92 related articles for article (PubMed ID: 1285385)
1. Protein folding pathways determined using disulphide bonds.
Creighton TE
Bioessays; 1992 Mar; 14(3):195-9. PubMed ID: 1285385
[TBL] [Abstract][Full Text] [Related]
2. Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein.
Darby NJ; Creighton TE
J Mol Biol; 1993 Aug; 232(3):873-96. PubMed ID: 7689114
[TBL] [Abstract][Full Text] [Related]
3. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates.
Darby NJ; Morin PE; Talbo G; Creighton TE
J Mol Biol; 1995 Jun; 249(2):463-77. PubMed ID: 7540214
[TBL] [Abstract][Full Text] [Related]
4. 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.
van Mierlo CP; Kemmink J; Neuhaus D; Darby NJ; Creighton TE
J Mol Biol; 1994 Jan; 235(3):1044-61. PubMed ID: 7507172
[TBL] [Abstract][Full Text] [Related]
5. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase.
Weissman JS; Kim PS
Nature; 1993 Sep; 365(6442):185-8. PubMed ID: 7690463
[TBL] [Abstract][Full Text] [Related]
6. Mutational analysis of hydrogen bonding residues in the BPTI folding pathway.
Bulaj G; Goldenberg DP
J Mol Biol; 2001 Oct; 313(3):639-56. PubMed ID: 11676545
[TBL] [Abstract][Full Text] [Related]
7. 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.
van Mierlo CP; Darby NJ; Keeler J; Neuhaus D; Creighton TE
J Mol Biol; 1993 Feb; 229(4):1125-46. PubMed ID: 7680380
[TBL] [Abstract][Full Text] [Related]
8. Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding.
Dadlez M; Kim PS
Biochemistry; 1996 Dec; 35(50):16153-64. PubMed ID: 8973187
[TBL] [Abstract][Full Text] [Related]
9. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor.
Staley JP; Kim PS
Nature; 1990 Apr; 344(6267):685-8. PubMed ID: 1691452
[TBL] [Abstract][Full Text] [Related]
10. Disulphide-coupled protein folding pathways.
Creighton T
Philos Trans R Soc Lond B Biol Sci; 1995 Apr; 348(1323):5-10. PubMed ID: 7770487
[TBL] [Abstract][Full Text] [Related]
11. Hydrophobic interactions accelerate early stages of the folding of BPTI.
Dadlez M
Biochemistry; 1997 Mar; 36(10):2788-97. PubMed ID: 9062106
[TBL] [Abstract][Full Text] [Related]
12. Phi-values for BPTI folding intermediates and implications for transition state analysis.
Bulaj G; Goldenberg DP
Nat Struct Biol; 2001 Apr; 8(4):326-30. PubMed ID: 11276252
[TBL] [Abstract][Full Text] [Related]
13. On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes.
Creighton TE; Bagley CJ; Cooper L; Darby NJ; Freedman RB; Kemmink J; Sheikh A
J Mol Biol; 1993 Aug; 232(4):1176-96. PubMed ID: 7690407
[TBL] [Abstract][Full Text] [Related]
14. Disulfide bonds in protein folding studies: friends or foes?
Dadlez M
Acta Biochim Pol; 1997; 44(3):433-52. PubMed ID: 9511956
[TBL] [Abstract][Full Text] [Related]
15. Conformation of native, reduced and [5-55]Ala bovine pancreatic trypsin inhibitor in the gas phase.
Nesatiy V; Chen YL; Collings BA; Douglas DJ
Rapid Commun Mass Spectrom; 1998; 12(1):40-4. PubMed ID: 9450353
[TBL] [Abstract][Full Text] [Related]
16. Evidence for the underlying cause of diversity of the disulfide folding pathway.
Chang JY
Biochemistry; 2004 Apr; 43(15):4522-9. PubMed ID: 15078098
[TBL] [Abstract][Full Text] [Related]
17. 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.
Zdanowski K; Dadlez M
J Mol Biol; 1999 Mar; 287(2):433-45. PubMed ID: 10080904
[TBL] [Abstract][Full Text] [Related]
18. Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor.
Ma LC; Anderson S
Biochemistry; 1997 Mar; 36(12):3728-36. PubMed ID: 9132026
[TBL] [Abstract][Full Text] [Related]
19. Modeling the role of disulfide bonds in protein folding: entropic barriers and pathways.
Camacho CJ; Thirumalai D
Proteins; 1995 May; 22(1):27-40. PubMed ID: 7675784
[TBL] [Abstract][Full Text] [Related]
20. 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.
Kortemme T; Hollecker M; Kemmink J; Creighton TE
J Mol Biol; 1996 Mar; 257(1):188-98. PubMed ID: 8632454
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]