Zobrazeno 1 - 10
of 37
pro vyhledávání: '"R O Ryan"'
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 5, Pp 1066-1072 (1995)
To facilitate structure-function studies of Manduca sexta apolipophorin III (apoLp-III), its nucleotide coding sequence was cloned from a fat body cDNA library by in vitro DNA amplification. The amplification product was cloned in the pET expression
Externí odkaz:
https://doaj.org/article/74e5a560855f46d996d2eca35486c862
Autor:
B J Blacklock, R O Ryan
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 1, Pp 108-116 (1995)
Studies have been conducted to characterize structural and functional properties of Manduca sexta lipid transfer particle (LTP). LTP is a high molecular weight complex of three apolipoproteins and lipid that facilitates the transfer of lipids between
Externí odkaz:
https://doaj.org/article/391506fef5c9407e9ff3d67bf54d2491
Publikováno v:
Journal of Lipid Research, Vol 26, Iss 2, Pp 241-247 (1985)
Most insects have a major lipoprotein species in the blood (hemolymph) that serves to transport fat from the midgut to the storage depots in fat body cells and from the fat body to peripheral tissues. The generic name lipophorin is used for this lipo
Externí odkaz:
https://doaj.org/article/5990b1617f0f4499873b2bacf561ef6d
Publikováno v:
Biochemistry and Cell Biology. 75:45-53
Publikováno v:
European journal of biochemistry. 268(13)
Apolipoprotein E (apoE) plays a critical role in plasma lipid homeostasis through its function as a ligand for the low-density lipoprotein (LDL) receptor family. Receptor recognition is mediated by residues 130-150 in the independently folded, 22-kDa
Publikováno v:
Journal of biomolecular NMR. 19(1)
Autor:
V, Narayanaswami, Y, Yamauchi, P M, Weers, H, Maekawa, R, Sato, K, Tsuchida, K, Oikawa, C M, Kay, R O, Ryan
Publikováno v:
European journal of biochemistry. 267(3)
Apolipophorin III (apoLp-III) from the silkmoth, Bombyx mori, has been over-expressed in Escherichia coli, purified and characterized. Far-UV CD spectroscopic analysis revealed 65% alpha-helix secondary structure. Near-UV CD spectra obtained in buffe
Publikováno v:
The Journal of biological chemistry. 274(31)
Apolipophorin III (apoLp-III) from Locusta migratoria is an exchangeable apolipoprotein that binds reversibly to lipid surfaces. In the lipid-free state this 164-residue protein exists as a bundle of five elongated amphipathic alpha-helices. Upon lip
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 76(2-3)
A characteristic property of amphipathic exchangeable apolipoproteins is an ability to exist alternately in lipid-free and lipid-bound states. In the present study, we have used 1H-15N-heteronuclear single quantum correlation spectroscopy to probe st
Autor:
C A, Fisher, R O, Ryan
Publikováno v:
Journal of lipid research. 40(1)
The N-terminal domain of human apolipoprotein E3 (apoE3) adopts an elongated, globular four helix bundle conformation in the lipid-free state. Upon lipid binding, the protein is thought to undergo a significant conformational change that is essential