ArticleBiophysical journal2021
Conformational exchange of fatty acid binding protein induced by protein-nanodisc interactions.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Investigating protein-membrane interactions using native reverse micelles constructed from naturally sourced lipids.Protein science : a publication of the Protein Society · 2023Article
- Understanding FABP7 binding to fatty acid micelles and membranes.Biophysical journal · 2023Article
- Effects of ligand binding on dynamics of fatty acid binding protein and interactions with membranes.Biophysical journal · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Fatty acid binding proteins (FABPs) can facilitate the transfer of long-chain fatty acids between intracellular membranes across considerable distances. The transfer process involves fatty acids, their donor membrane and acceptor membrane, and FABPs, implying that potential protein-membrane interactions exist. Despite intensive studies on FABP-membrane interactions, the interaction mode remains elusive, and the protein-membrane association and dissociation rates are inconsistent. In this study, we used nanodiscs (NDs) as mimetic membranes to investigate FABP-membrane interactions. Our NMR experiments showed that human intestinal FABP interacts weakly with both negatively charged and neutral membranes, but it prefers the negatively charged one. Through simultaneous analysis of NMR relaxation in the rotating-frame (R
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