These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
167 related articles for article (PubMed ID: 15317817)
1. The long and short flavodoxins: II. The role of the differentiating loop in apoflavodoxin stability and folding mechanism. López-Llano J; Maldonado S; Jain S; Lostao A; Godoy-Ruiz R; Sanchez-Ruiz JM; Cortijo M; Fernández-Recio J; Sancho J J Biol Chem; 2004 Nov; 279(45):47184-91. PubMed ID: 15317817 [TBL] [Abstract][Full Text] [Related]
2. The long and short flavodoxins: I. The role of the differentiating loop in apoflavodoxin structure and FMN binding. López-Llano J; Maldonado S; Bueno M; Lostao A; Angeles-Jiménez M; Lillo MP; Sancho J J Biol Chem; 2004 Nov; 279(45):47177-83. PubMed ID: 15317816 [TBL] [Abstract][Full Text] [Related]
3. 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]
8. 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]
9. Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI. Lawson RJ; von Wachenfeldt C; Haq I; Perkins J; Munro AW Biochemistry; 2004 Oct; 43(39):12390-409. PubMed ID: 15449930 [TBL] [Abstract][Full Text] [Related]
10. Apoflavodoxin folding mechanism: an alpha/beta protein with an essentially off-pathway intermediate. Fernández-Recio J; Genzor CG; Sancho J Biochemistry; 2001 Dec; 40(50):15234-45. PubMed ID: 11735406 [TBL] [Abstract][Full Text] [Related]
11. 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]
12. 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; 79(3):281-98. PubMed ID: 10867188 [TBL] [Abstract][Full Text] [Related]
13. 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; 280(9):7836-44. PubMed ID: 15632150 [TBL] [Abstract][Full Text] [Related]
14. 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]
15. Stabilization of apoflavodoxin by replacing hydrogen-bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln. Irún MP; Maldonado S; Sancho J Protein Eng; 2001 Mar; 14(3):173-81. PubMed ID: 11342714 [TBL] [Abstract][Full Text] [Related]
16. Conformational stability of Helicobacter pylori flavodoxin: fit to function at pH 5. Cremades N; Bueno M; Neira JL; Velázquez-Campoy A; Sancho J J Biol Chem; 2008 Feb; 283(5):2883-95. PubMed ID: 17998211 [TBL] [Abstract][Full Text] [Related]
17. A comparison of the urea-induced unfolding of apoflavodoxin and flavodoxin from Desulfovibrio vulgaris. Nuallain BO; Mayhew SG Eur J Biochem; 2002 Jan; 269(1):212-23. PubMed ID: 11784315 [TBL] [Abstract][Full Text] [Related]
18. 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]
19. Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength. Houwman JA; Westphal AH; Visser AJWG; Borst JW; van Mierlo CPM Phys Chem Chem Phys; 2018 Mar; 20(10):7059-7072. PubMed ID: 29473921 [TBL] [Abstract][Full Text] [Related]
20. Direct examination of the relevance for folding, binding and electron transfer of a conserved protein folding intermediate. Lamazares E; Vega S; Ferreira P; Medina M; Galano-Frutos JJ; Martínez-Júlvez M; Velázquez-Campoy A; Sancho J Phys Chem Chem Phys; 2017 Jul; 19(29):19021-19031. PubMed ID: 28702545 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]