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References from The credentials for Ribonuclease A to be catalytically active: The prerequisite of oxidative protein folding. Local targets link to admitted publications; unresolved targets remain external evidence.
Folding of small disulfide-rich proteins: clarifying the puzzle
10.1016/j.tibs.2006.03.005 · 2006 · External reference
The protein disulfide isomerase family: key players in health and disease
10.1089/ars.2011.4439 · 2012 · External reference
Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism
10.1021/bi201075b · 2011 · External reference
The catalytic diversity of RNAs
10.1038/nrm1647 · 2005 · External reference
Peptidyl-prolyl cis-trams isomerases, a superfamily of ubiquitous folding catalysts
10.1007/s000180050299 · 1999 · External reference
Nature of the unfolded state of ribonuclease a: effect of Cis-trans X- pro peptide bond isomerization
10.1021/bi960745a · 1996 · External reference
A very fast phase in the refolding of disulfide-intact ribonuclease a: implications for the refolding and unfolding pathways
10.1021/bi00175a022 · 1994 · External reference
Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease a missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease a and kinetic roles of Cys65 and Cys72
10.1021/bi9725327 · 1998 · External reference
Catalysis of protein folding by prolyl isomerase
10.1038/329268a0 · 1987 · External reference
K.R. Acahrya, high-resolution crystal structures of ribonuclease a complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors
10.1110/ps.03196603 · 2003 · External reference
The case of oxidative folding of ribonuclease A: factors impacting fold maturation of ER-processed proteins
2011 · External reference
The structure-forming juncture in oxidative protein folding: what happens in the ER?
10.1007/5584_2017_88 · 2017 · External reference
Oxidative folding of proteins
10.1021/ar000063m · 2000 · External reference
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
10.1016/s0021-9258(18)37859-1 · 1988 · External reference
Ribonuclease A
10.1021/cr960427h · 1998 · External reference
Mechanisms of disulfide bond formation in nascent polypeptides entering the secretory pathway
1994 · External reference
Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways
10.1021/bi972823f · 1998 · External reference
Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways
10.1021/bi972822n · 1998 · External reference
Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution
10.1021/bi00061a027 · 1993 · External reference
Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration
10.1021/bi00061a028 · 1993 · External reference
The role of human ribonuclease a family in health and diseases: a systematic review
10.1016/j.isci.2022.105284 · 2022 · External reference
Disulphide bridges in globular proteins
10.1016/0022-2836(81)90515-5 · 1981 · External reference
Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: further insights into the folding process
10.1021/bi990570f · 1999 · External reference
Disulfide bonds and protein folding
10.1021/bi992922o · 2000 · External reference
Two new structured intermediates in the oxidative folding of RNase A
10.1016/s0014-5793(99)01391-5 · 1999 · External reference
Structural determinants of oxidative folding in proteins
10.1073/pnas.041615798 · 2001 · External reference
Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins
10.1021/bi010409g · 2001 · External reference
Protein disulfide isomerase
10.1016/s1570-9639(04)00063-9 · 2004 · External reference
The refined crystal structure of ribonuclease A at 2.0 A resolution
10.1016/s0021-9258(19)68195-0 · 1982 · External reference
Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A
10.1021/bi960090d · 1996 · External reference
Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond
10.1021/bi980086x · 1998 · External reference
The structure-forming juncture in oxidative protein folding: what happens in the ER?
10.1007/5584_2017_88 · ExternalCitation · doi-reference
Peptidyl-prolyl cis-trams isomerases, a superfamily of ubiquitous folding catalysts
10.1007/s000180050299 · ExternalCitation · doi-reference
Disulphide bridges in globular proteins
10.1016/0022-2836(81)90515-5 · ExternalCitation · doi-reference
The role of human ribonuclease a family in health and diseases: a systematic review
10.1016/j.isci.2022.105284 · ExternalCitation · doi-reference
Folding of small disulfide-rich proteins: clarifying the puzzle
10.1016/j.tibs.2006.03.005 · ExternalCitation · doi-reference
Two new structured intermediates in the oxidative folding of RNase A
10.1016/s0014-5793(99)01391-5 · ExternalCitation · doi-reference
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
10.1016/s0021-9258(18)37859-1 · ExternalCitation · doi-reference
The refined crystal structure of ribonuclease A at 2.0 A resolution
10.1016/s0021-9258(19)68195-0 · ExternalCitation · doi-reference
Protein disulfide isomerase
10.1016/s1570-9639(04)00063-9 · ExternalCitation · doi-reference
Oxidative folding of proteins
10.1021/ar000063m · ExternalCitation · doi-reference
Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution
10.1021/bi00061a027 · ExternalCitation · doi-reference
Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration
10.1021/bi00061a028 · ExternalCitation · doi-reference
A very fast phase in the refolding of disulfide-intact ribonuclease a: implications for the refolding and unfolding pathways
10.1021/bi00175a022 · ExternalCitation · doi-reference
Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins
10.1021/bi010409g · ExternalCitation · doi-reference
Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism
10.1021/bi201075b · ExternalCitation · doi-reference
Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A
10.1021/bi960090d · ExternalCitation · doi-reference
Nature of the unfolded state of ribonuclease a: effect of Cis-trans X- pro peptide bond isomerization
10.1021/bi960745a · ExternalCitation · doi-reference
Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease a missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease a and kinetic roles of Cys65 and Cys72
10.1021/bi9725327 · ExternalCitation · doi-reference
Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways
10.1021/bi972822n · ExternalCitation · doi-reference
Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways
10.1021/bi972823f · ExternalCitation · doi-reference
Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond
10.1021/bi980086x · ExternalCitation · doi-reference
Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: further insights into the folding process
10.1021/bi990570f · ExternalCitation · doi-reference
Disulfide bonds and protein folding
10.1021/bi992922o · ExternalCitation · doi-reference
Ribonuclease A
10.1021/cr960427h · ExternalCitation · doi-reference
Catalysis of protein folding by prolyl isomerase
10.1038/329268a0 · ExternalCitation · doi-reference
The catalytic diversity of RNAs
10.1038/nrm1647 · ExternalCitation · doi-reference
Structural determinants of oxidative folding in proteins
10.1073/pnas.041615798 · ExternalCitation · doi-reference
The protein disulfide isomerase family: key players in health and disease
10.1089/ars.2011.4439 · ExternalCitation · doi-reference
K.R. Acahrya, high-resolution crystal structures of ribonuclease a complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors
10.1110/ps.03196603 · ExternalCitation · doi-reference
