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Journal Abstract Search

248 related items for PubMed ID: 18384808

  • 1. The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2008 May 02; 378(3):715-25. PubMed ID: 18384808
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  • 5. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.
    Jennings PA, Wright PE.
    Science; 1993 Nov 05; 262(5135):892-6. PubMed ID: 8235610
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  • 6. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.
    Cavagnero S, Dyson HJ, Wright PE.
    J Mol Biol; 1999 Jan 08; 285(1):269-82. PubMed ID: 9878405
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  • 9. Energetic frustration of apomyoglobin folding: role of the B helix.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2010 Mar 12; 396(5):1319-28. PubMed ID: 20043917
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  • 10. Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
    Nishimura C, Dyson HJ, Wright PE.
    Proc Natl Acad Sci U S A; 2005 Mar 29; 102(13):4765-70. PubMed ID: 15769860
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  • 12. Experimental studies of pathways of protein folding.
    Baldwin RL.
    Ciba Found Symp; 1991 Mar 29; 161():190-201; discussion 201-5. PubMed ID: 1667633
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  • 19. How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.
    Dyson HJ, Wright PE.
    Acc Chem Res; 2017 Jan 17; 50(1):105-111. PubMed ID: 28032989
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  • 20. Molten globular characteristics of the native state of apomyoglobin.
    Lin L, Pinker RJ, Forde K, Rose GD, Kallenbach NR.
    Nat Struct Biol; 1994 Jul 17; 1(7):447-52. PubMed ID: 7664063
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