These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
2. The unfolding mechanism and the disulfide structures of denatured lysozyme. Chang JY, Li L. FEBS Lett; 2002 Jan 30; 511(1-3):73-8. PubMed ID: 11821052 [Abstract] [Full Text] [Related]
3. Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine beta-trypsin. Krokoszynska I, Dadlez M, Otlewski J. J Mol Biol; 1998 Jan 23; 275(3):503-13. PubMed ID: 9466927 [Abstract] [Full Text] [Related]
5. Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide. Chang JY, Ballatore A. J Protein Chem; 2000 May 23; 19(4):299-310. PubMed ID: 11043935 [Abstract] [Full Text] [Related]
6. The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin. Chang JY, Li L. J Biol Chem; 2001 Mar 30; 276(13):9705-12. PubMed ID: 11118458 [Abstract] [Full Text] [Related]
7. The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers. Chang JY, Li L. J Protein Chem; 2002 Mar 30; 21(3):203-13. PubMed ID: 12018622 [Abstract] [Full Text] [Related]
8. Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability. Kowalski JM, Parekh RN, Wittrup KD. Biochemistry; 1998 Feb 03; 37(5):1264-73. PubMed ID: 9477952 [Abstract] [Full Text] [Related]
9. 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 22; 257(1):188-98. PubMed ID: 8632454 [Abstract] [Full Text] [Related]
10. Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor. Ma LC, Anderson S. Biochemistry; 1997 Mar 25; 36(12):3728-36. PubMed ID: 9132026 [Abstract] [Full Text] [Related]
11. The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor. Chang JY, Li L, Canals F, Aviles FX. J Biol Chem; 2000 May 12; 275(19):14205-11. PubMed ID: 10799497 [Abstract] [Full Text] [Related]
12. The unfolding pathway of leech carboxypeptidase inhibitor. Salamanca S, Villegas V, Vendrell J, Li L, Aviles FX, Chang JY. J Biol Chem; 2002 May 17; 277(20):17538-43. PubMed ID: 11893741 [Abstract] [Full Text] [Related]
13. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. J Mol Biol; 1992 Apr 20; 224(4):905-11. PubMed ID: 1373775 [Abstract] [Full Text] [Related]
14. Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding. Li R, Battiste JL, Woodward C. Biochemistry; 2002 Feb 19; 41(7):2246-53. PubMed ID: 11841216 [Abstract] [Full Text] [Related]
15. "Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor. Liu Y, Breslauer K, Anderson S. Biochemistry; 1997 May 06; 36(18):5323-35. PubMed ID: 9154914 [Abstract] [Full Text] [Related]
16. Comparison of complexes formed by a crustacean and a vertebrate trypsin with bovine pancreatic trypsin inhibitor - the key to achieving extreme stability? Molnár T, Vörös J, Szeder B, Takáts K, Kardos J, Katona G, Gráf L. FEBS J; 2013 Nov 06; 280(22):5750-63. PubMed ID: 24034223 [Abstract] [Full Text] [Related]
17. Analysis of the extent of unfolding of denatured insulin-like growth factor. Chang JY, Märki W, Lai PH. Protein Sci; 1999 Jul 06; 8(7):1463-8. PubMed ID: 10422834 [Abstract] [Full Text] [Related]
18. The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI. Chang JY. Biochemistry; 1996 Sep 10; 35(36):11702-9. PubMed ID: 8794751 [Abstract] [Full Text] [Related]
19. Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers. Chang JY. J Biol Chem; 1999 Jan 01; 274(1):123-8. PubMed ID: 9867819 [Abstract] [Full Text] [Related]
20. Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds. Hurle MR, Marks CB, Kosen PA, Anderson S, Kuntz ID. Biochemistry; 1990 May 08; 29(18):4410-9. PubMed ID: 1693524 [Abstract] [Full Text] [Related] Page: [Next] [New Search]