PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2719939-13 1989 The data indicate that introduction of a region of RNase A containing the Cys-65--Cys-72 disulfide bond into angiogenin dramatically increases RNase-like enzymatic activity while reducing its angiogenicity. Disulfides 89-98 ribonuclease A family member 1, pancreatic Homo sapiens 51-58 6269576-2 1981 Reduced RNase A was reoxidized, and the incorrectly formed disulfide bonds were reshuffled to the native ones by oxidized and reduced glutathiones, as described in the first paper of this series. Disulfides 59-68 ribonuclease A family member 1, pancreatic Homo sapiens 8-15 924986-1 1977 Disulfide-reduced RNase A, which could be reoxidized to give the native enzyme, was shown to have a CD spectrum quite different from that of the native enzyme or a random coil. Disulfides 0-9 ribonuclease A family member 1, pancreatic Homo sapiens 18-25 924986-2 1977 Disulfide-reduced and fully cysteine-S-carboxamidomethylated RNase A because the derivative was stable and gave a spectrum identical to that of reduced RNase A. Disulfides 0-9 ribonuclease A family member 1, pancreatic Homo sapiens 61-68 924986-2 1977 Disulfide-reduced and fully cysteine-S-carboxamidomethylated RNase A because the derivative was stable and gave a spectrum identical to that of reduced RNase A. Disulfides 0-9 ribonuclease A family member 1, pancreatic Homo sapiens 152-159 19344116-1 2009 Ribonuclease A (RNase A) undergoes more rapid conformational folding with its disulfide bonds intact than during oxidative folding from its reduced form. Disulfides 78-87 ribonuclease A family member 1, pancreatic Homo sapiens 0-14 28942648-0 2017 Dynamics of Disulfide-Bond Disruption and Formation in the Thermal Unfolding of Ribonuclease A. Disulfides 12-21 ribonuclease A family member 1, pancreatic Homo sapiens 80-94 28942648-2 2017 RNase A contains four disulfide bonds, which were found to be necessary for the native structure of the protein to form. Disulfides 22-31 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 28942648-6 2017 The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72. Disulfides 28-37 ribonuclease A family member 1, pancreatic Homo sapiens 123-130 28942648-6 2017 The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72. Disulfides 104-113 ribonuclease A family member 1, pancreatic Homo sapiens 123-130 28942648-6 2017 The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72. Disulfides 104-113 ribonuclease A family member 1, pancreatic Homo sapiens 123-130 28942648-9 2017 By analyzing residue-position fluctuations, it was found that native disulfide bonds are located in the highly flexible regions of the protein, which is probably why their presence is necessary for the stability of RNase A. Disulfides 69-78 ribonuclease A family member 1, pancreatic Homo sapiens 215-222 25703060-6 2015 RNase A was used as a model protein in this study because the disulfide bonds of this protein have been well characterized. Disulfides 62-71 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 25703060-7 2015 Application of this approach to peptides digested with Asp-N/C (chemical digestion) and trypsin under acid hydrolysis conditions identified the four native disulfide bonds of RNase A. Disulfides 156-165 ribonuclease A family member 1, pancreatic Homo sapiens 175-182 19344116-1 2009 Ribonuclease A (RNase A) undergoes more rapid conformational folding with its disulfide bonds intact than during oxidative folding from its reduced form. Disulfides 78-87 ribonuclease A family member 1, pancreatic Homo sapiens 16-23 19344116-4 2009 However, in the mutants Y92G and Y92A, a key structured disulfide-bonded species, des-[65-72], involved in the oxidative folding pathway of RNase A, was destabilized. Disulfides 56-65 ribonuclease A family member 1, pancreatic Homo sapiens 140-147 16013863-4 2005 For RNAse A, quantitative reduction of the disulfide bonds lead to the exposure of an additional arginine residue and two different conformations of the reduced protein were observed by ESI-MS that could be distinguished according to their charge-state distribution. Disulfides 43-52 ribonuclease A family member 1, pancreatic Homo sapiens 4-11 19956338-4 2008 RNase A and B each contain four disulfide bonds, and the addition of a reducing reagent, such as dithiothreitol, was found to be required to achieve efficient acidic proteolysis. Disulfides 32-41 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 19309163-1 2009 The oxidative folding pathways of two four-disulfide proteins of the ribonuclease family, ONC and RNase A, which have similar three-dimensional folds but only 30% sequence homology, are compared. Disulfides 43-52 ribonuclease A family member 1, pancreatic Homo sapiens 98-105 16403016-6 2006 It is shown that chemical cleavage at aspartate residues in the protease resistant RNase A, followed by tryptic digestion can be optimized so that the rigid protein breaks up into MALDI-MS detectable fragments, leaving the disulfide bonds intact. Disulfides 223-232 ribonuclease A family member 1, pancreatic Homo