunits rings, which can be in the apo state or loaded with either ATP or ADP; GroES consists of a single 7-subunits ring.
	0.60	GroEL-ATP7 and GroES-ADP7-GroEL-ATP7 pair highlight the conformation differences upon ATP binding to the GroEL cis ring (see Figure 2B) whereas the results for the GroES-ATP7-GroEL and GroES-ATP7-(single-ring)GroEL pair suggest that these two complexes are similar.
30469470	0.98	Hsp60 forms large oligomers in the other cell compartments, and functions together with Hsp10 in protein folding.
	0.95	Hsp10 is supposed to coordinate the behavior of the single Hsp60 monomers and regulate the ATPase cycle.
	0.93	Hsp60 inner cavity are protected from interactions with other components of the surrounding environment, and as described above, Hsp10 forms a lid at the top of the double ring system, closing the opening of the central cavity.
	0.91	Hsp60-Hsp10 complex.
	0.77	heat shock protein 60 (Hsp60) belongs to the group I of chaperonins, and it is classically defined as an intramitochondrial protein that assists with the correct folding of other mitochondrial proteins, together with its co-chaperonin, Hsp10.
29208924	0.97	HSP60 in the presence of HSP10, as found previously with GroEL/GroES.
	0.97	HSP60 induces the interaction between HSP60 and HSP10, but hardly induces the the football-type complex compared with the ATPase activity.
	0.97	HSP10 is clearly decreased in comparison with GTP, consistent with the strong interaction between HSP60 and HSP10 seen in the trypsin sensitivity assay (Fig. 2A).
	0.97	HSP60/HSP10 complex in presence or absence of 0.5 mM GTP displayed approximately 80% efficiency at all concentrations of ATP tested (Fig. 5B,C).
	0.96	GroEL, which is composed of two heptameric rings stacked back-to-back, binds to GroES in an ATP-dependent manner and generally forms an asymmetric bullet-type complex.
	0.96	HSP60 with HSP10, along with productive refolding of the denatured substrate proteins, the GTPase activity of HSP60 was structurally and functionally quite different.
	0.96	HSP60 in the presence or absence of HSP10.
	0.96	HSP60 in the absence or presence of HSP10.
	0.96	HSP60 and HSP10 was detected as full-length HSP10 protein bands in the ATP-concentration range from 0.05 to 1.0 mM, while GTP-dependent interaction was in the GTP-concentration range from 0.5 to 1.0 mM. The protein band signals with GTP were less than those of the ATP-dependent interaction (Fig. 2A and Figure S2A, B).
	0.96	HSP60/HSP10 complex in the presence of ATP or GTP.
	0.95	HSP60 and HSP10 induced by the GTPase activity was weaker than that with ATP, these allosteric transitions might be involved in structural changes resulting in a state capable of binding HSP10.
	0.94	HSP60 formed a clear sigmoidal curve in the absence or presence of HSP10 with Hill coefficients of 2.58 ( +- 0.22) and 1.99 ( +- 0.33), respectively, indicating strong positive cooperativity with respect to GTP.
	0.94	HSP60 and HSP10, we next performed an acid-denatured GFP refolding assay.
	0.94	HSP60 in the presence of ATP or GTP and presence or absence of HSP10 (Figures S2C to E).
	0.94	HSP60, and the large peaks around 11.5 min corresponded to HSP10.
	0.94	HSP60 and HSP10 in the presence of ATP was not detected.
	0.93	HSP60 is converted to a tetradecameric double-ring structure in the presence of ATP, and HSP60 forms a football-type complex when both ATP and the co-chaperone, HSP10, are present.
	0.92	HSP10, the roll-off of the ATPase activity of HSP60 seemed to be reduced.
	0.91	HSP60, but not HSP10, could directly bind to and hydrolyze both ATP and GTP.
	0.90	HSP60 was not suppressed by HSP10, quite different from the ATPase activity.
	0.87	HSP10 and GTP, the molecular weight of HSP60 increased, but the change was smaller than in the presence of both HSP10 and ATP (Fig. 3D).
	0.83	HSP60 or HSP60/HSP10 in the presence of 3.5 mM ATP with or without 0.5 mM GTP were almost all at the same levels.
	0.82	HSP60/HSP10 (ATP concentrations 0.01, 0.5, 1.0 and 3.5 mM) with or without 0.5 mM GTP (Fig. 5B,C).
	0.81	HSP60 in the absence or presence of HSP10 in the low concentration range from 0 to 0.02 mM. The kinetic curves were directly fitted to the Hill equation 2. (C), GTPase activity of HSP60 in the presence or absence of HSP10 was calculated by curve fitting to the Hill equation 2. (D), Purified HSP60 was incubated with GTP at 37 C for 2 h. Sample of time 0 and 2 h were separated by a C18-reverse phase column and absorbance at 256 nm was recorded.
	0.81	HSP60 or HSP60/HSP10 complex is affected by GTP.
	0.78	HSP60 and HSP10 induced by ATP- or GTPase activity.
	0.78	HSP60/HSP10 complex was significantly increased by the treatment with aluminum fluoride (Fig. 4A and S3).
	0.72	HSP60/HSP10 oligomer.
	0.71	HSP60 or HSP10.
	0.71	HSP60/HSP10 complex is classified as single-ring structures consisting of a single-ring (HSP607) and single-ring complex (HSP607-HSP107), and the double-ring structures consisting of a double-ring (HSP6014), bullet-type complex (HSP6014-HSP107) and football-type complex (HSP6014-(HSP107)2), as shown in Figure S1B.
