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417 related items for 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 17; 43(32):10475-89. PubMed ID: 15301546 [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 17; 130(50):16914-20. PubMed ID: 19053416 [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 25; 131(7):2739-46. PubMed ID: 19170491 [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 03; 50(17):3441-50. PubMed ID: 21425856 [Abstract] [Full Text] [Related]
17. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Walkenhorst WF, Green SM, Roder H. Biochemistry; 1997 May 13; 36(19):5795-805. PubMed ID: 9153420 [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 13; 39(4):689-98. PubMed ID: 19894043 [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 22; 114(2-3):181-9. PubMed ID: 15829351 [Abstract] [Full Text] [Related]