sapiens 83-90 11982363-1 2002 RNase A, a model protein for oxidative folding studies, has four native disulfide bonds. Disulfides 72-81 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 11982363-0 2002 Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A. Disulfides 49-58 ribonuclease A family member 1, pancreatic Homo sapiens 180-187 14529290-2 2003 To create a more efficient redox buffer for the in vitro folding of disulfide containing proteins, aromatic thiols were investigated for their ability to increase the folding rate of scrambled RNase A. Disulfides 68-77 ribonuclease A family member 1, pancreatic Homo sapiens 193-200 14529290-3 2003 Scrambled RNase A is fully oxidized RNase A with a relatively random distribution of disulfide bonds. Disulfides 85-94 ribonuclease A family member 1, pancreatic Homo sapiens 10-17 12795589-5 2003 It is shown here that there is a 10-fold increase in the propensity of the unfolded reduced forms of RNase A to form the native set of disulfides directly, compared to the propensity under strongly denaturing conditions (4-6 M GdnHCl). Disulfides 135-145 ribonuclease A family member 1, pancreatic Homo sapiens 101-108 12011044-4 2002 Scrambled RNase A (scRNase A), a misfolded protein, only slowly refolds spontaneously into an active form because of the rate-limiting unfolding of misfolded disulfide isomers. Disulfides 158-167 ribonuclease A family member 1, pancreatic Homo sapiens 10-17 11982363-6 2002 The application of this method enabled us to populate and, in turn, study the key intermediates with two native disulfide bonds on the oxidative folding pathway of RNase A; it also facilitated the isolation of des [58-110] and des [26-84], the other two native-like structured des species whose isolation had thus far not been possible. Disulfides 112-121 ribonuclease A family member 1, pancreatic Homo sapiens 164-171 11555655-5 2001 The addition of a non-native disulfide bond to ERDD RNase 1 not only increases the conformational stability of the enzyme but also increases its cytotoxicity such that its IC(50) value is only 8-fold greater than that of Onconase. Disulfides 29-38 ribonuclease A family member 1, pancreatic Homo sapiens 52-59 10920260-0 2000 Stabilization of human RNase 1 by introduction of a disulfide bond between residues 4 and 118. Disulfides 52-61 ribonuclease A family member 1, pancreatic Homo sapiens 23-30 11206080-1 2000 The folding of ribonuclease A (RNase A) has been extensively studied by characterizing the disulfide containing intermediates using different experimental conditions and analytical techniques. Disulfides 91-100 ribonuclease A family member 1, pancreatic Homo sapiens 15-29 11206080-1 2000 The folding of ribonuclease A (RNase A) has been extensively studied by characterizing the disulfide containing intermediates using different experimental conditions and analytical techniques. Disulfides 91-100 ribonuclease A family member 1, pancreatic Homo sapiens 31-38 11206080-3 2000 We have studied the oxidative folding of a RNase A derivative containing at position 67 the substitution Asn --> isoAsp where the local structure of the loop 65-72 has been modified keeping intact the C65-C72 disulfide bond. Disulfides 212-221 ribonuclease A family member 1, pancreatic Homo sapiens 43-50 11009618-5 2000 By comparison of the folding kinetics of the mutants with that of wild-type RNase A, the contribution of each disulfide bond to the folding process has been evaluated. Disulfides 110-119 ribonuclease A family member 1, pancreatic Homo sapiens 76-83 11009618-8 2000 The removal of the C58-C110 and C26-C84 disulfide bonds has a dramatic effect on the kinetics of RNase A folding. Disulfides 40-49 ribonuclease A family member 1, pancreatic Homo sapiens 97-104 10920260-2 2000 The 4-118CL RNase 1 that refolded under redox conditions was a monomer without free SH groups and retained 11% of the activity of the wild-type recombinant RNase 1, indicating that the mutant enzyme was correctly folded with the formation of an additional disulfide bond between Cys4 and Cys118. Disulfides 256-265 ribonuclease A family member 1, pancreatic Homo sapiens 12-19 10920260-2 2000 The 4-118CL RNase 1 that refolded under redox conditions was a monomer without free SH groups and retained 11% of the activity of the wild-type recombinant RNase 1, indicating that the mutant enzyme was correctly folded with the formation of an additional disulfide bond between Cys4 and Cys118. Disulfides 256-265 ribonuclease A family member 1, pancreatic Homo sapiens 156-163 9562551-3 1998 RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively. Disulfides 78-87 ribonuclease A family member 1, pancreatic Homo sapiens 95-109 10821658-6 2000 Forming a mixed disulfide between the side chain of Cys41 of K41C RNase A and cysteamine replaces the amino group and increases k(cat)/K(m) by 10(3)-fold. Disulfides 16-25 ribonuclease A family member 1, pancreatic Homo sapiens 66-73 10677237-21 2000 The differences are largely due to the four disulfide bonds in RNase A, which stabilize adjacent structures. Disulfides 44-53 