	0.69	HSP60/HSP10 complex mainly formed single-ring structures mostly containing the single-ring complex (HSP607-HSP107) in the presence of GTP (three panels on the second step and fourth step of Figures 3A,B and S2E).
	0.67	HSP60 in the presence of 0.01 mM ATP was suppressed by HSP10 (Fig. 1B), we postulated that HSP60 could bind to HSP10 and refold the non-native substrate.
	0.65	HSP60/HSP10 complex by the ATP- and GTPase activities, we performed a SEC-MALS analysis.
	0.65	HSP60-HSP10 complex.
	0.61	HSP60/HSP10 complex assumes the double-ring structures, containing mainly the football-type complex in the presence of ATP, and the single-ring structures, mainly containing the single-ring complex, in the presence of GTP.
	0.60	HSP60 was displayed in the presence of both HSP10 and ATP, suggesting that the stability of the oligomeric state of HSP60 was increased by both HSP10 and ATP.
	0.58	HSP60 ATPase activity by the co-chaperone HSP10 has been previously reported, and it was also detected in this experiment (Fig. 1A,B and S1B).
	0.55	HSP60 was suppressed by HSP10, whereas GTPase activity unaffected.
	0.52	HSP60/HSP10 complex mainly formed the double-ring structures in the presence of ATP and the single-ring structures in the presence of the GTP.
	0.51	HSP60/HSP10 complex at ATP concentrations from 0 to 1.0 mM also fit well to Eqn.
25355063	0.97	Hsp60 and Hsp10 levels with smoking habits led us to wonder about the effects of cigarette smoke on the expression and subcellular localization of these proteins in bronchial mucosa, i.e. in epithelial and lamina propria cells.
	0.97	Hsp10 and Hsp60 have a similar distribution and higher than normal levels in cells before and after stress and during pathogenesis of a number of diseases, including cancer and inflammatory diseases.
	0.96	Hsp10 has roles, probably independent of Hsp60, different from its canonical function as co-chaperone for Hsp60 in protein folding inside mitochondria.
	0.96	Hsp10, in contrast to Hsp60, was localized not only in the cytoplasm but also in nuclei of epithelial and lamina propria cells of bronchial mucosa in vivo.
	0.94	Hsp10 and Hsp60 levels were increased in the bronchial epithelium of severe/very severe COPD compared with control non-smokers; by contrast, in lamina propria the number of Hsp10 positive cells was significantly increased in all stages of stable COPD compared with control smokers with normal lung function and non-smoking subjects, while the number of Hsp60-positive cells was significantly higher only in severe/very severe COPD compared with control smokers with normal lung function.
	0.94	Hsp10 has also been found increased in some precursors of normal human bone-marrow cells and it disappeared during lineage maturation, while Hsp60 did not show changes in levels during bone marrow cell differentiation.
	0.92	Hsp10 and Hsp60 levels and cellular localization
	0.91	Hsp10 and Hsp60 have for a long time been considered typical intramitochondrial molecules devoted to assisting protein folding inside the organelle.
	0.88	Hsp10 and Hsp60 in human bronchial mucosa.
	0.87	Hsp10 and Hsp60, in relation to the COPD severity.
	0.84	Hsp10 but not Hsp60 positivity in the nucleus, before and after CSE exposure; (iii) CSE did not cause an appreciable overall increase in levels of Hsp10 in either cell line; (iv) CSE exposure determined in both cells lines qualitative changes in Hsp10, as indicated by Mr and pI shifts.
	0.82	Hsp10 and Hsp60 levels did not show quantitative changes in epithelium or in lamina propria of the bronchial mucosa of smokers compared with non-smokers (figure 1a).
	0.81	Hsp10 by electron microscopy and the immunogold technique and western blotting analyses of Hsp10 and Hsp60 in cell lines.
	0.79	Hsp10 and Hsp60 in 16HBE and HFL-1 cells before and after CSE treatment.
	0.72	Hsp10 and Hsp60 with procaspase-3 occurs in the mitochondria of Jurkat cells, and that the disruption of this complex is accompanied by the release of active caspase fragments from the mitochondrial intermembrane space, which is followed by progression to cell death.
	0.69	Hsp10 and Hsp60 in all the tested conditions.
	0.63	Hsp10 is present in epithelium and lamina propria cells of non-smokers and smokers, whereas Hsp60 is present only in epithelial cells.
	0.61	Hsp10 and Hsp60 levels; as described above the immunohistochemical method did not detect changes (figure 3a).
	0.58	Hsp10) is classically considered a mitochondrial co-chaperonin that interacts with Hsp60 to assist in the folding of other mitochondrial proteins.
	0.56	Hsp10 and Hsp60 decrease in bronchial dysplasia and adeno-squamous carcinoma, but increase in airways mucosa in smokers with chronic obstructive pulmonary disease (COPD).
	0.55	Hsp10 were similar to those that had been reported earlier for Hsp60.
	0.53	Hsp10 and Hsp60 levels.
29732373	0.97	GroEL-GroES complex plays a critical role in partial unfolding of misfolded intermediates for further folding (Shtilerman et al.,; Lin et al.,; Weaver et al.,).
	0.97	Hsp60 was initially characterized as a nuclear-encoded mitochondrial protein to help fold proteins newly imported into mitochondria in conjunction with co-chaperonin Hsp10 (10 kDa heat shock protein) (Jindal et al.,; Ostermann et al.,; Reading et al.,).
