Cesar Roncero
University of Salamanca
51 Papers
582 Citations
Cesar Roncero is an academic researcher from University of Salamanca. The author has contributed to research in topics: Chitin synthase & Chitin. The author has an hindex of 26, co-authored 48 publications. Previous affiliations of Cesar Roncero include University of Illinois at Chicago & Spanish National Research Council.
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Papers
Chs7p, a New Protein Involved in the Control of Protein Export from the Endoplasmic Reticulum that Is Specifically Engaged in the Regulation of Chitin Synthesis in Saccharomyces cerevisiae
TL;DR: Results show that Chs7p forms part of a new mechanism specifically involved in Chs3p export from the ER and consequently, in the regulation of CSIII activity.
Characterization of CHS4 (CAL2), a gene of Saccharomyces cerevisiae involved in chitin biosynthesis and allelic to SKT5 and CSD4.
TL;DR: It is proposed that Chs4p would be an essential component of the CSIII complex, acting as a post‐translational regulator of this activity, and in addition to the chitin defect, the chs4 mutant shows a severe defect in mating.
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Calcofluor Antifungal Action Depends on Chitin and a Functional High-Osmolarity Glycerol Response (HOG) Pathway: Evidence for a Physiological Role of the Saccharomyces cerevisiae HOG Pathway under Noninducing Conditions
TL;DR: Characterization of some multicopy suppressors of the calcofluor resistance phenotype indicated that constitutive HOG functionality participates in the maintenance of cell wall architecture, a conclusion supported by the antagonism observed between the protein kinase and HOG signal transduction pathways.
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Characterization of the chitin biosynthesis process as a compensatory mechanism in the fks1 mutant of Saccharomyces cerevisiae.
L. J. García-Rodriguez,Jose Angel Trilla,C Castro,María Henar Valdivieso,Angeles Duran,Cesar Roncero +5 more
TL;DR: Deregulation of CSIII activity is mainly due to the intracellular delocalization of Chs3p and Chs4p, the two main components of the CSIII active complex.
91
Triiodothyronine Induces the Transcription of the Uncoupling Protein Gene and Stabilizes Its mRNA in Fetal Rat Brown Adipocyte Primary Cultures
TL;DR: Treatment of confluent fetal rat brown adipocytes with 10 nM triiodothyronine in a serum-free medium increased the amount of UCP mRNA in a time-dependent manner, resulting in a higher content of immunoreactive mitochondrial UCP and functional UCP.
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