PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14687928-8 2004 In comparison, urea-denatured GroEL, BSA and the refolding mixture in the absence of proteins resulted in the recovery of 72, 50, and 49% rhodanese activity, respectively. Urea 15-19 heat shock protein family D (Hsp60) member 1 Homo sapiens 30-35 22273181-2 2012 In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures, in the presence of ox-GroEL (oxidized GroEL), which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP. Urea 55-59 heat shock protein family D (Hsp60) member 1 Homo sapiens 123-128 22273181-2 2012 In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures, in the presence of ox-GroEL (oxidized GroEL), which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP. Urea 55-59 heat shock protein family D (Hsp60) member 1 Homo sapiens 139-144 22273181-3 2012 We found that ox-GroEL could efficiently bind the urea-unfolded rhodanese at 4 C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). Urea 50-54 heat shock protein family D (Hsp60) member 1 Homo sapiens 17-22 15710410-1 2005 In tritium-hydrogen exchange experiments, the large GroEL substrate Rubisco was unfolded and exchanged in urea/acid/tritiated water, then diluted into either protic buffer or protic buffer containing GroEL. Urea 106-110 heat shock protein family D (Hsp60) member 1 Homo sapiens 52-57 28017766-2 2017 GroEL denaturation with urea and dilution in buffer leads to formation of a folded GroEL monomer. Urea 24-28 heat shock protein family D (Hsp60) member 1 Homo sapiens 0-5 28017766-2 2017 GroEL denaturation with urea and dilution in buffer leads to formation of a folded GroEL monomer. Urea 24-28 heat shock protein family D (Hsp60) member 1 Homo sapiens 83-88 28017766-6 2017 We present the equilibrium unfolding of monomeric GroEL as studied by urea and heat mediated unfolding processes. Urea 70-74 heat shock protein family D (Hsp60) member 1 Homo sapiens 50-55 12790657-3 2003 In a suspended system, mini-GroEL showed significant enhancement of the activity recovery of rhIFN-gamma, applyed with a 1-5:1 stoichiometry of mini-GroEL to rhIFN-gamma at 25 degrees C. Moreover, 1 M urea in the renaturation buffer had a synergistic effect on suppressing the aggregation and improving the activity recovery. Urea 201-205 heat shock protein family D (Hsp60) member 1 Homo sapiens 28-33 12790657-3 2003 In a suspended system, mini-GroEL showed significant enhancement of the activity recovery of rhIFN-gamma, applyed with a 1-5:1 stoichiometry of mini-GroEL to rhIFN-gamma at 25 degrees C. Moreover, 1 M urea in the renaturation buffer had a synergistic effect on suppressing the aggregation and improving the activity recovery. Urea 201-205 heat shock protein family D (Hsp60) member 1 Homo sapiens 149-154 12061791-6 2002 A strong interaction with rhodanese was obtained when the enzyme was pre-incubated with urea, indicating that exposure of hydrophobic surfaces alone on oxidized rhodanese was not sufficient for the formation of a strong complex and that a more unfolded structure of rhodanese was required to interact strongly with GroEL. Urea 88-92 heat shock protein family D (Hsp60) member 1 Homo sapiens 315-320 11020386-2 2001 We have studied the effect of macromolecular crowding reagents, such as polysaccharides and bovine serum albumin, on the refolding of tetradecameric GroEL from urea-denatured protein monomers. Urea 160-164 heat shock protein family D (Hsp60) member 1 Homo sapiens 149-154 11841236-3 2002 The study of the interaction of different urea-induced forms of rhodanese with GroEL suggests that species preceding the domain folded form bind directly and productively to GroEL. Urea 42-46 heat shock protein family D (Hsp60) member 1 Homo sapiens 79-84 11841236-3 2002 The study of the interaction of different urea-induced forms of rhodanese with GroEL suggests that species preceding the domain folded form bind directly and productively to GroEL. Urea 42-46 heat shock protein family D (Hsp60) member 1 Homo sapiens 174-179 11841236-5 2002 Partially folded rhodanese can be released from the GroEL-GroES-ADP complex by subdenaturing concentrations of urea as a homogeneous species that is committed to fold to the native conformation with little or no partitioning to the aggregated state. Urea 111-115 heat shock protein family D (Hsp60) member 1 Homo sapiens 52-57 11222029-1 2000 The chaperonins GroEL and GroES were shown to facilitate the refolding of urea-unfolded rhodanese in an ATP-dependent process at 25 or 37 degrees C. A diminished chaperonin activity was observed at 10 degrees C, however. Urea 74-78 heat shock protein family D (Hsp60) member 1 Homo sapiens 16-21 11222029-2 2000 At low temperature, GroEL retains its ability to form a complex with urea-unfolded rhodanese or with GroES. Urea 69-73 heat shock protein family D (Hsp60) member 1 Homo sapiens 20-25 10757973-2 2000 This study reports on the unfolding and disassembly of GroEL in guanidine hydrochloride and urea. Urea 92-96 heat shock protein family D (Hsp60) member 1 Homo sapiens 55-60 9452440-6 1998 Urea denaturation, sedimentation velocity ultracentrifugation, and electron microscopy revealed that the quaternary structure of GroEL in the presence of Zn2+ had a stability and morphology equivalent to unliganded GroEL. Urea 0-4 heat shock protein family D (Hsp60) member 1 Homo sapiens 129-134 10495893-4 1999 However, the free monomeric GroEL was substantially less stable to urea and heat than the corresponding subunit in the composition of native oligomeric