	0.97	Hsp60-Hsp10's chaperoning activity.
	0.97	Hsp60 (Ban et al.,), suggesting that the covalent interaction between ETB and Cys442 may allosterically modulate Hsp60-Hsp10's chaperoning activity without interfering with its ATPase activity.
	0.97	Hsp60-Hsp10 complex (PDB: 4PJ1) is color-coded in red (Hsp10) and green (Hsp60) cartoons.
	0.96	GroEL-GroES complex undergoes extensive conformational changes during the folding pathway wherein the hydrophobic patches can initially bind unfolded polypeptides primarily through hydrophobic interactions (Finka et al.,).
	0.96	Hsp60 complex that is more disease relevant than the mitochondrial Hsp60-Hsp10 complex that is essential for normal mitochondrial homeostasis?
	0.95	GroEL are driven by multiple factors including GroES binding, substrate binding, ATP binding and ATP hydrolysis (Horwich and Fenton,).
	0.95	Hsp60-Hsp10 complex from Trypanosoma brucei (Abdeen et al.,) to treat African sleeping sickness.
	0.93	Hsp60, and/or Hsp10 have also been shown to reside in other subcellular compartments including extracellular space, cytosol, and nucleus.
	0.93	Hsp60-Hsp10 vs. bacterial GroEL-GroES (Tanabe et al.,), a large number of small molecules were identified as GroEL-GroES inhibitors from a high-throughput screening of ~700,000 compounds (Johnson et al.,; Abdeen et al.,).
	0.91	Hsp60 is a direct mitochondrial protein target of MC and MC inhibited the refolding activity of the Hsp60-Hsp10 complex.
	0.90	Hsp60 is also involved in autoimmunity, it is tentative to speculate that mizoribine's activity on the Hsp60-Hsp10 complex or Hsp60 alone may also contribute to its immunosuppressive effect although supplementing GTP could reverse mizoribine's immunosuppressive effect (Turka et al.,).
	0.88	GroEL-GroES vs. Hsp60-Hsp10 (Abdeen et al.,).
	0.84	Hsp60-Hsp10 complex.
	0.83	Hsp60-Hsp10 complex (Nisemblat et al.,) shall facilitate our understanding of how the inhibitors interact with Hsp60.
	0.69	Hsp60-Hsp10 complex (Nisemblat et al.,) revealed that it is located at a site in close proximity to the ATP binding pocket (Figure 3), suggesting potential allosteric modulation.
	0.67	Hsp60-Hsp10 chaperone complex is very important in maintaining mitochondrial homeostasis and plays a critical role in different diseases including autoimmune diseases and cancers.
	0.65	Hsp60-Hsp10 complex.
23226518	0.97	GroEL was inhibited by both GroES and mHsp10 (by 67% and 53%, respectively) and that of mHsp60 was inhibited, as expected, only by mHsp10 (by 49%) (Table 1).
	0.96	GroES mobile loop (IVL) make contact with three residues L234, L237 and V264, located in the H and I helixes of the GroEL apical domain.
	0.96	GroEL in vivo, together with either GroES or mHsp10.
	0.96	GroEL was found to block GroES binding, although substrate binding in this mutant remained unimpaired ("trap" GroEL).
	0.94	GroEL mutants that acquire the ability to function with a GroES temperature sensitive mutant (G24D) are impaired in their ability to function with wild-type GroES.
	0.92	GroEL (A), wild-type mHsp60 (B), E321K mHsp60 (C), R264K/E358K mHsp60 (D), in the presence of increasing concentrations of mHsp10 (white triangles), GroES (black triangles) and the low-affinity mutants: mHsp10_L33A (white diamonds) and GroES_L27A (black diamonds).
	0.91	GroEL amino acids that are located in the apical domain, none of them would be expected to directly interact with the mobile loop of the co-chaperonin, based on the crystal structure of the GroEL-GroES complex.
	0.90	GroEL-GroES complex was solved at 3 A resolution, allowing for visualization of the contact sites between the two oligomers.
	0.89	GroEL subunits it was shown that the transition of GroEL to its GroES-bound conformation, is accompanied by the formation of a salt bridge between D359 of the apical domain and K80 of the equatorial domain (Fig. 1C).
	0.84	GroEL was shown to directly contact the GroES mobile loop in the GroEL-GroES complex crystal structure.
	0.83	Hsp60 mutants that are able to function with the bacterial co-chaperonin, GroES.
	0.82	GroEL and in mammals as mHsp60) and the co-chaperonin (known in bacteria as GroES and in mammals mHsp10).
	0.79	GroES, is a highly conserved residue among co-chaperonins that was shown to contact GroEL in the crystal structure.
	0.76	GroEL with either mHsp10 or GroES was inhibited by ~75% (Fig. 8A).
	0.75	GroEL was shown to be related to L27 from the IVL tripeptide of the GroES mobile loop.
	0.64	GroEL-GroES and mHsp60-mHsp10 combinations serve as positive controls; the mHsp60-GroES combination serves as negative control.
20600107	0.97	GroEL is composed of 14 identical subunits and its cofactor GroES acts as a lid by binding to GroEL in the presence of ATP.
	0.97	GroEL substrates before and after GroES lid closure at the bulk level.
	0.96	GroEL-GroES system (herein GroEL/ES) promotes protein folding has been a focus of intense research (for reviews, see).
	0.96	GroEL cavities are closed by GroES.
	0.96	GroES-GroEL complex is destabilized, leading to both GroES and substrate release from the cis GroEL.
	0.94	GroEL upon ATP and GroES addition in real time.
	0.93	GroEL, the substrate is usually released and encapsulated in the cavity by GroES and ATP binding.
	0.87	GroES and ATP to close the GroEL cavity, on average further FRET increases occur between the two hydrophobic regions of VHL, accompanied by FRET decreases between the N- and C-termini.
