A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state-Reference-Cited by-同舟云学术

A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state

Published:2017-11-13 Issue:12 Volume:24 Page:1093-1099
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Melchior John T^ORCID,Walker Ryan G,Cooke Allison L,Morris Jamie,Castleberry Mark,Thompson Thomas B,Jones Martin K,Song Hyun D,Rye Kerry-Anne,Oda Michael N,Sorci-Thomas Mary G,Thomas Michael J,Heinecke Jay W,Mei Xiaohu,Atkinson David^ORCID,Segrest Jere P,Lund-Katz Sissel,Phillips Michael C^ORCID,Davidson W Sean^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3501.pdf

Reference63 articles.

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3. Borhani, D.W., Engler, J.A. & Brouillette, C.G. Crystallization of truncated human apolipoprotein A-I in a novel conformation. Acta Crystallogr. D Biol. Crystallogr. 55, 1578–1583 (1999).

4. Mei, X. & Atkinson, D. Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization. J. Biol. Chem. 286, 38570–38582 (2011).

5. Melchior, J.T. et al. An evaluation of the crystal structure of C-terminal truncated apolipoprotein A-I in solution reveals structural dynamics related to lipid binding. J. Biol. Chem. 291, 5439–5451 (2016).

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