Kinetics of Fatty Acid Interactions with Fatty Acid Binding Proteins from Adipocyte, Heart, and Intestine (∗)
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TLDR
It is suggested that entering or leaving the FABP binding cavity involves similar mechanisms for all 3 FABPs and may involve amino acid residues located within the portal regions of these proteins.About:
This article is published in Journal of Biological Chemistry.The article was published on 1996-05-10 and is currently open access. It has received 70 citations till now. The article focuses on the topics: Fatty acid & Fatty acid-binding protein.read more
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Journal ArticleDOI
Intracellular lipid-binding proteins and their genes
TL;DR: Intracellular lipid-binding proteins are a family of low-molecular-weight single-chain polypeptides that form 1:1 complexes with fatty acids, retinoids, or other hydrophobic ligands that are products of a large multigene family of unlinked loci distributed throughout the genome.
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Insights into binding of fatty acids by fatty acid binding proteins.
TL;DR: Members of the phylogenetically related intracellular lipid binding protein (iLBP) are characterized by a highly conserved tertiary structure, but reveal distinct binding preferences with regard to ligand structure and conformation when binding is assessed by the Lipidex method or isothermal titration calorimetry, a true equilibrium method.
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The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice
TL;DR: It is proposed that I‐FABP functions as a lipid‐sensing component of energy homeostasis that alters body weight gain in agender‐specific fashion and is not essential for dietary fat absorption in mice.
Journal ArticleDOI
Kinetics and molecular properties of pheromone binding and release
Walter S. Leal,Angela M. Chen,Yuko Ishida,Vicky P. Chiang,Melissa L. Erickson,Tania I. Morgan,Jennifer M. Tsuruda +6 more
TL;DR: Molecular interactions of bombykol with both native and mutated PBPs were analyzed by a novel binding assay, and fluorescence studies shed light on the contributions of Trp-37 and Trt-127 emissions to the overall fluorescence.
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New insights into the fatty acid-binding protein (FABP) family in the small intestine
TL;DR: Although, they exhibit differences in their binding specificities and location along the small intestine supporting a specialization, it is likely that L-FABP and I-BABP genes exert the same type of basic function(s) in the enterocyte, in contrast to I-F ABP.
References
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Journal ArticleDOI
A new generation of Ca2+ indicators with greatly improved fluorescence properties.
TL;DR: A new family of highly fluorescent indicators has been synthesized for biochemical studies of the physiological role of cytosolic free Ca2+ using an 8-coordinate tetracarboxylate chelating site with stilbene chromophores that offer up to 30-fold brighter fluorescence.
Journal ArticleDOI
Data Reduction and Error Analysis for the Physical Sciences.
TL;DR: Numerical methods matrices graphs and tables histograms and graphs computer routines in Pascal and Monte Carlo techniques dependent and independent variables least-squares fit to a polynomial least-square fit to an arbitrary function fitting composite peaks direct application of the maximum likelihood.
Journal ArticleDOI
A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues.
TL;DR: A protein of molecular weight ∼ 12,000 which binds long-chain fatty acids and certain other lipids has been identified in cytosol of intestinal mucosa, liver, myocardium, adipose tissue, and kidney and appears to be identical with the smaller of two previously described cytoplasmic anion-binding proteins.
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Polarization of the fluorescence of macromolecules. 1. Theory and experimental method
Book ChapterDOI
Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins
Leonard J. Banaszak,Nathan S. Winter,Zhaohui Xu,David A. Bernlohr,S. W. Cowan,Alwyn T. Jones +5 more
TL;DR: This chapter focuses on the structural analyses and comparisons between members of a multigene family of hydrophobic ligand-binding proteins and provides a detailed comparison of intra- and extracellular lipid binding proteins with known crystal structures.