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147 related items for PubMed ID: 18507376

  • 1. Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein.
    Jensen MR, Houben K, Lescop E, Blanchard L, Ruigrok RW, Blackledge M.
    J Am Chem Soc; 2008 Jun 25; 130(25):8055-61. PubMed ID: 18507376
    [Abstract] [Full Text] [Related]

  • 2. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.
    Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE.
    J Mol Biol; 2004 Jul 23; 340(5):1131-42. PubMed ID: 15236972
    [Abstract] [Full Text] [Related]

  • 3. Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.
    Nodet G, Salmon L, Ozenne V, Meier S, Jensen MR, Blackledge M.
    J Am Chem Soc; 2009 Dec 16; 131(49):17908-18. PubMed ID: 19908838
    [Abstract] [Full Text] [Related]

  • 4. Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.
    Dames SA, Aregger R, Vajpai N, Bernado P, Blackledge M, Grzesiek S.
    J Am Chem Soc; 2006 Oct 18; 128(41):13508-14. PubMed ID: 17031964
    [Abstract] [Full Text] [Related]

  • 5. Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.
    Blocquel D, Habchi J, Gruet A, Blangy S, Longhi S.
    Mol Biosyst; 2012 Jan 18; 8(1):392-410. PubMed ID: 22108848
    [Abstract] [Full Text] [Related]

  • 6. On the origin of NMR dipolar waves in transient helical elements of partially folded proteins.
    Jensen MR, Blackledge M.
    J Am Chem Soc; 2008 Aug 27; 130(34):11266-7. PubMed ID: 18665596
    [Abstract] [Full Text] [Related]

  • 7. Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy.
    Belle V, Rouger S, Costanzo S, Liquière E, Strancar J, Guigliarelli B, Fournel A, Longhi S.
    Proteins; 2008 Dec 27; 73(4):973-88. PubMed ID: 18536007
    [Abstract] [Full Text] [Related]

  • 8. Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings.
    Fieber W, Kristjansdottir S, Poulsen FM.
    J Mol Biol; 2004 Jun 18; 339(5):1191-9. PubMed ID: 15178258
    [Abstract] [Full Text] [Related]

  • 9. Solution structure of the C-terminal nucleoprotein-RNA binding domain of the vesicular stomatitis virus phosphoprotein.
    Ribeiro EA, Favier A, Gerard FC, Leyrat C, Brutscher B, Blondel D, Ruigrok RW, Blackledge M, Jamin M.
    J Mol Biol; 2008 Oct 03; 382(2):525-38. PubMed ID: 18657547
    [Abstract] [Full Text] [Related]

  • 10. Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein.
    Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S.
    J Mol Recognit; 2010 Oct 03; 23(5):435-47. PubMed ID: 20058326
    [Abstract] [Full Text] [Related]

  • 11. Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints.
    Marsh JA, Forman-Kay JD.
    J Mol Biol; 2009 Aug 14; 391(2):359-74. PubMed ID: 19501099
    [Abstract] [Full Text] [Related]

  • 12. Structural selection of a native fold by peptide recognition. Insights into the thioredoxin folding mechanism.
    Santos J, Sica MP, Buslje CM, Garrote AM, Ermácora MR, Delfino JM.
    Biochemistry; 2009 Jan 27; 48(3):595-607. PubMed ID: 19119857
    [Abstract] [Full Text] [Related]

  • 13. Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy.
    Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S.
    J Biomol Struct Dyn; 2013 Jan 27; 31(5):453-71. PubMed ID: 22881220
    [Abstract] [Full Text] [Related]

  • 14. Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings.
    Meier S, Grzesiek S, Blackledge M.
    J Am Chem Soc; 2007 Aug 08; 129(31):9799-807. PubMed ID: 17636913
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  • 17. Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition.
    Jensen MR, Bernadó P, Houben K, Blanchard L, Marion D, Ruigrok RW, Blackledge M.
    Protein Pept Lett; 2010 Aug 08; 17(8):952-60. PubMed ID: 20450486
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  • 20. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.
    Jensen MR, Markwick PR, Meier S, Griesinger C, Zweckstetter M, Grzesiek S, Bernadó P, Blackledge M.
    Structure; 2009 Sep 09; 17(9):1169-85. PubMed ID: 19748338
    [Abstract] [Full Text] [Related]

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