421 related articles for article (PubMed ID: 15301546)
1. 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]
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; 130(50):16914-20. PubMed ID: 19053416
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. 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]
5. 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]
6. 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]
7. Folding of horse cytochrome c in the reduced state.
Bhuyan AK; Udgaonkar JB
J Mol Biol; 2001 Oct; 312(5):1135-60. PubMed ID: 11580255
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
Patra AK; Udgaonkar JB
Biochemistry; 2007 Oct; 46(42):11727-43. PubMed ID: 17902706
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.
Mizuguchi M; Arai M; Ke Y; Nitta K; Kuwajima K
J Mol Biol; 1998; 283(1):265-77. PubMed ID: 9761689
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate.
Capaldi AP; Ferguson SJ; Radford SE
J Mol Biol; 1999 Mar; 286(5):1621-32. PubMed ID: 10064719
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Gradual Folding of an Off-Pathway Molten Globule Detected at the Single-Molecule Level.
Lindhoud S; Pirchi M; Westphal AH; Haran G; van Mierlo CP
J Mol Biol; 2015 Sep; 427(19):3148-57. PubMed ID: 26163276
[TBL] [Abstract][Full Text] [Related]
17. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease.
Walkenhorst WF; Green SM; Roder H
Biochemistry; 1997 May; 36(19):5795-805. PubMed ID: 9153420
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold.
Bollen YJ; van Mierlo CP
Biophys Chem; 2005 Apr; 114(2-3):181-9. PubMed ID: 15829351
[TBL] [Abstract][Full Text] [Related]
20. The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates.
Bollen YJ; Kamphuis MB; van Mierlo CP
Proc Natl Acad Sci U S A; 2006 Mar; 103(11):4095-100. PubMed ID: 16537490
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
