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Cited by 296

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Structural and functional analysis of fatty acid-binding proteins

Open access
Storch, Judith, McDermott, Lindsay·2009·Journal of Lipid Research

Abstract

The mammalian FA-binding proteins (FABPs) bind long-chain FA with high affinity. The large number of FABP types is suggestive of distinct functions in specific tissues. Multiple experimental approaches have shown that individual FABPs possess both unique and overlapping functions, some of which are based on specific elements in the protein structure. Although FA binding affinities for all FABPs tend to correlate directly with FA hydrophobicity, structure-function studies indicate that subtle three-dimensional changes that occur upon ligand binding may promote specific protein-protein or protein-membrane interactions that ultimately determine the function of each FABP. The conformational changes are focused in the FABP helical/portal domain, a region that was identified by in vitro studies to be vital for the FA transport properties of the FABPs. Thus, the FABPs modulate intracellular lipid homeostasis by regulating FA transport in the nuclear and extra-nuclear compartments of the cell; in so doing, they also impact systemic energy homeostasis.

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Metadata

Authors
Storch, J., & McDermott, L.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
2009-04
Volume
50
Pages
S126-S131
ISSN
0022-2275 (ISSN-L)
OpenAlex
W2034937725
Cited by
296
References
3
FWCI
3.97
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structural and functional analysis of fatty acid-binding proteins. https://app.cochat.ai/papers/10.1194/jlr.r800084-jlr200
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Storch, J., & McDermott, L. (2009). Structural and functional analysis of fatty acid-binding proteins. Journal of Lipid Research. https://doi.org/10.1194/jlr.r800084-jlr200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.