particles. Urea 67-71 heat shock protein family D (Hsp60) member 1 Homo sapiens 28-33 10187830-5 1999 Reactivation of MBP-E1 denatured in 8 M urea was absolutely dependent on GroEL/GroES and Mg2+-ATP, and exhibited strikingly slow kinetics with a rate constant of 376 M-1 s-1, analogous to denatured untagged E1. Urea 40-44 heat shock protein family D (Hsp60) member 1 Homo sapiens 73-78 9786862-6 1998 The addition of a non-denaturing concentration of urea accelerated the inactivation and partitioning of rhodanese onto GroEL. Urea 50-54 heat shock protein family D (Hsp60) member 1 Homo sapiens 119-124 9330224-9 1997 It is also able to assist the refolding of urea-denatured rhodanese by GroEL. Urea 43-47 heat shock protein family D (Hsp60) member 1 Homo sapiens 71-76 8995221-1 1997 The interaction of GroEL with urea-unfolded dihydrofolate reductase (DHFR) has been studied in the presence of DHFR substrates by investigating the ability of GroES to release enzyme under conditions where a stable GroES-GroEL-DHFR ternary complex can be formed. Urea 30-34 heat shock protein family D (Hsp60) member 1 Homo sapiens 19-24 7673187-1 1995 Conditions are reported that, for the first time, permit the folding and assembly of active chaperonin, GroEL, following denaturation in 8 m urea. Urea 141-145 heat shock protein family D (Hsp60) member 1 Homo sapiens 104-109 7499369-1 1995 The urea-induced dissociation and subsequent conformational transitions of the nucleotide-bound form of GroEL were studied by light scattering, 4,4"-bis(1-anilino-8- naphthalenesulfonic acid) binding, and intrinsic tyrosine fluorescence. Urea 4-8 heat shock protein family D (Hsp60) member 1 Homo sapiens 104-109 7577988-0 1995 Residual structure in urea-denatured chaperonin GroEL. Urea 22-26 heat shock protein family D (Hsp60) member 1 Homo sapiens 48-53 7577988-1 1995 The urea denaturation of the chaperonin GroEL has been studied by circular dichroism, intrinsic tyrosine fluorescence and fluorescence of the hydrophobic probe, 1,1"-bis(4-anilino)naphthalene-5,5"-disulfonic acid (bisANS). Urea 4-8 heat shock protein family D (Hsp60) member 1 Homo sapiens 40-45 7577988-2 1995 It is shown that GroEL denaturation, monitored by CD and intrinsic fluorescence measurements, can be well described by a two-state transition that is complete by 3-3.1 M urea. Urea 170-174 heat shock protein family D (Hsp60) member 1 Homo sapiens 17-22 7577988-6 1995 In contrast to the CD and intrinsic fluorescence measurements, bisANS bound to GroEL exhibits considerable fluorescence intensity under conditions where the CD and intrinsic fluorescence signals have already reached their minimum values (> 3.1 M urea). Urea 249-253 heat shock protein family D (Hsp60) member 1 Homo sapiens 79-84 7665563-2 1995 Efficient renaturation of urea-denatured rhodanese using the chaperonin GroE system requires GroEL, GroES, and ATP. Urea 26-30 heat shock protein family D (Hsp60) member 1 Homo sapiens 93-98 7696310-1 1995 The present work shows that monomers of cpn60 (groEL) formed at 2.5 M urea could be assembled to tetradecamers in a process that was independent of ATP. Urea 70-74 heat shock protein family D (Hsp60) member 1 Homo sapiens 40-45 7706275-5 1995 GroEL at pH 5.5 is tetradecameric and can capture urea-denatured rhodanese and release it as active enzyme. Urea 50-54 heat shock protein family D (Hsp60) member 1 Homo sapiens 0-5 7706275-7 1995 The GroEL-rhodanese complex is more stable to dissociation by 2.25 M urea than the complex formed at pH 7.8. Urea 69-73 heat shock protein family D (Hsp60) member 1 Homo sapiens 4-9 7696310-1 1995 The present work shows that monomers of cpn60 (groEL) formed at 2.5 M urea could be assembled to tetradecamers in a process that was independent of ATP. Urea 70-74 heat shock protein family D (Hsp60) member 1 Homo sapiens 47-52 7696310-2 1995 Reassembled cpn60 was able to assist the folding of urea unfolded rhodanese. Urea 52-56 heat shock protein family D (Hsp60) member 1 Homo sapiens 12-17 7696310-3 1995 When cpn60 was incubated at urea concentrations higher than 2.75 M, assembly of tetradecameric cpn60 did not occur after dialysis, and the presence of ATP did not stimulate the assembly process. Urea 28-32 heat shock protein family D (Hsp60) member 1 Homo sapiens 5-10 7696310-6 1995 Assembly and disassembly of cpn60 tetradecamers were followed as a function of the urea concentration by ultracentrifugation and gel electrophoresis in the presence of urea. Urea 83-87 heat shock protein family D (Hsp60) member 1 Homo sapiens 28-33 7696310-6 1995 Assembly and disassembly of cpn60 tetradecamers were followed as a function of the urea concentration by ultracentrifugation and gel electrophoresis in the presence of urea. Urea 168-172 heat shock protein family D (Hsp60) member 1 Homo sapiens 28-33 7905478-7 1994 The present work demonstrates that the rhodanese-cpn60 complex can be dissociated by urea to allow folding to proceed, thus removing the obligatory requirement for cpn10 and ATP. Urea 85-89 heat shock protein family D (Hsp60) member 1 Homo sapiens 49-54 7905478-10 1994 Intermediate cpn60 species, possibly heptamers, are detected at intermediate urea concentrations after addition of unfolded rhodanese. Urea 77-81 heat shock protein family D (Hsp60) member 1 Homo sapiens 13-18 7905478-11 1994 The use of urea has demonstrated a functionally related loosening of subunit interactions in cpn60 that is not detectable under usual solution conditions. Urea 11-15 heat shock protein family D (Hsp60) member 1 Homo sapiens 93-98