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1674 related items for PubMed ID: 27844185

  • 1. A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.
    Rozentur-Shkop E, Goobes G, Chill JH.
    J Biomol NMR; 2016 Dec; 66(4):243-257. PubMed ID: 27844185
    [Abstract] [Full Text] [Related]

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  • 3. The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein Interactions: A Structural View.
    Sokolik CG, Qassem N, Chill JH.
    Biomolecules; 2020 Jul 21; 10(7):. PubMed ID: 32708183
    [Abstract] [Full Text] [Related]

  • 4. NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein.
    Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH.
    Biophys J; 2013 Jul 16; 105(2):481-93. PubMed ID: 23870269
    [Abstract] [Full Text] [Related]

  • 5. Molecular Dynamics Simulations Combined with Nuclear Magnetic Resonance and/or Small-Angle X-ray Scattering Data for Characterizing Intrinsically Disordered Protein Conformational Ensembles.
    Chan-Yao-Chong M, Durand D, Ha-Duong T.
    J Chem Inf Model; 2019 May 28; 59(5):1743-1758. PubMed ID: 30840442
    [Abstract] [Full Text] [Related]

  • 6. NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
    Kurzbach D, Kontaxis G, Coudevylle N, Konrat R.
    Adv Exp Med Biol; 2015 May 28; 870():149-85. PubMed ID: 26387102
    [Abstract] [Full Text] [Related]

  • 7. Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.
    Arai M, Sugase K, Dyson HJ, Wright PE.
    Proc Natl Acad Sci U S A; 2015 Aug 04; 112(31):9614-9. PubMed ID: 26195786
    [Abstract] [Full Text] [Related]

  • 8. Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.
    Kragelj J, Ozenne V, Blackledge M, Jensen MR.
    Chemphyschem; 2013 Sep 16; 14(13):3034-45. PubMed ID: 23794453
    [Abstract] [Full Text] [Related]

  • 9. Triple-color FRET analysis reveals conformational changes in the WIP-WASp actin-regulating complex.
    Fried S, Reicher B, Pauker MH, Eliyahu S, Matalon O, Noy E, Chill J, Barda-Saad M.
    Sci Signal; 2014 Jun 24; 7(331):ra60. PubMed ID: 24962707
    [Abstract] [Full Text] [Related]

  • 10. Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters.
    Kragelj J, Blackledge M, Jensen MR.
    Adv Exp Med Biol; 2015 Jun 24; 870():123-47. PubMed ID: 26387101
    [Abstract] [Full Text] [Related]

  • 11. New Structural Insights into Formation of the Key Actin Regulating WIP-WASp Complex Determined by NMR and Molecular Imaging.
    Halle-Bikovski A, Fried S, Rozentur-Shkop E, Biber G, Shaked H, Joseph N, Barda-Saad M, Chill JH.
    ACS Chem Biol; 2018 Jan 19; 13(1):100-109. PubMed ID: 29215267
    [Abstract] [Full Text] [Related]

  • 12. Improved validation of IDP ensembles by one-bond Cα-Hα scalar couplings.
    Gapsys V, Narayanan RL, Xiang S, de Groot BL, Zweckstetter M.
    J Biomol NMR; 2015 Nov 19; 63(3):299-307. PubMed ID: 26433382
    [Abstract] [Full Text] [Related]

  • 13. A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities.
    Kauffmann C, Kazimierczuk K, Schwarz TC, Konrat R, Zawadzka-Kazimierczuk A.
    J Biomol NMR; 2020 May 19; 74(4-5):257-265. PubMed ID: 32239382
    [Abstract] [Full Text] [Related]

  • 14. Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments.
    Milles S, Salvi N, Blackledge M, Jensen MR.
    Prog Nucl Magn Reson Spectrosc; 2018 Dec 19; 109():79-100. PubMed ID: 30527137
    [Abstract] [Full Text] [Related]

  • 15. Ensemble characterization of an intrinsically disordered FG-Nup peptide and its F>A mutant in DMSO-d6.
    Reid KM, Sunanda P, Raghothama S, Krishnan VV.
    Biopolymers; 2017 Nov 19; 108(6):. PubMed ID: 28734076
    [Abstract] [Full Text] [Related]

  • 16. Generating Intrinsically Disordered Protein Conformational Ensembles from a Database of Ramachandran Space Pair Residue Probabilities Using a Markov Chain.
    Cukier RI.
    J Phys Chem B; 2018 Oct 04; 122(39):9087-9101. PubMed ID: 30204435
    [Abstract] [Full Text] [Related]

  • 17. Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between the c-Crk N-SH3 domain and the peptide Sos.
    Xue Y, Yuwen T, Zhu F, Skrynnikov NR.
    Biochemistry; 2014 Oct 21; 53(41):6473-95. PubMed ID: 25207671
    [Abstract] [Full Text] [Related]

  • 18. Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
    Kosol S, Contreras-Martos S, Cedeño C, Tompa P.
    Molecules; 2013 Sep 04; 18(9):10802-28. PubMed ID: 24008243
    [Abstract] [Full Text] [Related]

  • 19. Longitudinal relaxation properties of (1)H(N) and (1)H(α) determined by direct-detected (13)C NMR experiments to study intrinsically disordered proteins (IDPs).
    Hošek T, Gil-Caballero S, Pierattelli R, Brutscher B, Felli IC.
    J Magn Reson; 2015 May 04; 254():19-26. PubMed ID: 25771525
    [Abstract] [Full Text] [Related]

  • 20. Intrinsically disordered protein-specific force field CHARMM36IDPSFF.
    Liu H, Song D, Lu H, Luo R, Chen HF.
    Chem Biol Drug Des; 2018 Oct 04; 92(4):1722-1735. PubMed ID: 29808548
    [Abstract] [Full Text] [Related]

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