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Luis C. Romero

Researcher at Spanish National Research Council

Publications -  96
Citations -  6324

Luis C. Romero is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Cysteine & Arabidopsis. The author has an hindex of 36, co-authored 88 publications receiving 4394 citations. Previous affiliations of Luis C. Romero include University of Seville & Rutgers University.

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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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An O-Acetylserine(thiol)lyase Homolog with l-Cysteine Desulfhydrase Activity Regulates Cysteine Homeostasis in Arabidopsis

TL;DR: The results suggest that DES1 from Arabidopsis is an l-Cys desulfhydrase involved in maintaining Cys homeostasis, mainly at late developmental stages or under environmental perturbations.
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S-sulfhydration: a cysteine posttranslational modification in plant systems

TL;DR: Investigation of Arabidopsis proteins modified by S-sulfhydration shows evidence of the mechanism of action of hydrogen sulfide as a signaling molecule in plant systems and reversibly regulates the functions of plant proteins in a manner similar to that described in mammalian systems.
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Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis.

TL;DR: Protein persulfidation in the Arabidopsis proteome is widespread and is the molecular mechanism by which hydrogen sulfide performs its signaling role.
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A novel endo-beta -1,3-glucanase, bgn13.1, involved in the mycoparasitism of trichoderma harzianum

TL;DR: Sequence comparison shows that this beta-1,3-glucanase, first described for filamentous fungi, belongs to a family different from that of its previously described bacterial, yeast, and plant counterparts.