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Akademický článek

Swapping the N- and C-terminal domains of human apolipoprotein E3 and AI reveals insights into their structure/activity relationship.

Autor: Mark T Lek, Siobanth Cruz, Nnejiuwa U Ibe, Wendy H J Beck, John K Bielicki, Paul M M Weers, Vasanthy Narayanaswami

Publikováno v: PLoS ONE, Vol 12, Iss 6, p e0178346 (2017)

Apolipoprotein (apo) E3 and apoAI are exchangeable apolipoproteins that play a dominant role in regulating plasma lipoprotein metabolism. ApoE3 (299 residues) is composed of an N-terminal (NT) domain bearing a 4-helix bundle and a C-terminal (CT) dom

Externí odkaz: https://doaj.org/article/13ed6acafcff45beb0d1ed062e7adf06

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Modulation of the lipid binding properties of the N-terminal domain of human apolipoprotein E3

Autor: P M, Weers, V, Narayanaswami, R O, Ryan

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::59370e36dadb5217b2832eb0c2478df6
https://pubmed.ncbi.nlm.nih.gov/11432739

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Complete 1H, 15N, and 13C assignments of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III

Autor: D, Fan, L, Reese, X, Ren, P M, Weers, R O, Ryan, J, Wang

Publikováno v: Journal of biomolecular NMR. 19(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::980a4771dcd716bd79f0e19c29dbbf70
https://pubmed.ncbi.nlm.nih.gov/11246860

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Spectroscopic characterization of the conformational adaptability of Bombyx mori apolipophorin III

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::28bce2376cc2088d0dc249f91d3324f6
https://pubmed.ncbi.nlm.nih.gov/10651809

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Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34, and 95 in Locusta migratoria apolipophorin III

Autor: P M, Weers, V, Narayanaswami, C M, Kay, R O, Ryan

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2c8b8753e39505396dec5349902135f4
https://pubmed.ncbi.nlm.nih.gov/10419496

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Biosynthesis of locust lipophorin. Apolipophorins I and II originate from a common precursor

Autor: P M, Weers, W J, Van Marrewijk, A M, Beenakkers, D J, Van der Horst

Publikováno v: The Journal of biological chemistry. 268(6)

Biosynthesis of apolipophorins of high density lipophorin of the locust Locusta migratoria was studied in vitro. Analysis of immunoprecipitates from homogenates of in vitro labeled fat body revealed a common precursor for apolipophorin I (apoLp-I, M(

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b57a667fa2f65f9f50a1d0a88c5a8129
https://pubmed.ncbi.nlm.nih.gov/8440714

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