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Journal Abstract Search

328 related items for PubMed ID: 10353840

  • 1. Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: further insights into the folding process.
    Volles MJ, Xu X, Scheraga HA.
    Biochemistry; 1999 Jun 01; 38(22):7284-93. PubMed ID: 10353840
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  • 3. Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A.
    Xu X, Rothwarf DM, Scheraga HA.
    Biochemistry; 1996 May 21; 35(20):6406-17. PubMed ID: 8639587
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  • 4. 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
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  • 8. Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins.
    Leung HJ, Xu G, Narayan M, Scheraga HA.
    J Pept Res; 2005 Jan 31; 65(1):47-54. PubMed ID: 15686534
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  • 11. 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
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  • 12. Assessing the magnitude of folding forces along the oxidative folding pathway of multi-disulfide-containing proteins.
    Narayan M, Xu G, Schultz SK, Scheraga HA.
    J Am Chem Soc; 2003 Dec 31; 125(52):16184-5. PubMed ID: 14692748
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  • 14. Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways.
    Rothwarf DM, Li YJ, Scheraga HA.
    Biochemistry; 1998 Mar 17; 37(11):3767-76. PubMed ID: 9521696
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  • 15. 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
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  • 16. Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins.
    Narayan M, Welker E, Scheraga HA.
    J Am Chem Soc; 2003 Feb 26; 125(8):2036-7. PubMed ID: 12590517
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  • 17. 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
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  • 19. Characterization of kinetic and thermodynamic phases in the prefolding process of bovine pancreatic ribonuclease A coupled with fast SS formation and SS reshuffling.
    Arai K, Kumakura F, Iwaoka M.
    Biochemistry; 2010 Dec 14; 49(49):10535-42. PubMed ID: 21062079
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  • 20. The effect of additional disulfide bonds on the stability and folding of ribonuclease A.
    Pecher P, Arnold U.
    Biophys Chem; 2009 Apr 14; 141(1):21-8. PubMed ID: 19155118
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