265 related articles for article (PubMed ID: 18024596)
1. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin.
Stagg L; Zhang SQ; Cheung MS; Wittung-Stafshede P
Proc Natl Acad Sci U S A; 2007 Nov; 104(48):18976-81. PubMed ID: 18024596
[TBL] [Abstract][Full Text] [Related]
2. Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin.
Homouz D; Stagg L; Wittung-Stafshede P; Cheung MS
Biophys J; 2009 Jan; 96(2):671-80. PubMed ID: 19167312
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states.
Muralidhara BK; Wittung-Stafshede P
Biochemistry; 2004 Oct; 43(40):12855-64. PubMed ID: 15461458
[TBL] [Abstract][Full Text] [Related]
5. Macromolecular crowding increases structural content of folded proteins.
Perham M; Stagg L; Wittung-Stafshede P
FEBS Lett; 2007 Oct; 581(26):5065-9. PubMed ID: 17919600
[TBL] [Abstract][Full Text] [Related]
6. Role of cations in stability of acidic protein Desulfovibrio desulfuricans apoflavodoxin.
Sedlák E; Stagg L; Wittung-Stafshede P
Arch Biochem Biophys; 2008 Jun; 474(1):128-35. PubMed ID: 18342618
[TBL] [Abstract][Full Text] [Related]
7. Macromolecular crowding tunes folding landscape of parallel α/β protein, apoflavodoxin.
Stagg L; Christiansen A; Wittung-Stafshede P
J Am Chem Soc; 2011 Feb; 133(4):646-8. PubMed ID: 21175168
[TBL] [Abstract][Full Text] [Related]
8. FMN binding and unfolding of Desulfovibrio desulfuricans flavodoxin: "hidden" intermediates at low denaturant concentrations.
Muralidhara BK; Wittung-Stafshede P
Biochim Biophys Acta; 2005 Mar; 1747(2):239-50. PubMed ID: 15698959
[TBL] [Abstract][Full Text] [Related]
9. 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; 283(41):27383-27394. PubMed ID: 18640986
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. 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]
12. 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]
13. Effect of Ficoll 70 on thermal stability and structure of creatine kinase.
Wang Y; He H; Li S
Biochemistry (Mosc); 2010 May; 75(5):648-54. PubMed ID: 20632946
[TBL] [Abstract][Full Text] [Related]
14. 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; 39(4):689-98. PubMed ID: 19894043
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. 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]
17. Conformational stability of apoflavodoxin.
Genzor CG; Beldarraín A; Gómez-Moreno C; López-Lacomba JL; Cortijo M; Sancho J
Protein Sci; 1996 Jul; 5(7):1376-88. PubMed ID: 8819170
[TBL] [Abstract][Full Text] [Related]
18. Cooperative stabilization of a molten globule apoflavodoxin fragment.
Maldonado S; Jiménez MA; Langdon GM; Sancho J
Biochemistry; 1998 Jul; 37(30):10589-96. PubMed ID: 9692948
[TBL] [Abstract][Full Text] [Related]
19. Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state.
Hong J; Gierasch LM
J Am Chem Soc; 2010 Aug; 132(30):10445-52. PubMed ID: 20662522
[TBL] [Abstract][Full Text] [Related]
20. No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin.
Apiyo D; Guidry J; Wittung-Stafshede P
Biochim Biophys Acta; 2000 Jun; 1479(1-2):214-24. PubMed ID: 10862971
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
