B
Betina Córsico
Researcher at National University of La Plata
Publications - 46
Citations - 1217
Betina Córsico is an academic researcher from National University of La Plata. The author has contributed to research in topics: Fatty acid-binding protein & Fatty acid. The author has an hindex of 17, co-authored 43 publications receiving 993 citations. Previous affiliations of Betina Córsico include National Scientific and Technical Research Council & Facultad de Ciencias Médicas.
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Journal ArticleDOI
The emerging functions and mechanisms of mammalian fatty acid-binding proteins
Judith Storch,Betina Córsico +1 more
TL;DR: Several members of the FABP family have been shown to function directly in the regulation of cognate nuclear transcription factor activity via ligand-dependent translocation to the nucleus.
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The α-Helical Domain of Liver Fatty Acid Binding Protein Is Responsible for the Diffusion-Mediated Transfer of Fatty Acids to Phospholipid Membranes†
TL;DR: The results showed a significant modification of the absolute rate of FA transfer from the chimeric proteins compared to that of the wild type, indicating that the slower rate ofFA transfer observed for wild-type LFABP relative to this of wild- type IFABP is, in part, determined by the helical domain of the proteins.
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Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles.
TL;DR: Results indicate that the central domain formed by two type Y helices swings away from lipid contact in the discoidal lipoproteins and is able to insert into membrane bilayers, a process that may be of great importance for the mechanism of cholesterol exchange between high density lipoprotein A-I and cell membranes.
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Protein-Membrane Interaction and Fatty Acid Transfer from Intestinal Fatty Acid-binding Protein to Membranes SUPPORT FOR A MULTISTEP PROCESS
TL;DR: The hypothesis that the portal region undergoes a conformational change during protein-membrane interaction, which leads to release of the bound fatty acid to the membrane, is supported and that the α2 segment is of particular importance in the establishment of charge-charge interactions between IFABP and membranes.
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Conformation of apolipoprotein ai in reconstituted lipoprotein particles and particle-membrane interaction : effect of cholesterol
TL;DR: Results suggest that in small cholesterol-poor particles, apoAI could have a conformation determining a high affinity for membranes, which could facilitate cholesterol efflux, and after cholesterol enrichment, a conformational change in apo AI could decrease the affinity for membrane allowing the lipoprotein release.