Topic
Fatty acid-binding protein
About: Fatty acid-binding protein is a research topic. Over the lifetime, 1721 publications have been published within this topic receiving 81530 citations. The topic is also known as: FABP.
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TL;DR: The crystal structure of the recombinant form of rat liver fatty acid-binding protein was completed to 2.3 Å and refined to an R factor of 19.0%.
246 citations
TL;DR: A rapid and marked capacity for changes in dietary fatty acid availability to modulate the expression of mRNA-encoding proteins is necessary for fatty acid transport and oxidative metabolism and is evidence of nutrient-gene interactions in human skeletal muscle.
245 citations
TL;DR: It is concluded that fatty acids or fatty acid metabolites activate the aP2 gene and subsequently modulate its expression and the role of fatty acids in the regulation of adipose-related genes is investigated.
243 citations
01 Jan 2011
TL;DR: Fatty acid-binding proteins (FABP) as discussed by the authors are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intra-cell hydrophobic ligands and trafficking them throughout cellular compartments, including peroxisomes, mitochondria, endoplasmic reticulum and nucleus.
Abstract: Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus. FABPs are small, structurally conserved cytosolic proteins consisting of a water-filled, interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. At the superior surface, two alpha-helices cap the pocket and are thought to regulate binding. FABPs have broad specificity, including the ability to bind long-chain (C16‐C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators. FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human. The human genome consists of nine putatively functional protein-coding FABP genes. The most recently identified family member, FABP12, has been less studied.
239 citations
TL;DR: In this article, the ability of I- and L-FABP to bind fatty acids of different chain length and degree of saturation using a hydroxyalkoxypropyl dextran-based assay was analyzed.
237 citations