These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

171 related articles for article (PubMed ID: 9395082)

  • 1. Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
    Eliezer D; Jennings PA; Dyson HJ; Wright PE
    FEBS Lett; 1997 Nov; 417(1):92-6. PubMed ID: 9395082
    [TBL] [Abstract][Full Text] [Related]  

  • 2. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
    Yao J; Chung J; Eliezer D; Wright PE; Dyson HJ
    Biochemistry; 2001 Mar; 40(12):3561-71. PubMed ID: 11297422
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Is apomyoglobin a molten globule? Structural characterization by NMR.
    Eliezer D; Wright PE
    J Mol Biol; 1996 Nov; 263(4):531-8. PubMed ID: 8918936
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 92(12):5446-50. PubMed ID: 7777528
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 40(48):14459-67. PubMed ID: 11724558
    [TBL] [Abstract][Full Text] [Related]  

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

  • 7. The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure.
    Nishimura C; Dyson HJ; Wright PE
    J Mol Biol; 2008 May; 378(3):715-25. PubMed ID: 18384808
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding.
    Eliezer D; Yao J; Dyson HJ; Wright PE
    Nat Struct Biol; 1998 Feb; 5(2):148-55. PubMed ID: 9461081
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin.
    Fink AL; Oberg KA; Seshadri S
    Fold Des; 1998; 3(1):19-25. PubMed ID: 9502317
    [TBL] [Abstract][Full Text] [Related]  

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

  • 11. 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; 39(11):2894-901. PubMed ID: 10715109
    [TBL] [Abstract][Full Text] [Related]  

  • 12. High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded.
    Kitahara R; Yamada H; Akasaka K; Wright PE
    J Mol Biol; 2002 Jul; 320(2):311-9. PubMed ID: 12079388
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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; 2(6):869-76. PubMed ID: 8318892
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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; 46(14):4379-89. PubMed ID: 17367166
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.
    Jennings PA; Wright PE
    Science; 1993 Nov; 262(5135):892-6. PubMed ID: 8235610
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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; 102(13):4765-70. PubMed ID: 15769860
    [TBL] [Abstract][Full Text] [Related]  

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

  • 18. 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; 285(1):269-82. PubMed ID: 9878405
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin.
    Tcherkasskaya O; Ptitsyn OB
    Protein Eng; 1999 Jun; 12(6):485-90. PubMed ID: 10388845
    [TBL] [Abstract][Full Text] [Related]  

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

    [Next]    [New Search]
    of 9.