Application of target repositioning and in silico screening to exploit fatty acid binding proteins (FABPs) from Echinococcus multilocularis as possible drug targets

JA Bélgamo, LN Alberca, JL Pórfido… - Journal of Computer …, 2020 - Springer
Fatty acid binding proteins (FABPs) are small intracellular proteins that reversibly bind fatty
acids and other hydrophobic ligands. In cestodes, due to their inability to synthesise fatty …

High-amylose resistant starch increases hormones and improves structure and function of the gastrointestinal tract: a microarray study

MJ Keenan, RJ Martin, AM Raggio, KL McCutcheon… - Lifestyle …, 2012 - karger.com
Abstract Background/Aims: Type 2 resistant starch from high-amylose maize (HAM-RS2) is
associated with increased fermentation, increased expression of proglucagon (gene for GLP …

Truncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation

LM Curto, CR Angelani, JJ Caramelo, JM Delfino - Biophysical journal, 2012 - cell.com
Δ98Δ is a functional all-β sheet variant of intestinal fatty acid binding protein (IFABP) that
was generated by controlled proteolysis. This framework is useful to study the molecular …

[HTML][HTML] A microarray study indicates high-amylose resistant starch increases hormones and improves structure and function of the GI tract

MJ Keenan, RJ Martin, AM Raggio… - … of nutrigenetics and …, 2012 - ncbi.nlm.nih.gov
Methods Adult, male SD rats were fed one of the following three diets for a four week study
period: cornstarch control (CC, 3.74 kcal/g), dietary energy density control (EC, 3.27 kcal/g) …

Toward a common aggregation mechanism for a β-barrel protein family: Insights derived from a stable dimeric species

CR Angelani, LM Curto, IS Cabanas… - … et Biophysica Acta (BBA …, 2014 - Elsevier
Δ78Δ is a second generation functional all-β sheet variant of IFABP (intestinal fatty acid
binding protein) corresponding to the fragment 29–106 of the parent protein. This protein …

Structural coalescence underlies the aggregation propensity of a β-barrel protein motif

CR Angelani, JJ Caramelo, LM Curto, JM Delfino - Plos one, 2017 - journals.plos.org
A clear understanding of the structural foundations underlying protein aggregation is an
elusive goal of central biomedical importance. A step toward this aim is exemplified by the β …

Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity

LM Curto, CR Angelani, JM Delfino - Prostaglandins, Leukotrienes and …, 2015 - Elsevier
Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or
peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here …

Identificación y caracterización de proteínas específicas del nematode parásito Dioctophyme renale

AN Giorello - 2023 - sedici.unlp.edu.ar
La Dioctofimosis es una enfermedad parasitaria causada por el nematode gigante
Dioctophyme renale cuya prevalencia está incrementando en América del Sur debido a …

[HTML][HTML] Análisis estructural y funcional de proteínas solubles que unen lípidos de intestino e hígado

LJ Falomir-Lockhart, B Córsico… - Acta bioquímica …, 2013 - SciELO Argentina
Luego de la ingesta, el epitelio del intestino delgado está encargado de asimilar grandes
cantidades de nutrientes, como aminoácidos, glúcidos y ácidos grasos. Las proteínas …

[PDF][PDF] Local Unfolding of Helical Portal Region of Human Intestinal Fatty Acid Binding Protein Allows Ligand Entry for Binding

X TIANSHU - 2016 - core.ac.uk
I would like to extend my gratitude to my supervisor, Professor Dr. Yang Daiwen, for his
continuing guidance in five years. He helped me to solve many tough problems in this …