161 related articles for article (PubMed ID: 28156097)
1. 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]
2. Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.
Libich DS; Tugarinov V; Clore GM
Proc Natl Acad Sci U S A; 2015 Jul; 112(29):8817-23. PubMed ID: 26124125
[TBL] [Abstract][Full Text] [Related]
3. 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]
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. 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]
6. 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]
7. Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement.
Wälti MA; Libich DS; Clore GM
J Phys Chem Lett; 2018 Jun; 9(12):3368-3371. PubMed ID: 29869885
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. 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]
10. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.
Betancourt MR; Thirumalai D
J Mol Biol; 1999 Apr; 287(3):627-44. PubMed ID: 10092464
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.
Gupta AJ; Haldar S; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2014 Jul; 426(15):2739-54. PubMed ID: 24816391
[TBL] [Abstract][Full Text] [Related]
13. Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR.
Bezsonova I; Korzhnev DM; Prosser RS; Forman-Kay JD; Kay LE
Biochemistry; 2006 Apr; 45(15):4711-9. PubMed ID: 16605239
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. Thermodynamic stability and folding of GroEL minichaperones.
Golbik R; Zahn R; Harding SE; Fersht AR
J Mol Biol; 1998 Feb; 276(2):505-15. PubMed ID: 9512719
[TBL] [Abstract][Full Text] [Related]
16. Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR.
Libich DS; Fawzi NL; Ying J; Clore GM
Proc Natl Acad Sci U S A; 2013 Jul; 110(28):11361-6. PubMed ID: 23798407
[TBL] [Abstract][Full Text] [Related]
17. Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.
Tugarinov V; Kay LE
J Am Chem Soc; 2007 Aug; 129(30):9514-21. PubMed ID: 17628064
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding.
Bouvignies G; Kay LE
J Biomol NMR; 2012 Aug; 53(4):303-10. PubMed ID: 22689067
[TBL] [Abstract][Full Text] [Related]
20. Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity.
Zahn R; Perrett S; Fersht AR
J Mol Biol; 1996 Aug; 261(1):43-61. PubMed ID: 8760501
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
