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Journal Abstract Search

437 related items for PubMed ID: 8235610

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2. Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.
    Cavagnero S, Nishimura C, Schwarzinger S, Dyson HJ, Wright PE.
    Biochemistry; 2001 Dec 04; 40(48):14459-67. PubMed ID: 11724558
    [Abstract] [Full Text] [Related]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. 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
    [Abstract] [Full Text] [Related]

  • 5. Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.
    Nishimura C.
    Proc Jpn Acad Ser B Phys Biol Sci; 2017 May 02; 93(1):10-27. PubMed ID: 28077807
    [Abstract] [Full Text] [Related]

  • 6. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.
    Loh SN, Kay MS, Baldwin RL.
    Proc Natl Acad Sci U S A; 1995 Jun 06; 92(12):5446-50. PubMed ID: 7777528
    [Abstract] [Full Text] [Related]

  • 7. Experimental studies of pathways of protein folding.
    Baldwin RL.
    Ciba Found Symp; 1991 Jun 06; 161():190-201; discussion 201-5. PubMed ID: 1667633
    [Abstract] [Full Text] [Related]

  • 8. Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2006 Jan 06; 355(1):139-56. PubMed ID: 16300787
    [Abstract] [Full Text] [Related]

  • 9. Molten globular characteristics of the native state of apomyoglobin.
    Lin L, Pinker RJ, Forde K, Rose GD, Kallenbach NR.
    Nat Struct Biol; 1994 Jul 06; 1(7):447-52. PubMed ID: 7664063
    [Abstract] [Full Text] [Related]

  • 10. The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2002 Sep 20; 322(3):483-9. PubMed ID: 12225742
    [Abstract] [Full Text] [Related]

  • 11. Structural characterization of partially folded intermediates of apomyoglobin H64F.
    Schwarzinger S, Mohana-Borges R, Kroon GJ, Dyson HJ, Wright PE.
    Protein Sci; 2008 Feb 20; 17(2):313-21. PubMed ID: 18227434
    [Abstract] [Full Text] [Related]

  • 12. Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding.
    Barrick D, Baldwin RL.
    Protein Sci; 1993 Jun 20; 2(6):869-76. PubMed ID: 8318892
    [Abstract] [Full Text] [Related]

  • 13. Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue.
    Garcia C, Nishimura C, Cavagnero S, Dyson HJ, Wright PE.
    Biochemistry; 2000 Sep 19; 39(37):11227-37. PubMed ID: 10985768
    [Abstract] [Full Text] [Related]

  • 14. Probing the non-native H helix translocation in apomyoglobin folding intermediates.
    Aoto PC, Nishimura C, Dyson HJ, Wright PE.
    Biochemistry; 2014 Jun 17; 53(23):3767-80. PubMed ID: 24857522
    [Abstract] [Full Text] [Related]

  • 15. How Ala-->Gly mutations in different helices affect the stability of the apomyoglobin molten globule.
    Luo Y, Baldwin RL.
    Biochemistry; 2001 May 01; 40(17):5283-9. PubMed ID: 11318652
    [Abstract] [Full Text] [Related]

  • 16. Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form.
    Kiefhaber T, Baldwin RL.
    J Mol Biol; 1995 Sep 08; 252(1):122-32. PubMed ID: 7666424
    [Abstract] [Full Text] [Related]

  • 17. Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin.
    Eliezer D, Chung J, Dyson HJ, Wright PE.
    Biochemistry; 2000 Mar 21; 39(11):2894-901. PubMed ID: 10715109
    [Abstract] [Full Text] [Related]

  • 18. Diffusive motions control the folding and unfolding kinetics of the apomyoglobin pH 4 molten globule intermediate.
    Ramos CH, Weisbuch S, Jamin M.
    Biochemistry; 2007 Apr 10; 46(14):4379-89. PubMed ID: 17367166
    [Abstract] [Full Text] [Related]

  • 19. Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin.
    Majorina MA, Balobanov VA, Uversky VN, Melnik BS.
    FEBS Lett; 2020 Oct 10; 594(20):3293-3304. PubMed ID: 32770670
    [Abstract] [Full Text] [Related]

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