https://repositorio.uchile.cl/handle/2250/117694 Libros y capítulos de libros 2026-05-09T19:46:59Z https://repositorio.uchile.cl/handle/2250/197286 Genome editing and protein energy malnutrition Moreno Nombela, S.; Romero Parra, Javier Hernán; Ruiz Ojeda, F. J.; Solis Urra, P.; Baig, A. T.; Plaza Díaz, J. Protein-energy malnutrition is a state of disordered catabolism resulting from metabolic derangements or starvation. It is associated with chronic disease, hypoglycemia, hypothermia, serious infections, and even an increased prevalence of morbidity and mortality in countries with poor socioeconomic or environmental factors. Adequate food administration is essential to satisfy the main caloric and nutritional demands of humans. The most significant factors seen in the development of protein-energy malnutrition in areas of high incidence, such as underdeveloped countries, are inadequate food and nutrient supplies. It has been well established that one of the strategies to alleviate undernourishment is the biofortification of staple crops. This is because vegetables and plants are significant sources of crucial nutrients for human growth and development. To enhance plant nutrition, recent tactics aim to formulated balanced and diverse diets with acceptable levels of vitamins and minerals that benefit human health. New advances in plant biotechnology and animal productivity could control key enzymes in several metabolic pathways, enriching important nutrients such as iron and vitamins and decreasing the content of disadvantageous compounds such as acrylamide-forming amino acids and phytic acids. Numerous biofortified crops such as rice, maize, and wheat have been created to resolve the problem of nutrition deficiencies. Some examples of these methodologies are genome editing engineered nucleases, transcriptional activator-like effector nucleases, zinc finger nucleases, and clustered regularly interspaced short palindromic repeats and associated Cas9 endonuclease which have been created and widely studied for their application, efficiency, and specificity. 2023-01-01T00:00:00Z https://repositorio.uchile.cl/handle/2250/192947 Posttranslational Protein Translocation through Membranes at the Single-Molecule Level Quiroga Roger, Diego; Alfaro Valdés, Hilda M.; Wilson Moya, Christian A.M. Protein secretion studies started in the 1950s with George Palade’s electron microscopy (EM) work (Palade, 1952, 1975). Protein secretion is a very relevant process because more than 30 percent of synthesized proteins work in organelles or outside the cells (Arora and Tamm, 2001). In eukaryotic cells, the proteins secreted to the exterior are synthesized in the cytoplasm and transported inside the endoplasmic reticulum (ER), then pass to the Golgi apparatus and finally to secretory vesicles. Blobel and Sabatini in the 1970s discovered signal sequences at the N-terminus extreme of secretory proteins that allow them to be recognized by receptors thus mediating and facilitating their entrance to ER interior (Blobel and Dobberstein, 1975; Sabatini et al., 1982). Proteins enter the ER lumen by a protein conducting channel formed by a protein complex, known as the translocon, discovered in yeast in Randy Schekman´s laboratory, which is universally conserved (Deshaies et al., 1991). In eukaryotic cells, the translocation of proteins into ER lumen is carried out by the Sec61 complex (Rapoport, 2007; Zimmermann et al., 2011), whereas the bacterial homologue is the heterotrimeric SecY complex, which allows the secretion of proteins to the exterior (Park and Rapoport, 2012). 2022-01-01T00:00:00Z https://repositorio.uchile.cl/handle/2250/192940 Mechanical Properties of Chaperone BiP, the Master Regulator of the Endoplasmic Reticulum Alfaro Valdés, Hilda M.; Burgos Bravo, Francesca; Casanova Morales, Nathalie; Quiroga Roger, Diego; Wilson Moya, Christian A.M. Immunoglobulin heavy-chain-binding protein (BiP protein) is a 75-kDa Hsp70 monomeric ATPase motor that plays broad and crucial roles maintaining proteostasis inside the cell. Its malfunction has been related with the appearance of many and important health problems such as neurodegenerative diseases, cancer, and heart diseases, among others. In particular, it is involved in many endoplasmic reticulum (ER) processes and functions, such as protein synthesis, folding, and assembly, and also it works in the posttranslational mechanism of protein translocation. However, it is unknown what kind of molecular motor BiP works like, since the mechanochemical mechanism that BiP utilizes to perform its work during posttranslational translocation across the ER is not fully understood. One novel approach to study both structural and catalytic properties of BiP considers that the viscoelastic regime behavior of the enzymes (considering them as a spring) and their mechanical properties are correlated with catalysis and ligand binding. Structurally, BiP is formed by two domains, and to establish a correlation between BiP structure and catalysis and how its conformational and viscoelastic changes are coupled to ligand binding, catalysis, and allosterism (information transmitted between the domains), optical tweezers and nano-rheology techniques have been essential in this regard. 2018-01-01T00:00:00Z https://repositorio.uchile.cl/handle/2250/192849 Memoria anual 2017 2017-01-01T00:00:00Z