BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

162 related articles for article (PubMed ID: 16647718)

  • 1. Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin.
    Bueno M; Ayuso-Tejedor S; Sancho J
    J Mol Biol; 2006 Jun; 359(3):813-24. PubMed ID: 16647718
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate.
    Campos LA; Bueno M; Lopez-Llano J; Jiménez MA; Sancho J
    J Mol Biol; 2004 Nov; 344(1):239-55. PubMed ID: 15504414
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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; 306(4):877-88. PubMed ID: 11243795
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Residue-specific analysis of frustration in the folding landscape of repeat beta/alpha protein apoflavodoxin.
    Stagg L; Samiotakis A; Homouz D; Cheung MS; Wittung-Stafshede P
    J Mol Biol; 2010 Feb; 396(1):75-89. PubMed ID: 19913555
    [TBL] [Abstract][Full Text] [Related]  

  • 5. A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin.
    Larriva M; Prieto L; Bruscolini P; Rey A
    Proteins; 2010 Jan; 78(1):73-82. PubMed ID: 19688823
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Equilibrium phi-analysis of a molten globule: the 1-149 apoflavodoxin fragment.
    López-Llano J; Campos LA; Bueno M; Sancho J
    J Mol Biol; 2006 Feb; 356(2):354-66. PubMed ID: 16364364
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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; 406(4):604-19. PubMed ID: 21216251
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins.
    Ayuso-Tejedor S; Angarica VE; Bueno M; Campos LA; Abián O; Bernadó P; Sancho J; Jiménez MA
    J Mol Biol; 2010 Jul; 400(4):922-34. PubMed ID: 20553732
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 130(50):16914-20. PubMed ID: 19053416
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation.
    Campos LA; Garcia-Mira MM; Godoy-Ruiz R; Sanchez-Ruiz JM; Sancho J
    J Mol Biol; 2004 Nov; 344(1):223-37. PubMed ID: 15504413
    [TBL] [Abstract][Full Text] [Related]  

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

  • 12. Underexposed polar residues and protein stabilization.
    Ayuso-Tejedor S; Abián O; Sancho J
    Protein Eng Des Sel; 2011 Jan; 24(1-2):171-7. PubMed ID: 20937603
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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; 7(11):2331-44. PubMed ID: 9827999
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Energetics of aliphatic deletions in protein cores.
    Bueno M; Campos LA; Estrada J; Sancho J
    Protein Sci; 2006 Aug; 15(8):1858-72. PubMed ID: 16877708
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Filling small, empty protein cavities: structural and energetic consequences.
    Bueno M; Cremades N; Neira JL; Sancho J
    J Mol Biol; 2006 May; 358(3):701-12. PubMed ID: 16563433
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Structural examination of phi-value analysis in protein folding.
    Feng H; Vu ND; Zhou Z; Bai Y
    Biochemistry; 2004 Nov; 43(45):14325-31. PubMed ID: 15533036
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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; 282(3):653-66. PubMed ID: 9737928
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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; 50(17):3441-50. PubMed ID: 21425856
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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; 43(32):10475-89. PubMed ID: 15301546
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Native-specific stabilization of flavodoxin by the FMN cofactor: structural and thermodynamical explanation.
    Campos LA; Sancho J
    Proteins; 2006 May; 63(3):581-94. PubMed ID: 16444751
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.