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The structure of vitellogenin provides a molecular model for the assembly and secretion of atherogenic lipoproteins.
Mann CJ, Anderson TA, Read J, Chester SA, Harrison GB, Köchl S, Ritchie PJ, Bradbury P, Hussain FS, Amey J, Vanloo B, Rosseneu M, Infante R, Hancock JM, Levitt DG, Banaszak LJ, Scott J, Shoulders CC. Mann CJ, et al. Among authors: vanloo b. J Mol Biol. 1999 Jan 8;285(1):391-408. doi: 10.1006/jmbi.1998.2298. J Mol Biol. 1999. PMID: 9878414
Helix-helix interactions in reconstituted high-density lipoproteins.
Lins L, Brasseur R, De Pauw M, Van Biervliet JP, Ruysschaert JM, Rosseneu M, Vanloo B. Lins L, et al. Among authors: vanloo b. Biochim Biophys Acta. 1995 Aug 24;1258(1):10-8. doi: 10.1016/0005-2760(95)00080-v. Biochim Biophys Acta. 1995. PMID: 7654775
Three arginine residues in apolipoprotein A-I are critical for activation of lecithin:cholesterol acyltransferase.
Roosbeek S, Vanloo B, Duverger N, Caster H, Breyne J, De Beun I, Patel H, Vandekerckhove J, Shoulders C, Rosseneu M, Peelman F. Roosbeek S, et al. Among authors: vanloo b. J Lipid Res. 2001 Jan;42(1):31-40. J Lipid Res. 2001. PMID: 11160363 Free article.
In this model, residues R149, R153, and R160 do not form salt bridges with the antiparallel apoA-I monomer, but instead are pointing toward the surface of the disc, enabling interactions with LCAT. - Roosbeek, S., B. Vanloo, N. Duverger, H. Caster, J. Breyne, I. De …
In this model, residues R149, R153, and R160 do not form salt bridges with the antiparallel apoA-I monomer, but instead are pointing toward …
56 results