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Vincent L. G. Postis

Researcher at University of Leeds

Publications -  36
Citations -  1380

Vincent L. G. Postis is an academic researcher from University of Leeds. The author has contributed to research in topics: Membrane protein & Membrane. The author has an hindex of 14, co-authored 36 publications receiving 1127 citations. Previous affiliations of Vincent L. G. Postis include Joseph Fourier University & University of Bordeaux.

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Journal ArticleDOI

A method for detergent-free isolation of membrane proteins in their local lipid environment

TL;DR: This protocol describes the preparation of styrene maleic acid (SMA) co-polymer to extract membrane proteins from prokaryotic and eukaryotic expression systems and provides a practical tool kit for those wanting to use SMALPs to study membrane proteins.
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Crystal structure of a prokaryotic homologue of the mammalian oligopeptide–proton symporters, PepT1 and PepT2

TL;DR: The crystal structure of PepTSo is presented, a functionally similar prokaryotic homologue of the mammalian peptide transporters from Shewanella oneidensis, which reveals a ligand‐bound occluded state for the MFS and provides new insights into a general transport mechanism.
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The use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy

TL;DR: It is shown how a SMALP scaffold can be used to visualise membrane proteins, embedded in a near-native lipid environment, by negative stain electron microscopy, yielding structures at a modest resolution in a short (days) timeframe.
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Intrinsic acyl-CoA thioesterase activity of a peroxisomal ATP binding cassette transporter is required for transport and metabolism of fatty acids.

TL;DR: CTS, and most likely the other ABCD family members, represent rare examples of polytopic membrane proteins with an intrinsic additional enzymatic function that may regulate the entry of substrates into the β-oxidation pathway.
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Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure

TL;DR: The structure of the Escherichia coli multidrug efflux transporter AcrB in a SMALP scaffold to sub-nm resolution is reported, with the resulting map being consistent with high resolution crystal structures and other EM derived maps.