	0.86	GroEL binds a wide range of non-native polypeptides within its central cavity and, together with its cofactor GroES, assists their folding in an ATP-dependent manner.
	0.84	GroES/EL on a bound polypeptide substrate which may arise from the random nature of the specific binding to the various identical subunits of GroEL, and may help explain why multiple rounds of binding and hydrolysis are required for some chaperonin substrates.
	0.79	GroEL/GroES cavity.
	0.72	GroEL has two distinct rings, and the GroEL capped with GroES is called the cis ring, while the non-capped ring is called the trans ring.
28594255	0.97	Hsp60 and Hsp10 constructs were designed and expressed with N-terminal His6 tags to facilitate high yield purification via affinity column chromatography.
	0.97	Hsp60 complex using negative stain electron microscopy revealed the oligomeric assembly of Hsp60 to be in a double-ring tetradecameric conformation that was unable to bind its co-chaperonin Hsp10 in the absence of nucleotide (Fig. 2).
	0.96	Hsp60-His6 producing only monomers, Hsp10-His6 was able to assemble in to heptameric rings as observed in the negative stain electron micrographs indicating that the His6 tag had no effect on Hsp10 quaternary structure.
	0.93	Hsp60 in the absence of Hsp10.
	0.93	Hsp60 are in the closed conformation and incapable of binding substrate or Hsp10; features that are also observed in GroEL.
	0.92	Hsp60 and Hsp10 proteins that can facilitate future biochemical and structural analyses.
	0.92	Hsp60 and Hsp10 proteins.
	0.91	Hsp60 and Hsp10 oligomeric complexes.
	0.88	Hsp60 side views (blue box), Hsp60 top views (green box), and Hsp10 heptamers (red box).
	0.86	Hsp60 and Hsp10 monomers require a pre-existing Hsp60/10 complex for assembly into their final quaternary structures.
	0.81	Hsp60 or that the GroEL/ES chaperonin from the BL21 E. coli cell line may be responsible in assisting the formation of the assembled Hsp60 and Hsp10 complexes that were purified.
17052347	0.97	GroEL, GroES, GspD and Pyk, whereas patients # 4 and 6 were only positive with the GroEL, GspD and Pyk.
	0.96	GroEL, GroES, GspD, Ndk and Pyk within formalin-fixed, paraffin-embedded cell pellets and atheromatous heart tissues.
	0.94	GroEL, GroES, GspD, Ndk and Pyk within formalin-fixed, paraffin-embedded cell pellets and tissues from patients with severe coronary atherosclerosis.
	0.94	GroES and Pyk, and patient # 8 revealed positive reaction with the GroEL and GspD. All patients were negative when tested with the mLPS, whereas the pLPS/MOMP ab revealed positive reactions in patients # 10 and 12.
	0.94	GroEL and GroES in patient # 10 and GspD and Pyk in patient # 12, respectively, is displayed in figure 2.
	0.94	GroEL and GroES, which were upregulated under persistence in proteomic analysis, were likewise positive in most heart tissue specimens.
	0.87	GroEL, GroES, GspD and Pyk).
	0.82	GroEL, GroES, GspD, Ndk and Pyk) raised against differentially expressed proteins under an interferon-gamma (IFN-gamma) induced model of chlamydial persistence.
	0.79	GroEL, GroES and Pyk antibodies, and to a lesser extent, with the GspD (data not shown).
	0.66	GroEL and GroES tend to be useful markers to detect persistent infection in vitro and in vivo.
31444388	0.97	hsp60/hsp10, V72I mutant/hsp10 and D3G mutant/hsp10 in the presence of denatured alpha-lactalbumin substrate was measured by EnzChek Phosphate Assay.
	0.97	hsp60 with hsp10 bound (Fig. 3a).
	0.96	hsp60) and its co-chaperonin, human mitochondrial heat shock protein 10 (hsp10).
	0.96	hsp60/hsp10, V72I mutant/hsp10, D3G mutant/hsp10 was measured as described in the Methods section.
	0.94	hsp60/10 system have been inferred from the catalytic cycle of groEL/groES, the bacterial homolog of hsp60/10 and from the bacteriophage chaperonin phiEL.
	0.94	hsp60/hsp10 resulted in a reconstruction of a tetradecameric hsp60 structure with the hsp10 co-chaperonin capping only one of the chaperonin protein-folding chambers resulting in a so-called "bullet" conformation (Fig. 3).
	0.93	hsp60/hsp10, V72I mutant/hsp10, D3G mutant/hsp10 .
	0.89	hsp10 to produce the bullet conformation equivalent to the conformation seen when groEL hydrolyzes ATP to ADP.
29949977	0.97	GroEL structure and a true GroEL-GroES structure (Fig. 9).
	0.89	GroEL-GroES structure (PDB ID: 2C7C, filtered at 6 nm).
	0.88	GroEL (Fig. 9B) and GroEL-GroES (Fig. 9E) structures as compared to the true structures regarding their size and symmetric shape.
	0.87	GroEL and GroEL-GroES subtomograms captured in.
	0.79	GroEL/GroEL-GroES dataset by randomly selecting 400 subtomograms.
	0.63	GroEL and GroEL-GroES averages, which is only slightly higher than ours obtained from a significantly smaller number of only 400 subtomograms.
