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• W2055678922 endingPage "1278" @default.
• W2055678922 startingPage "1268" @default.
• W2055678922 abstract "Lipids are essential for many biological processes and crucial in the pathogenesis of several diseases. Intracellular lipid-binding proteins (iLBPs) provide mobile hydrophobic binding sites that allow hydrophobic or amphipathic lipid molecules to penetrate into and across aqueous layers. Thus iLBPs mediate the lipid transport within the cell and participate to a spectrum of tissue-specific pathways involved in lipid homeostasis. Structural studies have shown that iLBPs' binding sites are inaccessible from the bulk, implying that substrate binding should involve a conformational change able to produce a ligand entry portal. Many studies have been reported in the last two decades on iLBPs indicating that their dynamics play a pivotal role in regulating ligand binding and targeted release. The ensemble of reported data has not been reviewed until today. This review is thus intended to summarize and possibly generalize the results up to now described, providing a picture which could help to identify the missing notions necessary to improve our understanding of the role of dynamics in iLBPs' molecular recognition. Such notions would clarify the chemistry of lipid binding to iLBPs and set the basis for the development of new drugs." @default.
• W2055678922 created "2016-06-24" @default.
• W2055678922 creator A5005338945 @default.
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• W2055678922 creator A5037860953 @default.
• W2055678922 creator A5051321796 @default.
• W2055678922 creator A5074346443 @default.
• W2055678922 date "2014-07-01" @default.
• W2055678922 modified "2023-09-25" @default.
• W2055678922 title "The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins" @default.
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• W2055678922 doi "https://doi.org/10.1016/j.bbapap.2014.04.011" @default.
• W2055678922 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24768771" @default.
• W2055678922 hasPublicationYear "2014" @default.
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