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173 related items for PubMed ID: 18640986

  • 1. Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding.
    Engel R, Westphal AH, Huberts DHEW, Nabuurs SM, Lindhoud S, Visser AJWG, van Mierlo CPM.
    J Biol Chem; 2008 Oct 10; 283(41):27383-27394. PubMed ID: 18640986
    [Abstract] [Full Text] [Related]

  • 2. Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules.
    Nabuurs SM, Westphal AH, van Mierlo CP.
    J Am Chem Soc; 2008 Dec 17; 130(50):16914-20. PubMed ID: 19053416
    [Abstract] [Full Text] [Related]

  • 3. Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin.
    Bollen YJ, Sánchez IE, van Mierlo CP.
    Biochemistry; 2004 Aug 17; 43(32):10475-89. PubMed ID: 15301546
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  • 4. A general approach for detecting folding intermediates from steady-state and time-resolved fluorescence of single-tryptophan-containing proteins.
    Laptenok SP, Visser NV, Engel R, Westphal AH, van Hoek A, van Mierlo CP, van Stokkum IH, van Amerongen H, Visser AJ.
    Biochemistry; 2011 May 03; 50(17):3441-50. PubMed ID: 21425856
    [Abstract] [Full Text] [Related]

  • 5. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.
    van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E.
    Protein Sci; 1998 Nov 03; 7(11):2331-44. PubMed ID: 9827999
    [Abstract] [Full Text] [Related]

  • 6. Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement.
    Nabuurs SM, de Kort BJ, Westphal AH, van Mierlo CP.
    Eur Biophys J; 2010 Mar 03; 39(4):689-98. PubMed ID: 19894043
    [Abstract] [Full Text] [Related]

  • 7. Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.
    Lindhoud S, Westphal AH, Borst JW, van Mierlo CP.
    PLoS One; 2012 Mar 03; 7(9):e45746. PubMed ID: 23029219
    [Abstract] [Full Text] [Related]

  • 8. Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
    Nabuurs SM, Westphal AH, van Mierlo CP.
    J Am Chem Soc; 2009 Feb 25; 131(7):2739-46. PubMed ID: 19170491
    [Abstract] [Full Text] [Related]

  • 9. Last in, first out: the role of cofactor binding in flavodoxin folding.
    Bollen YJ, Nabuurs SM, van Berkel WJ, van Mierlo CP.
    J Biol Chem; 2005 Mar 04; 280(9):7836-44. PubMed ID: 15632150
    [Abstract] [Full Text] [Related]

  • 10. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.
    Steensma E, van Mierlo CP.
    J Mol Biol; 1998 Sep 25; 282(3):653-66. PubMed ID: 9737928
    [Abstract] [Full Text] [Related]

  • 11. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
    van Mierlo CP, Steensma E.
    J Biotechnol; 2000 May 26; 79(3):281-98. PubMed ID: 10867188
    [Abstract] [Full Text] [Related]

  • 12. Apoflavodoxin (un)folding followed at the residue level by NMR.
    van Mierlo CP, van den Oever JM, Steensma E.
    Protein Sci; 2000 Jan 26; 9(1):145-57. PubMed ID: 10739257
    [Abstract] [Full Text] [Related]

  • 13. Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.
    Visser NV, Westphal AH, van Hoek A, van Mierlo CP, Visser AJ, van Amerongen H.
    Biophys J; 2008 Sep 26; 95(5):2462-9. PubMed ID: 18708472
    [Abstract] [Full Text] [Related]

  • 14. Folding of proteins with a flavodoxin-like architecture.
    Houwman JA, van Mierlo CPM.
    FEBS J; 2017 Oct 26; 284(19):3145-3167. PubMed ID: 28380286
    [Abstract] [Full Text] [Related]

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  • 17. Stalled flavodoxin binds its cofactor while fully exposed outside the ribosome.
    Houwman JA, Westphal AH, van Berkel WJ, van Mierlo CP.
    Biochim Biophys Acta; 2015 Oct 26; 1854(10 Pt A):1317-24. PubMed ID: 26073784
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  • 19. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate.
    Irún MP, Garcia-Mira MM, Sanchez-Ruiz JM, Sancho J.
    J Mol Biol; 2001 Mar 02; 306(4):877-88. PubMed ID: 11243795
    [Abstract] [Full Text] [Related]

  • 20. Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering.
    Ayuso-Tejedor S, García-Fandiño R, Orozco M, Sancho J, Bernadó P.
    J Mol Biol; 2011 Mar 04; 406(4):604-19. PubMed ID: 21216251
    [Abstract] [Full Text] [Related]

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