185 related articles for article (PubMed ID: 27784783)
1. The Ribosome Restrains Molten Globule Formation in Stalled Nascent Flavodoxin.
Houwman JA; André E; Westphal AH; van Berkel WJ; van Mierlo CP
J Biol Chem; 2016 Dec; 291(50):25911-25920. PubMed ID: 27784783
[TBL] [Abstract][Full Text] [Related]
2. 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; 1854(10 Pt A):1317-24. PubMed ID: 26073784
[TBL] [Abstract][Full Text] [Related]
3. Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of alpha-beta parallel protein flavodoxin.
Nabuurs SM; van Mierlo CPM
J Biol Chem; 2010 Feb; 285(6):4165-4172. PubMed ID: 19959481
[TBL] [Abstract][Full Text] [Related]
4. Folding of proteins with a flavodoxin-like architecture.
Houwman JA; van Mierlo CPM
FEBS J; 2017 Oct; 284(19):3145-3167. PubMed ID: 28380286
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. 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; 7(9):e45746. PubMed ID: 23029219
[TBL] [Abstract][Full Text] [Related]
7. 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; 131(7):2739-46. PubMed ID: 19170491
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Topological switching between an alpha-beta parallel protein and a remarkably helical molten globule.
Nabuurs SM; Westphal AH; aan den Toorn M; Lindhoud S; van Mierlo CP
J Am Chem Soc; 2009 Jun; 131(23):8290-5. PubMed ID: 19456154
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. 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]
12. 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]
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. A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential.
Alagaratnam S; van Pouderoyen G; Pijning T; Dijkstra BW; Cavazzini D; Rossi GL; Van Dongen WM; van Mierlo CP; van Berkel WJ; Canters GW
Protein Sci; 2005 Sep; 14(9):2284-95. PubMed ID: 16131657
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Apoflavodoxin: structure, stability, and FMN binding.
Maldonado S; Lostao A; Irún MP; Férnandez-Recio J; Gustavo Genzor C; Begoña González E; Rubio JA; Luquita A; Daoudi F; Sancho J
Biochimie; 1998 Oct; 80(10):813-20. PubMed ID: 9893940
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin.
Apiyo D; Wittung-Stafshede P
Protein Sci; 2002 May; 11(5):1129-35. PubMed ID: 11967369
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting.
Muralidhara BK; Rathinakumar R; Wittung-Stafshede P
Arch Biochem Biophys; 2006 Jul; 451(1):51-8. PubMed ID: 16730634
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]