	0.51	GroEL and GroEL-GroES averages achieved cross-correlation coefficient of 0.87 and 0.78, respectively whereas the fitted atomic model with FA GroEL and GroEL-GroES averages achieved cross-correlation coefficients of 0.40 and 0.24, respectively.
29979378	0.97	CPN10, CPN60, and CPN70 were obtained from different populations.
	0.97	CPN60 was found to be significantly lower in the abnormal BD group compared with the normal BD group (P = .002); there were no significant differences in CPN10 and CPN70 (Fig. 2).
	0.94	CPN10 and significantly higher levels of CPN60 and CPN70.
	0.94	CPN10, CPN60, and CPN70 might have potential as biomarkers for BD and CPN60 blood level might distinguish patients with abnormal HPA axis activity from those with normal HPA axis activity.
	0.63	CPN10 (A), CPN60 (B), and CPN70 (C) between bipolar disorder patients with abnormal and normal HPA axis activity.
	0.53	CPN10 (A), CPN60 (B), and CPN70 (C) between healthy subjects and patients with bipolar disorder.
9334363	0.97	cpn10 subunits of the heptamer when it binds to cpn60, it may be possible for the two active sequences in Mt cpn10 to make contact with the receptor.
	0.95	cpn10 (SA12; reference), but not by a subclass-matched neutralizing mAb to Mt cpn60 (TB78; reference).
	0.95	cpn60 in the cpn60-cpn10 protein-folding complex, suggesting that the putative cell receptor for Mt cpn10 has some structural homology with cpn60.
	0.77	cpn10) or a mAb to Mt cpn60 to bone explants stimulated with a fixed concentration of Mt sonicate (3 mug/ml) on the release of calcium from calvarial explants and on the numbers of osteoclasts in the calvaria.
	0.75	chaperonin (cpn)10 has been found to be an essential growth and immunosuppressive factor in early pregnancy, and cpn60 induces cytokine synthesis and resorption of bone.
23304456	0.97	HSP10 acts as a cofactor for HSP60.
	0.95	HSP10 are evidenced by the fact that transfecting doxorubicin-treated cardiomyocytes with HSP10 and HSP60 by an adenoviral vector suppresses apoptosis and resulting cardiomyopathy.
	0.94	HSP10 is an important cofactor for HSP60.
	0.91	HSP60, the overexpression of HSP10 is met with an overexpression of BcL-2 and Bcl-xL. These molecules protect vascular endothelial cells from TNF-mediated apoptosis in addition to inhibiting activation of NF-kappabeta and thereby inhibiting the upregulation of proinflammatory genes.
	0.78	HSP10 of Chlamydia pneumoniae in patients with coronary artery disease failed to demonstrate significant differences in levels versus controls; however, the importance of HSP10 to the development of atherosclerosis may indeed lie in its genetic and physiologic link to HSP60.
24675290	0.97	Hsp60 and Hsp10 form the mitochondrial chaperonin complex, which is involved in mitochondrial protein folding.
	0.97	Hsp60 was first shown to reside in the mitochondria, and following interaction with Hsp10, is responsible for chaperoning nascent polypeptides as well as transporting target proteins from the cytoplasm into the mitochondria.
	0.96	GroEL and GroES.
	0.95	GroES (Hsp10), which forms a single heptameric ring, acts as a lid to the chamber and can bind to either end of the double GroEL rings.
	0.95	GroEL act in an alternate fashion, with ATP hydrolysis in one ring resulting in a structural transition in the opposite ring making it available for ATP binding, which in turn triggers the release of GroES and substrate protein from the original ring.
27630992	0.97	HSP60/HSP10 complex is composed of two seven-meric rings of the large subunit (HSP60) stacked back to back (Nisemblat et al.,; Figure 1A).
	0.97	HSP60/HSP10 complex may regulate the activity of the complex.
	0.96	HSP60) forms together with heat shock protein 10 (HSP10) double-barrel chaperonin complexes that are essential for folding to the native state of proteins in the mitochondrial matrix space.
	0.94	HSPD1 Gene Encoding the Large Subunit of the Mitochondrial HSP60/HSP10 Chaperonin Complex
	0.91	HSPD1 gene that encodes the HSP60 subunit of the HSP60/HSP10 chaperonin complex.
24765217	0.97	Hsp60 (HSPD), and Chaperonin/Hsp10 (HSPE) are especially attractrive candidates for DAMPs or alarmins which may be particularly relevant in the pathophysiology of the sepsis syndrome.
	0.96	Hsp10 (HSPE) forms a complex with the mitochondrial co-chaperone, Hsp60 (HSPD) and assists with the proper folding of mitochondrial proteins, as well as the reactivation of denatured proteins.
	0.93	Hsp60 (HSPD), and Hsp10 (HSPE) as the extracellular roles of these HSP families are the best characterized to date.
	0.90	Hsp60 (HSPD) is a key mitochondrial chaperone that forms a complex with the chaperonin (Cpn)/Hsp10 (HSPE).
29423396	0.97	GroES heptamer binding in one ring is not dependent on a GroES heptamer being released from the other, and substrate folding can occur at both GroEL rings simultaneously, thus causing the formation of symmetric complexes.
	0.71	HSP60 is encoded in the gene HSPD1 (also written hspd1) which is localized in chromosome 2 head to head with the gene that codes for the HSP10 co-chaperonin, designated HSP10 (also written cpn60 or HSPE1), and the two genes are separated by a bidirectional promoter (Hansen et al.,).
