19 Article(s)Download |
PMID | Title | Pub. Year | #Total Relationships |
1 | 24750237 | Bovine pancreatic trypsin inhibitor is a new antifungal peptide that inhibits cellular magnesium uptake. | 2014 Jun | 1 |
2 | 10080904 | Stability of the residual structure in unfolded BPTI in different conditions of temperature and solvent composition measured by disulphide kinetics and double mutant cycle analysis. | 1999 Mar 26 | 1 |
3 | 9450353 | Conformation of native, reduced and [5-55]Ala bovine pancreatic trypsin inhibitor in the gas phase. | 1998 | 4 |
4 | 8632454 | Comparison of the (30-51, 14-38) two-disulphide folding intermediates of the homologous proteins dendrotoxin K and bovine pancreatic trypsin inhibitor by two-dimensional 1H nuclear magnetic resonance. | 1996 Mar 22 | 7 |
5 | 7540214 | Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates. | 1995 Jun 2 | 4 |
6 | 7552729 | A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor. | 1995 Aug | 1 |
7 | 8846225 | A kinetic explanation for the rearrangement pathway of BPTI folding. | 1995 Dec | 3 |
8 | 7507172 | 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. | 1994 Jan 21 | 2 |
9 | 7504737 | Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding. | 1993 Dec 5 | 1 |
10 | 7680380 | Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. | 1993 Feb 20 | 1 |
11 | 7689114 | Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein. | 1993 Aug 5 | 5 |
12 | 7690463 | Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. | 1993 Sep 9 | 1 |
13 | 7694758 | Structural features important for the biological activity of the potassium channel blocking dendrotoxins. | 1993 Oct | 1 |
14 | 1373775 | Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. | 1992 Apr 20 | 4 |
15 | 1960731 | (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. | 1991 Nov 20 | 1 |
16 | 1960732 | Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. | 1991 Nov 20 | 3 |
17 | 1691452 | Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor. | 1990 Apr 12 | 3 |
18 | 2466495 | On the relevance of non-random polypeptide conformations for protein folding. | 1988 Aug | 1 |
19 | 6196487 | Conformational change of a globular protein elucidated at atomic resolution. Theoretical and nuclear magnetic resonance study. | 1983 Nov 15 | 1 |