E
Eduardo A. Ceccarelli
Researcher at National University of Rosario
Publications - 84
Citations - 4705
Eduardo A. Ceccarelli is an academic researcher from National University of Rosario. The author has contributed to research in topics: Ferredoxin—NADP(+) reductase & Ferredoxin. The author has an hindex of 28, co-authored 82 publications receiving 4039 citations. Previous affiliations of Eduardo A. Ceccarelli include National Scientific and Technical Research Council & University of California, San Diego.
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Journal ArticleDOI
Recombinant protein expression in Escherichia coli: advances and challenges.
TL;DR: The different approaches for the synthesis of recombinant proteins in E. coli are reviewed and recent progress in this ever-growing field is discussed.
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Open questions in ferredoxin‐NADP+ reductase catalytic mechanism
TL;DR: Using the formalism of the Albery-Knowles theory, which identifies which parameter(s) have to be modified to make these reductases even more proficient under a variety of conditions, natural or artificial, a rationale to interpret FNR evolution in terms of catalytic efficiency is provided.
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New tools for recombinant protein production in Escherichia coli: A 5-year update.
TL;DR: This work reviews the latest advances in recombinant protein production in E. coli using plasmids and cultivation conditions to optimize product yield.
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A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.
Z. Deng,Alessandro Aliverti,Giuliana Zanetti,Adrián K. Arakaki,Jorgelina Ottado,Elena G. Orellano,Nora B. Calcaterra,Eduardo A. Ceccarelli,Néstor Carrillo,P.A. Karplus,P.A. Karplus +10 more
TL;DR: In this article, the authors used mutants of this residue (Tyr 308) of pea ferredoxin-NADP+ reductase (FNR) to obtain the structures of productive NADP+ and NADPH complexes.
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Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strain
TL;DR: The results show that the expression of heterologous proteins coded by high RIL codon content coding sequences in a codon bias-adjusted strain is detrimental for their solubility, and the hypothesis that the possible elimination of translational pauses that increase translation rate leads to protein misfolding and aggregation is supported.