The credentials for Ribonuclease A to be catalytically active: The prerequisite of oxidative protein folding

Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond

10.1021/bi980086x · doi-reference

Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A

10.1021/bi960090d · doi-reference

The refined crystal structure of ribonuclease A at 2.0 A resolution

10.1016/s0021-9258(19)68195-0 · doi-reference

Protein disulfide isomerase

10.1016/s1570-9639(04)00063-9 · doi-reference

Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins

10.1021/bi010409g · doi-reference

Structural determinants of oxidative folding in proteins

10.1073/pnas.041615798 · doi-reference

Two new structured intermediates in the oxidative folding of RNase A

10.1016/s0014-5793(99)01391-5 · doi-reference

Disulfide bonds and protein folding

10.1021/bi992922o · 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 · doi-reference

Disulphide bridges in globular proteins

10.1016/0022-2836(81)90515-5 · doi-reference

The role of human ribonuclease a family in health and diseases: a systematic review

10.1016/j.isci.2022.105284 · doi-reference

Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration

10.1021/bi00061a028 · doi-reference

Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution

10.1021/bi00061a027 · doi-reference

Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways

10.1021/bi972822n · doi-reference

Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways

10.1021/bi972823f · doi-reference

Ribonuclease A

10.1021/cr960427h · doi-reference

Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds

10.1016/s0021-9258(18)37859-1 · doi-reference

Oxidative folding of proteins

10.1021/ar000063m · doi-reference

The structure-forming juncture in oxidative protein folding: what happens in the ER?

10.1007/5584_2017_88 · 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 · doi-reference

Catalysis of protein folding by prolyl isomerase

10.1038/329268a0 · 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 · doi-reference

A very fast phase in the refolding of disulfide-intact ribonuclease a: implications for the refolding and unfolding pathways

10.1021/bi00175a022 · doi-reference

Nature of the unfolded state of ribonuclease a: effect of Cis-trans X- pro peptide bond isomerization

10.1021/bi960745a · doi-reference

Peptidyl-prolyl cis-trams isomerases, a superfamily of ubiquitous folding catalysts

10.1007/s000180050299 · doi-reference

The catalytic diversity of RNAs

10.1038/nrm1647 · doi-reference

Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism

10.1021/bi201075b · doi-reference

The protein disulfide isomerase family: key players in health and disease

10.1089/ars.2011.4439 · doi-reference

Folding of small disulfide-rich proteins: clarifying the puzzle

10.1016/j.tibs.2006.03.005 · doi-reference