ribonuclease A family member 1, pancreatic Homo sapiens 63-70 10036174-4 1999 When a sample of partially denatured RNase A was placed under mild reducing conditions (0.2-1 mM dithiothreitol for 10 min), the disulfide bonds of the native RNase A remain intact, whereas those of scrambled isomers become fully reduced. Disulfides 129-138 ribonuclease A family member 1, pancreatic Homo sapiens 37-44 10036174-4 1999 When a sample of partially denatured RNase A was placed under mild reducing conditions (0.2-1 mM dithiothreitol for 10 min), the disulfide bonds of the native RNase A remain intact, whereas those of scrambled isomers become fully reduced. Disulfides 129-138 ribonuclease A family member 1, pancreatic Homo sapiens 159-166 9649343-9 1998 The global solvent exposure and the hydrodynamic volume of the denatured protein are much less than for maximally unfolded disulfide-intact RNase A. Disulfides 123-132 ribonuclease A family member 1, pancreatic Homo sapiens 140-147 9578571-3 1998 Previous studies revealed some of the structural features of Ang that underlie its catalytic inefficiency: Gln-117 blocks the space corresponding to the pyrimidine binding site of RNase A and Ang lacks the disulfide loop 65-72 that forms most of the purine binding site of RNase A. Disulfides 206-215 ribonuclease A family member 1, pancreatic Homo sapiens 180-187 9578571-3 1998 Previous studies revealed some of the structural features of Ang that underlie its catalytic inefficiency: Gln-117 blocks the space corresponding to the pyrimidine binding site of RNase A and Ang lacks the disulfide loop 65-72 that forms most of the purine binding site of RNase A. Disulfides 206-215 ribonuclease A family member 1, pancreatic Homo sapiens 273-280 10753451-4 2000 Protein refolding and renaturation were estimated by the change in the number of disulfide bonds of RNase A and the recovery of the enzymatic activity, respectively. Disulfides 81-90 ribonuclease A family member 1, pancreatic Homo sapiens 100-107 10753451-6 2000 However, the formation of disulfide bonds of reduced RNase A was accelerated by adding the modified microspheres, and the rate of renaturation was increased depending on the amount of charged DTT and the reaction time of the immobilization. Disulfides 26-35 ribonuclease A family member 1, pancreatic Homo sapiens 53-60 10753451-8 2000 The protein adsorption data demonstrated that the disulfide moieties of the modified microspheres react with the thiol moieties of the reduced RNase A to form a mixed disulfide. Disulfides 50-59 ribonuclease A family member 1, pancreatic Homo sapiens 143-150 10753451-8 2000 The protein adsorption data demonstrated that the disulfide moieties of the modified microspheres react with the thiol moieties of the reduced RNase A to form a mixed disulfide. Disulfides 167-176 ribonuclease A family member 1, pancreatic Homo sapiens 143-150 11013399-3 2000 Reduced and carboxyamidated ribonuclease A (RCAM) is a member of a class of disulfide-free RNase A molecules believed to be random coils (extensively denatured) in aqueous solution. Disulfides 76-85 ribonuclease A family member 1, pancreatic Homo sapiens 91-98 9562551-3 1998 RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively. Disulfides 78-87 ribonuclease A family member 1, pancreatic Homo sapiens 111-118 9315864-9 1997 The structural analysis of the intermediates formed during the refolding of RNase A showed for the first time that Grx is actually able to catalyze both formation and reduction of mixed disulfides involving glutatione. Disulfides 186-196 ribonuclease A family member 1, pancreatic Homo sapiens 76-83 9080194-3 1997 The presence of four disulfide bonds and the existence of two cis peptide bonds preceding prolines in the native state have complicated the analysis of the folding pathway of RNase A. Disulfides 21-30 ribonuclease A family member 1, pancreatic Homo sapiens 175-182 8639587-0 1996 Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A. Disulfides 34-43 ribonuclease A family member 1, pancreatic Homo sapiens 81-95 8639587-1 1996 The one-disulfide intermediates formed during the oxidative refolding of ribonuclease A (RNase A) have been characterized. Disulfides 8-17 ribonuclease A family member 1, pancreatic Homo sapiens 73-87 8639587-1 1996 The one-disulfide intermediates formed during the oxidative refolding of ribonuclease A (RNase A) have been characterized. Disulfides 8-17 ribonuclease A family member 1, pancreatic Homo sapiens 89-96 1400510-1 1992 Angiogenin is a 14.4-kDa human plasma protein with 65% homology to RNase A that retains the key active site residues and three of the four RNase A disulfide bonds. Disulfides 147-156 ribonuclease A family member 1, pancreatic Homo sapiens 67-74 34664930-3 2021 Cytotoxic ribonuclease A (RNase A) was effectively caged in the matrix of disulfide-hybridized silica NPs (encapsulation efficiency of ~64%), which were further functionalized with cancer targeting capability via surface imprinting with SA as imprinting template. Disulfides 74-83 ribonuclease A family member 1, pancreatic Homo sapiens 26-33