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Journal Abstract Search
971 related items for PubMed ID: 9188686
1. NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms. Shimotakahara S, Rios CB, Laity JH, Zimmerman DE, Scheraga HA, Montelione GT. Biochemistry; 1997 Jun 10; 36(23):6915-29. PubMed ID: 9188686 [Abstract] [Full Text] [Related]
2. Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A. Laity JH, Lester CC, Shimotakahara S, Zimmerman DE, Montelione GT, Scheraga HA. Biochemistry; 1997 Oct 21; 36(42):12683-99. PubMed ID: 9335525 [Abstract] [Full Text] [Related]
3. 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. Iwaoka M, Juminaga D, Scheraga HA. Biochemistry; 1998 Mar 31; 37(13):4490-501. PubMed ID: 9521769 [Abstract] [Full Text] [Related]
4. Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A. Shin HC, Narayan M, Song MC, Scheraga HA. Biochemistry; 2003 Oct 07; 42(39):11514-9. PubMed ID: 14516203 [Abstract] [Full Text] [Related]
5. Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond. Xu X, Scheraga HA. Biochemistry; 1998 May 19; 37(20):7561-71. PubMed ID: 9585571 [Abstract] [Full Text] [Related]
6. Regeneration studies of an analog of ribonuclease A missing disulfide bonds 65-72 and 40-95. Lester CC, Xu X, Laity JH, Shimotakahara S, Scheraga HA. Biochemistry; 1997 Oct 21; 36(42):13068-76. PubMed ID: 9335569 [Abstract] [Full Text] [Related]
7. Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions. Iwaoka M, Wedemeyer WJ, Scheraga HA. Biochemistry; 1999 Mar 02; 38(9):2805-15. PubMed ID: 10052952 [Abstract] [Full Text] [Related]
8. Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type protein in bovine pancreatic ribonuclease A: identification of specific regions of stable structure along the oxidative folding pathway. Laity JH, Montelione GT, Scheraga HA. Biochemistry; 1999 Dec 14; 38(50):16432-42. PubMed ID: 10600104 [Abstract] [Full Text] [Related]
9. The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Xu G, Narayan M, Scheraga HA. Biochemistry; 2005 Jul 19; 44(28):9817-23. PubMed ID: 16008366 [Abstract] [Full Text] [Related]
14. Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways. Talluri S, Rothwarf DM, Scheraga HA. Biochemistry; 1994 Aug 30; 33(34):10437-49. PubMed ID: 8068682 [Abstract] [Full Text] [Related]
17. Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A. Pearson MA, Karplus PA, Dodge RW, Laity JH, Scheraga HA. Protein Sci; 1998 May 30; 7(5):1255-8. PubMed ID: 9605332 [Abstract] [Full Text] [Related]
18. 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]