	0.68	HSP10 and HSP60 and, thereby, learn about the intrinsic mechanism of formation of the complete HSP60/HSP10 complex.
23409238	0.97	GroEL/GroES system has been intensively studied in attempts to understand the underlying mechanism of its mediated-folding of diverse substrate proteins.
	0.55	GroEL precedes the binding of the substrate protein and GroES.
31861751	0.97	HSP60/HSP10 is capable of suppressing doxorubicin-induced apoptosis in cardiomyocytes through increasing anti-apoptotic Bcl-xL and Bcl-2, decreasing pro-apoptotic Bax, and inhibiting the activation of procaspase-3.
	0.94	HSP60 and HSP10 in mitochondria.
27774450	0.96	HSP60/HSP10 complex, were decreased to approximately 20% in patient fibroblasts in spite of unchanged SOD2 transcript levels.
	0.96	HSP10 and HSP60 transcript levels showed no significant differences between patient and control fibroblasts (Supplementary Figure S1).
	0.96	HSP10/HSP60 ratio.
	0.93	HSP60, the fatty acid oxidation enzyme medium-chain acyl-CoA dehydrogenase (MCAD) that previously had been shown to interact with the HSP60/HSP10 complex (Saijo et al.,; Saijo and Tanaka,) and the mitochondrial outer membrane protein VDAC, which was not expected to interact with the HSP60/HSP10 complex.
	0.93	HSPE1 gene encoding the small subunit of the mitochondrial HSP60/HSP10 chaperonin complex is essential for cell function and mutations in its complex partner HSP60 have been associated with neurological diseases, we have in the present study focused on investigating the effects of the HSP10-p.
	0.91	HSP10 to HSP60 subunits.
	0.86	HSP60/HSP10 complex would be helpful for pinpointing further candidates, but is still lacking for the mammalian HSP60/HSP10 complex.
	0.85	HSP60 (10 muM), ATP (1 mMol/L) and the indicated concentrations of wild type (A) or p.Leu73Phe mutant (B) HSP10.
	0.84	GroEL/GroES complex have been characterized and distinguished into classes depending on the length of the time period they interact (Ewalt et al.,).
	0.83	HSPE1 gene encoding the HSP10 subunit of the HSP60/ HSP10 chaperonin complex that assists protein folding in the mitochondrial matrix.
	0.82	HSP60/HSP10 complex showed that leucine-73 of HSP10 is not localized in the domain that interacts with HSP60 subunits in the complex.
	0.75	HSP60/ HSP10 complex forms the protein quality control (PQC) system in the mitochondrial matrix and its expression is regulated by the mitochondrial unfolded protein response and the heat-shock responses (Aldridge et al.,).
	0.64	HSP10 protein is encoded by the HSPE1 gene that is located in a head to head arrangement with the HSPD1 gene encoding HSP60.
	0.61	HSP60/HSP10 complex (Yokota et al.,; Saijo et al.,).
	0.55	Heat shock protein 10 (HSP10) and heat shock protein 60 (HSP60) are the constituents of the HSP60/HSP10 chaperonin complex that assists folding of proteins in the mitochondrial matrix space (Cheng et al.,; Hartman et al.,).
14525625	0.96	cpn10 and cpn60 proteins appear conserved in all organisms.
	0.95	co-chaperonin protein 10 (cpn10) assists cpn60 in the folding of nonnative polypeptides in a wide range of organisms.
	0.89	cpn10 results in GroEL-assisted refolding of citrate synthase to 52 +- 4 %.
	0.87	GroEL-assisted refolding of citrate synthase in the presence of GroES.
	0.86	cpn60, cpn10 forms a cap covering the central cavity of cpn60, and folding of substrates (nonnative proteins) is achieved through cycles of ATP-dependent binding and dissociation.
	0.71	cpn10 mutations was tested in a GroEL-dependent citrate synthase refolding assay in vitro.
	0.66	cpn10 variant, however, failed to assist GroEL in substrate refolding (< 3 % citrate synthase refolding).
	0.61	cpn10 heptamer is to assist cpn60 in folding of nonnative proteins.
18030332	0.96	HSP10 and HSP60 are found in every cell as nuclear encoded genes which function within the mitochondria.
	0.94	HSP10 is unlikely as the genes encoding both HSP10 and HSP60 are organized in a head-to-head fashion with a shared bidirectional promoter.
	0.90	HSP10, HSP60 and BiP were measured by immunoassay and related to other plasma measures of inflammation.
	0.82	HSP10 synthesis did decrease in periodontal disease a corresponding decrease in HSP60 concentrations would be expected, and was not observed in this study.
	0.81	HSP10, HSP60 and BiP.
	0.71	HSP10 (A-B), BiP (C-D) and HSP60 (E-F) before, 24 hrs after and 6 months after periodontal therapy.
20338243	0.96	GroEL+GroES (PDB:1aon) are shown.
	0.91	GroEL, GroEL+GroES, ribosome large/small subunits, ribosome RNA/proteins, bacteriophage lambda, and rice dwarf virus.
	0.90	GroEL+GroES and Ribosome.
	0.51	GroEL), groups of 2-3 regions correspond to single proteins, whereas in the lid section (GroES), single regions correspond to each protein.
29415987	0.96	HSP60 KD may also disturb the mitochondrial supercomplex assembly by impairment of newly synthesized OXPHOS subunits folding through HSP10/HSP60 complex.
	0.93	HSP60 and HSP10 are co-chaperones working together in mitochondria, a coordinated expression pattern of these two proteins were frequently observed in different cancer types including PDAC (Table 1).
