scholarly journals The Lipid Bilayer Modulates the Structure and Function of an ATP-binding Cassette Exporter

2016 ◽  
Vol 291 (9) ◽  
pp. 4453-4461 ◽  
Author(s):  
Maria E. Zoghbi ◽  
Rebecca S. Cooper ◽  
Guillermo A. Altenberg
2014 ◽  
Vol 461 (2) ◽  
pp. 269-278 ◽  
Author(s):  
Sonali Gulati ◽  
Mohammed Jamshad ◽  
Timothy J. Knowles ◽  
Kerrie A. Morrison ◽  
Rebecca Downing ◽  
...  

A styrene maleic acid copolymer can be effectively used to extract and purify large eukaryotic transmembrane proteins in the absence of detergents, forming small bilayer discs encapsulating the protein, which have great potential for future structure and function studies.


2008 ◽  
Vol 103 (8) ◽  
pp. 825-835 ◽  
Author(s):  
Otmar Pfister ◽  
Angelos Oikonomopoulos ◽  
Konstantina-Ioanna Sereti ◽  
Regina L. Sohn ◽  
Darragh Cullen ◽  
...  

2002 ◽  
Vol 1 (4) ◽  
pp. 643-652 ◽  
Author(s):  
Christophe Anjard ◽  
William F. Loomis

ABSTRACT The ABC superfamily of genes is one of the largest in the genomes of both bacteria and eukaryotes. The proteins encoded by these genes all carry a characteristic 200- to 250-amino-acid ATP-binding cassette that gives them their family name. In bacteria they are mostly involved in nutrient import, while in eukaryotes many are involved in export. Seven different families have been defined in eukaryotes based on sequence homology, domain topology, and function. While only 6 ABC genes in Dictyostelium discoideum have been studied in detail previously, sequences from the well-advanced Dictyostelium genome project have allowed us to recognize 68 members of this superfamily. They have been classified and compared to animal, plant, and fungal orthologs in order to gain some insight into the evolution of this superfamily. It appears that many of the genes inferred to have been present in the ancestor of the crown organisms duplicated extensively in some but not all phyla, while others were lost in one lineage or the other.


2018 ◽  
Vol 1860 (4) ◽  
pp. 809-817 ◽  
Author(s):  
Naomi L. Pollock ◽  
Sarah C. Lee ◽  
Jaimin H. Patel ◽  
Aiman A. Gulamhussein ◽  
Alice J. Rothnie

Author(s):  
A. T. Nies ◽  
M. Rius ◽  
J. König ◽  
C. Herold-Mende ◽  
D. Keppler

2016 ◽  
Vol 397 (12) ◽  
pp. 1335-1354 ◽  
Author(s):  
Aldino Viegas ◽  
Thibault Viennet ◽  
Manuel Etzkorn

Abstract The choice of a suitable membrane mimicking environment is of fundamental importance for the characterization of structure and function of membrane proteins. In this respect, usage of the lipid bilayer nanodisc technology provides a unique potential for nuclear magnetic resonance (NMR)-based studies. This review summarizes the recent advances in this field, focusing on (i) the strengths of the system, (ii) the bottlenecks that may be faced, and (iii) promising capabilities that may be explored in future studies.


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