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Catalysis of protein folding by prolyl isomerase

Data up to Jan 2025

Published1987
Citations488
References16

Total Citations Per Year

Abstract

References (16)

Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

1975 • 1,108 citations

Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding

1982 • 1,041 citations

The Preparation of Subtilisin-modified Ribonuclease and the Separation of the Peptide and Protein Components

1959 • 632 citations

Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization

1978 • 229 citations

Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme

1973 • 157 citations

Unfolding and refolding of the constant fragment of the immunoglobulin light chain

1982 • 124 citations

A Native‐Like Intermediate on the Ribonuclease A Folding Pathway

1981 • 118 citations

The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase

1985 • 113 citations

The Heterogeneity of Bovine Pancreatic Ribonuclease S*

1967 • 91 citations

Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.

1986 • 85 citations

The Primary Structure of Porcine Pancreatic Ribonuclease

1970 • 81 citations

Identification and characterization of the direct folding process of hen egg-white lysozyme

1982 • 65 citations

Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis

1984 • 59 citations

Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediates

1983 • 43 citations

Recombination of S-peptide with S-protein during folding of ribonuclease S

1979 • 38 citations

Folding mechanism of porcine ribonuclease

1986 • 25 citations

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Catalysis of protein folding by prolyl isomerase (1987) – Nature | Metascience Observatory Explorer