	0.68	HSP60, HSP10 (also known as HSPE1) was significantly increased in PDAC tissues compared with normal tissues with the same fold change observed with HSP60; however, expression of HSP10 in PDAC tissues was not correlated with histological grade (Table 1).
19969325	0.96	HSP60, HSP70, GRP78 and HSP90 were the key modulators of adaptive immunity, whereas HSP22, alphaA-crystallin and HSP10 were operative in the signaling pathways of innate immune reactions.
	0.94	HSP65, HSP70 and HSP10, which involved treatment of animals with exogenous HSPs before or after the onset of autoimmune arthritis.
22174669	0.96	GroEL-GroES.
	0.95	GroEL-GroES (Figure 7A), the ATP site is more strongly connected to the inside of the cavity than the outside, but in this case the pattern is relatively symmetric between the rings.
31540420	0.96	HSP60/HSP10 complex, it performs crucial cellular activities including protein folding, transport of proteins across membranes and other non-chaperone functions.
22297444	0.95	Hsp10, Hsp70, and Hsp90, as well as Hsp60, have been found to change in parallel with the development of large bowel cancer, the most severe complication of UC.
	0.95	Hsp60, Hsp10 has been described as an anti-inflammatory agent.
	0.92	Hsp10 levels are increased in the intestinal mucosa of both CD and UC, compared to normal mucosa, and that it often co-localizes with Hsp60 in the same cells, both in Ep and LP.
	0.75	Hsp10 is classically considered the Hsp60 co-chaperonin, with both working inside mito-chondria for assisting the correct folding of proteins.
19802337	0.95	GroES sits atop GroEL, adding about 4 nm to its height.
	0.74	GroEL and GroES are one of most popular protein complexes studied by AFM, even if they are rather damage-prone.
29869885	0.95	GroEL extensively and are capable of penetrating deep within the cavity prior to encapsulation by GroES.
	0.88	GroES encapsulation is not an absolute requirement for GroEL function.
30060666	0.95	GroEL/GroES chaperonin system has gone largely unexplored.
	0.91	GroEL and GroES, and human HSP60 and HSP10, were expressed and purified as previously reported.
22696408	0.95	GroEL and GroEL+GroES maps, Nhs identifies the individual domains of the monomers (Fig. 3).
23166722	0.94	GroEL and GroES increases the yield of properly folded passenger proteins in vitro.
	0.89	GroEL heptamers while the other empty cavity binds the co-chaperonin GroES and ATP, enabling conformational changes to be propagated from one cavity to the other.
	0.84	GroES along with GroEL and ATP/Mg2+clearly stimulated the folding of both DHFR and G3PDH (Figure 5).
23783810	0.94	GroES bind to the GroEL ring with the protein ligand attached, a conformational change occurs that has not yet been fully mapped and is believed to change from one substrate to another.
	0.94	GroES and GroEL respectively.
29615920	0.94	HSP10, a homolog of the bacterial GroES, forms a cap closing the opening of the inner cavity of the HSP60 double ring, regulating substrate accessibility and ATPase activity (Martin et al.,; Fenton et al.,; David et al.,).
18463703	0.93	GroEL-GroES complex.
	0.90	GroEL/GroES chaperonin complex.
	0.84	GroEL/GroES Complexes
	0.82	GroEL-GroES chaperonin is an ellipsoidal protein complex that is approximately 16 nm long.
	0.77	GroEL/GroES complex.
	0.70	GroEL equatorial plane then this may also be relevant for the mechanism by which the GroEL/GroES chaperonin can help the refolding of proteins that are too big to be encapsulated.
	0.68	GroEL-GroES chaperone complex.
30770797	0.92	HSP60 and HSP10 chaperonins, and on Fdxr, a mitochondrial respiratory chain protein known to be transcriptionally activated by p53 and involved in responses to therapeutic drugs.
	0.90	HSP60, Fhit, or HSP10 antisera.
	0.70	HSP60 and 10, ferredoxin reductase (Fdxr), malate dehydrogenase (Mdh), electron-transfer flavoprotein (Etfb), and mitochondrial aldehyde dehydrogenase 2 (Aldh2); HSP60 and HSP10 are also distributed in the cytosol.
	0.57	HSP10 and HSP60 in DSP-treated H1299D1/Fhit and HCT116 cells (Fig. 2b).
31861692	0.92	Hsp60 plays a role in assisting the folding of other proteins with Hsp10 in an ATP-dependent manner in the mitochondrial matrix.
18266962	0.91	HSP60 and HSP10 associated to procaspase-3 and favoured its activation by cytochrome c in an ATP-dependent manner, suggesting that the chaperone function of HSP60 was involved in this process (Fig. 1A).
	0.87	HSP60 is regulated by HSP10, which binds to HSP60 and regulates its substrate binding and ATPase activity.
	0.87	HSP60 and HSP10 do not always act as a single functional unit: only newly mitochondria imported proteins are severely affected by inactivation of HSP10.
	0.84	HSP60 and HSP10 has been demonstrated by two independent groups.
	0.82	HSP60 and HSP10 release from the mitochondria (Fig. 1).
	0.76	HSP10 molecules bind to one HSP60 molecule.
23028910	0.90	Hsp10 interacts with Hsp60 in the extracellular milieu is unknown, but such an interaction has been suggested as a potential mechanism of action of XToll .
	0.83	Hsp60 and Hsp10 were determined in a cohort of 20 HIV-infected patients before and after effective combination anti-retroviral therapy (cART).
