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351 related items for PubMed ID: 9521769

  • 1. 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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  • 3. 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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  • 6. Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways.
    Rothwarf DM, Li YJ, Scheraga HA.
    Biochemistry; 1998 Mar 17; 37(11):3760-6. PubMed ID: 9521695
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  • 7. 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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  • 8. 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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  • 9. 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
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  • 10. 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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  • 11. Catalysis of the oxidative folding of bovine pancreatic ribonuclease A by protein disulfide isomerase.
    Shin HC, Scheraga HA.
    J Mol Biol; 2000 Jul 21; 300(4):995-1003. PubMed ID: 10891284
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  • 12. 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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  • 13. Shifting the competition between the intramolecular Reshuffling reaction and the direct oxidation reaction during the oxidative folding of kinetically trapped disulfide-insecure intermediates.
    Narayan M, Welker E, Wanjalla C, Xu G, Scheraga HA.
    Biochemistry; 2003 Sep 16; 42(36):10783-9. PubMed ID: 12962503
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  • 14. 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 16; 65(1):47-54. PubMed ID: 15686534
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  • 15. Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A.
    Dodge RW, Scheraga HA.
    Biochemistry; 1996 Feb 06; 35(5):1548-59. PubMed ID: 8634286
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  • 16. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.
    Ruoppolo M, Lundström-Ljung J, Talamo F, Pucci P, Marino G.
    Biochemistry; 1997 Oct 07; 36(40):12259-67. PubMed ID: 9315864
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  • 17. 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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  • 18. 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
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  • 19. Direct observation of conformational folding coupled with disulphide rearrangement by using a water-soluble selenoxide reagent--a case of oxidative regeneration of ribonuclease A under weakly basic conditions.
    Iwaoka M, Kumakura F, Yoneda M, Nakahara T, Henmi K, Aonuma H, Nakatani H, Tomoda S.
    J Biochem; 2008 Jul 14; 144(1):121-30. PubMed ID: 18407938
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  • 20. Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A.
    Ruoppolo M, Vinci F, Klink TA, Raines RT, Marino G.
    Biochemistry; 2000 Oct 03; 39(39):12033-42. PubMed ID: 11009618
    [Abstract] [Full Text] [Related]

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