C
Cecilia D'Alessio
Researcher at Fundación Instituto Leloir
Publications - 25
Citations - 799
Cecilia D'Alessio is an academic researcher from Fundación Instituto Leloir. The author has contributed to research in topics: Endoplasmic reticulum & Glycan. The author has an hindex of 13, co-authored 21 publications receiving 688 citations. Previous affiliations of Cecilia D'Alessio include Facultad de Ciencias Exactas y Naturales & University of Buenos Aires.
Papers
More filters
Journal ArticleDOI
UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control
Cecilia D'Alessio,Julio J. Caramelo,Julio J. Caramelo,Julio J. Caramelo,Armando J. Parodi,Armando J. Parodi +5 more
TL;DR: The N-glycan-dependent quality control of glycoprotein folding prevents endoplasmic to Golgi exit of folding intermediates, irreparably misfolded glycoproteins and incompletely assembled multimeric complexes and enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds.
Journal ArticleDOI
Genetic Evidence for the Heterodimeric Structure of Glucosidase II THE EFFECT OF DISRUPTING THE SUBUNIT-ENCODING GENES ON GLYCOPROTEIN FOLDING
TL;DR: Formation of monoglucosylated oligosaccharides decreased the folding rate and increased the folding efficiency of glycoproteins as pulse-chase experiments revealed that carboxypeptidase Y arrived at a higher rate but in decreased amounts to the vacuoles of gls2α than to those of wild type cells.
Journal ArticleDOI
The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress.
TL;DR: It is suggested that facilitation of glycoprotein folding mediated by the interaction of monoglucosylated oligosaccharides with calnexin is essential for cell viability under conditions of extreme ER stress such as underglycosylation of proteins caused by the alg6 mutation and high temperature.
Posted ContentDOI
Structural and Functional Comparison of SARS-CoV-2-Spike Receptor Binding Domain Produced in Pichia pastoris and Mammalian Cells
Alicia M. Zelada,Gabriela Alejandra Auge,Matías Blaustein,Luis M. Bredeston,Enrique Sebastian Corapi,Patricio O. Craig,Leandro Andres Cossio,Liliana Dain,Cecilia D'Alessio,Fernanda Elias,Natalia Fernández,Javier Gasulla,Natalia Gorojovsky,Gustavo Eduardo Gudesblat,Maria Georgina Herrera,Lorena Itatí Ibañez,Tommy Idrovo Hidalgo,Matías Iglesias Randon,Laura Kamenetzky,Alejandro D. Nadra,Diego Gabriel Noseda,Carlos Humberto Pavan,Maria Florencia Pavan,María Florencia Pignataro,Ernesto A. Roman,Lucas Ruberto,Natalia Rubinstein,Javier Santos,Francisco Velázquez Duarte +28 more
TL;DR: The conformation of the receptor binding domain (RBD) from severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is compared with Spike protein expressed in P. pastoris and in the well established HEK-293T mammalian cell system to potentially allow large scale immunizations to produce neutralizing antibodies.
Journal ArticleDOI
The UDP-glucose: glycoprotein glucosyltransferase (UGGT), a key enzyme in ER quality control, plays a significant role in plant growth as well as biotic and abiotic stress in Arabidopsis thaliana
Francisca Blanco-Herrera,Adrián A. Moreno,Rodrigo Tapia,Francisca Reyes,Macarena Araya,Cecilia D'Alessio,Cecilia D'Alessio,Armando J. Parodi,Ariel Orellana +8 more
TL;DR: The results show that a lack of UGGT activity alters plant vegetative development and impairs the response to several abiotic and biotic stresses, and uncover an unexpected role of U GGT in the incorporation of UDP-Glucose into the ER lumen in Arabidopsis thaliana.