Search Results - "Medus, Máximo Lopez"

N-glycosylation Triggers a Dual Selection Pressure in Eukaryotic Secretory Proteins by Medus, Máximo Lopez, Gomez, Gabriela E., Zacchi, Lucía F., Couto, Paula M., Labriola, Carlos A., Labanda, María S., Bielsa, Rodrigo Corti, Clérico, Eugenia M., Schulz, Benjamin L., Caramelo, Julio J.

“…Nearly one third of the eukaryotic proteome traverses the secretory pathway and most of these proteins are N -glycosylated in the lumen of the endoplasmic…”
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Structure of Calreticulin C-terminal Domain Is Modulated by Physiological Variations of Calcium Concentration by Giraldo, Ana María Villamil, Medus, Máximo Lopez, Lebrero, Mariano Gonzalez, Pagano, Rodrigo S, Labriola, Carlos A, Landolfo, Lucas, Delfino, José M, Parodi, Armando J, Caramelo, Julio J

“…Calreticulin is an abundant endoplasmic reticulum resident protein that fulfills at least two basic functions. Firstly, due to its ability to bind…”
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Protein Fibrillation Lag Times During Kinetic Inhibition by Pagano, Rodrigo S., López Medus, Máximo, Gómez, Gabriela E., Couto, Paula M., Labanda, María S., Landolfo, Lucas, D’Alessio, Cecilia, Caramelo, Julio J.

“…Protein aggregation is linked to more than 30 human pathologies, including Alzheimer’s and Parkinson’s diseases. Since small oligomers that form at the…”
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Endoplasmic reticulum calcium regulates the retrotranslocation of Trypanosoma cruzi calreticulin to the cytosol by Labriola, Carlos A, Conte, Ianina L, López Medus, Máximo, Parodi, Armando J, Caramelo, Julio J

“…For most secretory pathway proteins, crossing the endoplasmic reticulum (ER) membrane is an irreversible process. However, in some cases this flow can be…”
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The Structure of Calreticulin C-terminal Domain Is Modulated by Physiological Variations of Calcium Concentration2 by Giraldo, Ana María Villamil, Medus, Máximo Lopez, Lebrero, Mariano Gonzalez, Pagano, Rodrigo S., Labriola, Carlos A., Landolfo, Lucas, Delfino, José M., Parodi, Armando J., Caramelo, Julio J.

“…Calreticulin is an abundant endoplasmic reticulum resident protein that fulfills at least two basic functions. Firstly, due to its ability to bind…”
Get full text