	0.82	Hsp60 levels) between clinical biomarkers and Hsp10 levels were significant (data not shown).
	0.59	heat shock protein 60 (Hsp60) and heat shock protein 10 (Hsp10) are found in the mitochondria where they assemble into two back-to-back heptameric Hsp60/Hsp10 rings that function as ATP-dependent protein folding machines.
25390895	0.90	HSP60-Cpn10 protein complex accelerates the folding of polypeptides imported into mitochondria and reduces aggregation of unfolded inactive polypeptides.
	0.88	Cpn10 is considered a cooperating partner of HSP60 in protein folding processes.
25601566	0.89	GroEL/GroES complex, an "Anfinsen cage", ensures that, during folding, the protein simply cannot aggregate with any other protein.
	0.82	GroEL/GroES cavity, we note that a recent study of wild-type MBP shows that it rapidly collapses upon dilution from denaturant, within the dead time of mixing.
	0.76	GroEL/GroES.
	0.67	GroEL/GroES-dependent substrate protein DapA has suggested that its folding pathway inside the GroEL/GroES chaperonin cavity may differ from that taken in free solution under so-called "permissive conditions" of low temperature and concentration, where the protein can reach the native form either inside the encapsulated chaperonin cavity or free in solution.
25207654	0.89	HSP60 and HSP10 in bowel carcinomas with lymph node metastasis and found that HSP60 and HSP10 overexpression was functionally related to tumoral progression in bowel carcinomas.
	0.87	HSP60 and HSP10 expression in lung cancer with that of chronic obstructive pulmonary disease by immunohistochemistry and found the contradictory results that the loss of HSP60 and HSP10 immunopositivity is related to the development and progression of bronchial cancer in smokers with chronic obstructive pulmonary disease.
19399224	0.88	Gro-EL fragment and entire complex GroEL-GroES.
	0.76	GroEL interact with the co-chaperonin GroES.
16515699	0.86	groEL region analysed by Teng et al. (mean nucleotide sequences similarity scores between species of 69.7% (range: 48.0-96.8) vs. 81.7% (range: 77.2-95.2); p < 10-3), whereas it showed a tendency for higher variability than groES full-length sequences (73.3% (range: 62.1-95.1); p = 0.083) (Figure 2a).
	0.85	groES and/or the groEL genes of VGS.
	0.85	groES gene in its 3' region and the intergenic region between groES and groEL.
	0.79	groES full-length sequences, and tend to be more discriminant than the large groEL region previously analysed by Teng et al.. R2 is less variable but is also discriminant, and it has more conserved primer-binding sites.
	0.54	groES sequence and the groES-groEL spacer region.
28630164	0.85	GroEL/GroES chaperonin pair form a folding chamber of ~65 A diameter, inside which many cellular proteins reach the native state.
	0.58	GroES associates as a lid to GroEL through the interaction of seven unstructured loops that slide into seven hydrophobic pockets in GroEL.
29755985	0.84	hsp60/10 ADP complex is difficult because biochemical studies indicate that hsp60 has an affinity for hsp10 that is so low in the presence of ADP that the affinity is nearly immeasurable (Nielsen and Cowan,).
19568603	0.82	HSP60 may trigger apoptosis through caspase cascade activation by an association between HSP60/HSP10 complex and pro-caspase-3 inside the mitochondria, resulting in a subsequent release of the HSP60 into the cytoplasm.
29766408	0.81	Hsp10 levels to those found in controls and a lesser increase in BiP levels with no change in Hsp60.
	0.77	Hsp10, Hsp60 and BiP (Henderson and Pockley).
28382301	0.78	GroEL/ES is formed by GroEL and the cochaperonin GroES.
	0.68	GroES interacts with one of the seven-membered rings formed by GroEL after a conformational change has been induced in the subunits.
23762847	0.78	HSP60-HSP10 (GroEL-GroES) system is involved in classical protein folding.
26335776	0.78	HSP60, together with HSP70 and HSP10, are important for protein import into mitochondria.
24830947	0.73	GroEL/GroES because the co-chaperonin GroES release is induced by the transfer of allosteric information between the two rings.
31564980	0.72	HSP10 and HSP60 could increase the abundance of the anti-apoptotic Bcl-xl and Bcl-2, and reduced the protein content of the pro-apoptotic Bax in the study of doxorubicin in cardiac muscle cells.
25762445	0.71	HSP60 and HSP10 (Fig. 7b).
	0.71	HSP60 and HSP10 were induced modestly (approximately five- to sixfold) during heat shock (Fig. 7c), whereas those of cytoplasmic/nuclear chaperones were robustly induced (more than 25-fold) (Supplementary Fig. 7a).
	0.65	HSP60, HSP10, HSP110, HSP70 and HSP25 were correlated with each mRNA level (Fig. 7d).
	0.63	HSP60 and HSP10 (refs), and the HSR is modulated by mitochondrial signals such as increased levels of reactive oxygen species, which are produced in excess from impaired mitochondria.
	0.62	HSP60, HSP10 and mtHSP70, and proteases, such as Lon and ClpP. Although this response is regulated by ATFS-1 in C. elegans, a mammalian homologue of ATFS-1 has not yet been identified.
28119916	0.64	Hsp60 or Cpn60) complex (with Hsp10 on top) characteristic of bacteria and eukaryotic-cell mitochondria (the former two are hexadecamers while the latter is a tetradecamer).
29872356	0.57	HSP60, HSP40, HSP20-30, and HSP10 (small HSPs).
26700624	0.53	HSP60 not only causes a significant decrease in its ATP-hydrolysis activity but also it disturbs the interaction of HSP60 with its co-chaperonin HSP10.