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 *

304 related articles for article (PubMed ID: 22517863)

  • 1. Structure of an intermediate state in protein folding and aggregation.
    Neudecker P; Robustelli P; Cavalli A; Walsh P; Lundström P; Zarrine-Afsar A; Sharpe S; Vendruscolo M; Kay LE
    Science; 2012 Apr; 336(6079):362-6. PubMed ID: 22517863
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy.
    Neudecker P; Zarrine-Afsar A; Choy WY; Muhandiram DR; Davidson AR; Kay LE
    J Mol Biol; 2006 Nov; 363(5):958-76. PubMed ID: 16989862
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
    Korzhnev DM; Neudecker P; Zarrine-Afsar A; Davidson AR; Kay LE
    Biochemistry; 2006 Aug; 45(34):10175-83. PubMed ID: 16922492
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.
    Neudecker P; Zarrine-Afsar A; Davidson AR; Kay LE
    Proc Natl Acad Sci U S A; 2007 Oct; 104(40):15717-22. PubMed ID: 17898173
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.
    Libich DS; Tugarinov V; Ghirlando R; Clore GM
    Biochemistry; 2017 Feb; 56(7):903-906. PubMed ID: 28156097
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Insights into the folding and unfolding processes of wild-type and mutated SH3 domain by molecular dynamics and replica exchange molecular dynamics simulations.
    Chu WT; Zhang JL; Zheng QC; Chen L; Zhang HX
    PLoS One; 2013; 8(5):e64886. PubMed ID: 23734224
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.
    Neudecker P; Lundström P; Kay LE
    Biophys J; 2009 Mar; 96(6):2045-54. PubMed ID: 19289032
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy.
    Mittermaier A; Korzhnev DM; Kay LE
    Biochemistry; 2005 Nov; 44(47):15430-6. PubMed ID: 16300390
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain.
    Zarrine-Afsar A; Dahesh S; Davidson AR
    J Mol Biol; 2007 Oct; 373(3):764-74. PubMed ID: 17850820
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.
    Zhuravlev PI; Reddy G; Straub JE; Thirumalai D
    J Mol Biol; 2014 Jul; 426(14):2653-66. PubMed ID: 24846645
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
    Korzhnev DM; Salvatella X; Vendruscolo M; Di Nardo AA; Davidson AR; Dobson CM; Kay LE
    Nature; 2004 Jul; 430(6999):586-90. PubMed ID: 15282609
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.
    Lin SL; Zarrine-Afsar A; Davidson AR
    Protein Sci; 2009 Mar; 18(3):526-36. PubMed ID: 19241379
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain.
    Zarrine-Afsar A; Zhang Z; Schweiker KL; Makhatadze GI; Davidson AR; Chan HS
    Proteins; 2012 Mar; 80(3):858-70. PubMed ID: 22161863
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation.
    Bacarizo J; Martinez-Rodriguez S; Martin-Garcia JM; Andujar-Sanchez M; Ortiz-Salmeron E; Neira JL; Camara-Artigas A
    PLoS One; 2014; 9(12):e113224. PubMed ID: 25490095
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion.
    Hansen DF; Neudecker P; Vallurupalli P; Mulder FA; Kay LE
    J Am Chem Soc; 2010 Jan; 132(1):42-3. PubMed ID: 20000605
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding.
    Zarrine-Afsar A; Wallin S; Neculai AM; Neudecker P; Howell PL; Davidson AR; Chan HS
    Proc Natl Acad Sci U S A; 2008 Jul; 105(29):9999-10004. PubMed ID: 18626019
    [TBL] [Abstract][Full Text] [Related]  

  • 17. A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical Φ-value.
    Zarrine-Afsar A; Dahesh S; Davidson AR
    Proteins; 2012 May; 80(5):1343-9. PubMed ID: 22274997
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.
    Graña-Montes R; de Groot NS; Castillo V; Sancho J; Velazquez-Campoy A; Ventura S
    Antioxid Redox Signal; 2012 Jan; 16(1):1-15. PubMed ID: 21797671
    [TBL] [Abstract][Full Text] [Related]  

  • 19. A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.
    Karamanos TK; Pashley CL; Kalverda AP; Thompson GS; Mayzel M; Orekhov VY; Radford SE
    J Am Chem Soc; 2016 May; 138(19):6271-80. PubMed ID: 27117876
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.
    Korzhnev DM; Neudecker P; Mittermaier A; Orekhov VY; Kay LE
    J Am Chem Soc; 2005 Nov; 127(44):15602-11. PubMed ID: 16262426
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 16.