PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8318151-1 1993 The catalytic activity and activity changes during denaturation by guanidine hydrochloride of glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and alpha-chymotrypsin in crystalline state and in solution have been compared. Guanidine 67-90 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 94-134 7929125-1 1994 D-Glyceraldehyde-3-phosphate dehydrogenase (GAP-DH) is a protein containing no disulfide bonds; the guanidine HCl-denatured enzyme shows only a limited extent of refolding and reactivation upon dilution, and the enzyme is particularly prone to aggregation during the dilution process. Guanidine 100-113 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-42 7929125-1 1994 D-Glyceraldehyde-3-phosphate dehydrogenase (GAP-DH) is a protein containing no disulfide bonds; the guanidine HCl-denatured enzyme shows only a limited extent of refolding and reactivation upon dilution, and the enzyme is particularly prone to aggregation during the dilution process. Guanidine 100-113 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 44-50 7945247-0 1994 Inactivation precedes changes in allosteric properties and conformation of D-glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-bisphosphatase during denaturation by guanidinium chloride. Guanidine 173-193 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-117 7945247-4 1994 GAPDH is completely inactivated at 0.3 M GdmCl but at this GdmCl concentration it still binds NAD+ with negative co-operativity. Guanidine 41-46 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 7945247-4 1994 GAPDH is completely inactivated at 0.3 M GdmCl but at this GdmCl concentration it still binds NAD+ with negative co-operativity. Guanidine 59-64 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 16551514-5 2006 In contrast, GAPDH denatured in guanidine hydrochloride (GAPDHden) is reactivated in the presence of GroEL, GroES, Mg2+, and ATP, yielding 11-15% of its original activity, while the spontaneous reactivation yields only 2-3%. Guanidine 32-55 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 13-18 20833277-7 2010 However, compared to muscle glyceraldehyde-3-phoshate dehydrogenase, dN-GAPDS exhibited enhanced thermostability (the transition midpoints values are 60.8 and 67.4 C, respectively) and was much more resistant towards action of guanidine hydrochloride (inactivation constants are 2.45+-0.018 and 0.118 +- 0.008 min(-1), respectively). Guanidine 227-250 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 72-77 18725330-2 2008 It was demonstrated that non-native forms of GAPDH obtained by different ways (cold denaturation, oxidation of the enzyme, and its unfolding in guanidine hydrochloride) efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Guanidine 144-167 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 45-50 16551514-6 2006 The oxidation of GAPDH with hydrogen peroxide in the presence of 4 M guanidine hydrochloride results in the formation of the enzyme (GAPDHox) that cannot acquire its native conformation and binds to GroEL irreversibly. Guanidine 69-92 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 17-22 9531491-7 1998 The similar profiles of the effects of GroEL and ANS on the re-activation of GAPDH denatured by different concentrations of GuHCl suggest that GroEL and ANS recognize and bind to the same folding intermediate, which is similar to the relatively stable, partially unfolded, state of the enzyme denatured in 0.5-1.0 MGuHCl. Guanidine 124-129 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 77-82 10899610-2 2000 It was found that the conformers of alphaLA that efficiently reduce the trigger factor assisted reactivation of guanidine-denatured GAPDH by competitively binding with trigger factor are those derivatives that have loose structure. Guanidine 112-121 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 132-137 10998366-2 2000 Inactivation of GAPDH incubated with tau was more distinguishably detected than that of control GAPDH during thermal and guanidine hydrochloride (GdnHCl) denaturation. Guanidine 121-144 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 16-21 10998366-2 2000 Inactivation of GAPDH incubated with tau was more distinguishably detected than that of control GAPDH during thermal and guanidine hydrochloride (GdnHCl) denaturation. Guanidine 146-152 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 16-21 10998366-4 2000 A marked change in both the emission intensity and emission maximum of the intrinsic fluorescence at 335 nm of GAPDH with tau was observed when GdnHCl concentration was 0.8 M, but that of the control without tau occurred in 1.2 M GdnHCl. Guanidine 144-150 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 111-116 10998366-4 2000 A marked change in both the emission intensity and emission maximum of the intrinsic fluorescence at 335 nm of GAPDH with tau was observed when GdnHCl concentration was 0.8 M, but that of the control without tau occurred in 1.2 M GdnHCl. Guanidine 230-236 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 111-116 10998366-6 2000 Kinetics of inactivation of GAPDH with tau in 0.2 M GdnHCl was a monophasic procedure, instead of the biphasic procedure followed by the control, as described before [He, Zhao, Yan and Li (1993) Biochim. Guanidine 52-58 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 28-33 10642503-2 2000 In the present work it was shown that alpha-crystallin specifically increased the reactivation of guanidine-denatured glyceraldehyde-3-phosphate dehydrogenase with most of the activity being recovered. Guanidine 98-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 118-158