Search Results - "Vazquez, Diego S"

Molecular and Structural Parallels between Gluten Pathogenic Peptides and Bacterial-Derived Proteins by Bioinformatics Analysis by Vazquez, Diego S, Schilbert, Hanna M, Dodero, Veronica I

“…Gluten-related disorders (GRDs) are a group of diseases that involve the activation of the immune system triggered by the ingestion of gluten, with a worldwide…”
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Protein conformation and biomolecular condensates by Vazquez, Diego S., Toledo, Pamela L., Gianotti, Alejo R., Ermácora, Mario R.

“…Protein conformation and cell compartmentalization are fundamental concepts and subjects of vast scientific endeavors. In the last two decades, we have…”
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Thioredoxin from Escherichia coli as a Role Model of Molecular Recognition, Folding, Dynamics and Function by Vazquez, Diego S, Delfino, Jose Maria, Santos, Javier

“…Thioredoxin (TRX) catalyzes redox reactions via the reversible oxidation of the conserved active center CGPC and it is involved in multiple biological…”
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From celiac disease to coccidia infection and vice‐versa: The polyQ peptide CXCR3‐interaction axis by Lauxmann, Martin A., Vazquez, Diego S., Schilbert, Hanna M., Neubauer, Pia R., Lammers, Karen M., Dodero, Veronica I.

“…Zonulin is a physiological modulator of intercellular tight junctions, which upregulation is involved in several diseases like celiac disease (CeD). The polyQ…”
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Condensation of the β‐cell secretory granule luminal cargoes pro/insulin and ICA512 RESP18 homology domain by Toledo, Pamela L., Vazquez, Diego S., Gianotti, Alejo R., Abate, Milagros B., Wegbrod, Carolin, Torkko, Juha M., Solimena, Michele, Ermácora, Mario R.

“…ICA512/PTPRN is a receptor tyrosine‐like phosphatase implicated in the biogenesis and turnover of the insulin secretory granules (SGs) in pancreatic islet beta…”
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Protein nanocondensates: the next frontier by Toledo, Pamela L., Gianotti, Alejo R., Vazquez, Diego S., Ermácora, Mario R.

“…Over the past decade, myriads of studies have highlighted the central role of protein condensation in subcellular compartmentalization and spatiotemporal…”
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PrxQ B from Mycobacterium tuberculosis is a monomeric, thioredoxin-dependent and highly efficient fatty acid hydroperoxide reductase by Reyes, Aníbal M., Vazquez, Diego S., Zeida, Ari, Hugo, Martín, Piñeyro, M. Dolores, De Armas, María Inés, Estrin, Darío, Radi, Rafael, Santos, Javier, Trujillo, Madia

“…Mycobacterium tuberculosis (M. tuberculosis) is the intracellular bacterium responsible for tuberculosis disease (TD). Inside the phagosomes of activated…”
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Insights on the conformational dynamics of human frataxin through modifications of loop-1 by Noguera, Martín E., Aran, Martín, Smal, Clara, Vazquez, Diego S., Herrera, María Georgina, Roman, Ernesto A., Alaimo, Nadine, Gallo, Mariana, Santos, Javier

“…Human frataxin (FXN) is a highly conserved mitochondrial protein involved in iron homeostasis and activation of the iron-sulfur cluster assembly. FXN…”
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Molecular Basis of Hydroperoxide Specificity in Peroxiredoxins: The Case of AhpE from Mycobacterium tuberculosis by Zeida, Ari, Reyes, Aníbal M, Lichtig, Pablo, Hugo, Martín, Vazquez, Diego S, Santos, Javier, González Flecha, F. Luis, Radi, Rafael, Estrin, Dario A, Trujillo, Madia

“…Peroxiredoxins (Prxs) constitute a ubiquitous family of Cys-dependent peroxidases that play essential roles in reducing hydrogen peroxide, peroxynitrite, and…”
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The E. coli thioredoxin folding mechanism: The key role of the C-terminal helix by Vazquez, Diego S., Sánchez, Ignacio E., Garrote, Ana, Sica, Mauricio P., Santos, Javier

“…In this work, the unfolding mechanism of oxidized Escherichia coli thioredoxin (EcTRX) was investigated experimentally and computationally. We characterized…”
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Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants by Noguera, Martín E., Vazquez, Diego S., Ferrer-Sueta, Gerardo, Agudelo, William A., Howard, Eduardo, Rasia, Rodolfo M., Manta, Bruno, Cousido-Siah, Alexandra, Mitschler, André, Podjarny, Alberto, Santos, Javier

“…Thioredoxin is a ubiquitous small protein that catalyzes redox reactions of protein thiols. Additionally, thioredoxin from E. coli (EcTRX) is a widely-used…”
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A helix-coil transition induced by the metal ion interaction with a grafted iron-binding site of the CyaY protein family by Vazquez, Diego S, Agudelo, William A, Yone, Angel, Vizioli, Nora, Arán, Martín, González Flecha, F Luis, González Lebrero, Mariano C, Santos, Javier

“…Iron-protein interactions are involved in electron transfer reactions. Alterations of these processes are present in a number of human pathologies; among them,…”
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