Search Results - "Ceccarelli, Eduardo A"

New tools for recombinant protein production in Escherichia coli: A 5‐year update by Rosano, Germán L., Morales, Enrique S., Ceccarelli, Eduardo A.

“…The production of proteins in sufficient amounts is key for their study or use as biotherapeutic agents. Escherichia coli is the host of choice for recombinant…”
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Recombinant protein expression in Escherichia coli: advances and challenges by Rosano, Germán L, Ceccarelli, Eduardo A

“…Escherichia coli is one of the organisms of choice for the production of recombinant proteins. Its use as a cell factory is well-established and it has become…”
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A novel method for removing contaminant Hsp70 molecular chaperones from recombinant proteins by Morales, Enrique S., Parcerisa, Ivana L., Ceccarelli, Eduardo A.

“…The production of recombinant proteins in bacteria has increased significantly in recent years, becoming a common tool for both research and the industrial…”
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Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strain by Rosano, Germán L, Ceccarelli, Eduardo A

“…The expression of heterologous proteins in Escherichia coli is strongly affected by codon bias. This phenomenon occurs when the codon usage of the mRNA coding…”
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TAT-mediated transduction of bacterial redox proteins generates a cytoprotective effect on neuronal cells by Balaban, Cecilia L, Banchio, Claudia, Ceccarelli, Eduardo A

“…Cell penetrating peptides, also known as protein transduction domains, have the capacity to ubiquitously cross cellular membranes carrying many different…”
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Recombinant protein expression in microbial systems by Rosano, Germán L, Ceccarelli, Eduardo A

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The long-term antibody response after SARS-CoV-2 prime-boost vaccination in healthy individuals. The positive influence of extended between-dose intervals and heterologous schedule by Naidich, Gretel, Santucci, Natalia E, Pezzotto, Stella Maris, Ceccarelli, Eduardo A, Bottasso, Oscar A, Perichón, A Mario

“…Anti-COVID vaccination in Argentina was carried out using different protocols and variations in periods between administrations, as well as combinations of…”
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A novel Xanthomonas citri subsp. citri NADPH quinone reductase involved in salt stress response and virulence by Barcarolo, Maria Victoria, Garavaglia, Betiana S., Gottig, Natalia, Ceccarelli, Eduardo A., Catalano-Dupuy, Daniela L., Ottado, Jorgelina

“…Xanthomonas citri subsp. citri (Xcc), the causal agent of citrus canker is maintained as an epiphyte on citrus leaves until entering the plant tissue. During…”
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Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism by Soldano, Anabel, Klinke, Sebastián, Otero, Lisandro H, Rivera, Mario, Catalano-Dupuy, Daniela L, Ceccarelli, Eduardo A

“…Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the…”
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Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes by Sánchez-Azqueta, Ana, Catalano-Dupuy, Daniela L., López-Rivero, Arleth, Tondo, María Laura, Orellano, Elena G., Ceccarelli, Eduardo A., Medina, Milagros

“…Kinetic isotope effects in reactions involving hydride transfer and their temperature dependence are powerful tools to explore dynamics of enzyme catalytic…”
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Redox proteins as targets for drugs development against pathogens by Catalano-Dupuy, Daniela L, López-Rivero, Arleth, Soldano, Anabel, Ceccarelli, Eduardo A

“…Antimicrobial drug resistance in pathogens is an increasing human health problem. The rapid loss of effectiveness in antibiotics treatments and the…”
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Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases by Ceccarelli, Eduardo A., Arakaki, Adrián K., Cortez, Néstor, Carrillo, Néstor

“…Ferredoxin (flavodoxin)-NADP(H) reductases (FNRs) are ubiquitous flavoenzymes that deliver NADPH or low potential one-electron donors (ferredoxin, flavodoxin,…”
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Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a transit peptide only when it is located at the N-terminus of a protein by Bruch, Eduardo M, Rosano, Germán L, Ceccarelli, Eduardo A

“…Clp/Hsp100 chaperones are involved in protein quality control. They act as independent units or in conjunction with a proteolytic core to degrade irreversibly…”
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Open questions in ferredoxin‐NADP+ reductase catalytic mechanism by Carrillo, Néstor, Ceccarelli, Eduardo A.

“…Ferredoxin (flavodoxin)‐NADP(H) reductases (FNR) are ubiquitous flavoenzymes that deliver NADPH or low potential one‐electron donors (ferredoxin, flavodoxin)…”
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Structural-functional characterization and physiological significance of ferredoxin-NADP reductase from Xanthomonas axonopodis pv. citri by Tondo, María Laura, Musumeci, Matías A, Delprato, María Laura, Ceccarelli, Eduardo A, Orellano, Elena G

“…Xanthomonas axonopodis pv. citri is a phytopathogen bacterium that causes severe citrus canker disease. Similar to other phytopathogens, after infection by…”
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A highly stable plastidic-type ferredoxin-NADP(H) reductase in the pathogenic bacterium Leptospira interrogans by Catalano-Dupuy, Daniela L, Musumeci, Matías A, López-Rivero, Arleth, Ceccarelli, Eduardo A

“…Leptospira interrogans is a bacterium that is capable of infecting animals and humans, and its infection causes leptospirosis with a range of symptoms from…”
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Induced Fit and Equilibrium Dynamics for High Catalytic Efficiency in Ferredoxin-NADP(H) Reductases by Paladini, Darío H, Musumeci, Matías A, Carrillo, Néstor, Ceccarelli, Eduardo A

“…Ferredoxin-NADP(H) reductase (FNR) is a FAD-containing protein that catalyzes the reversible transfer of electrons between NADP(H) and ferredoxin or…”
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Biochemical characterization of ClpB3, a chloroplastic disaggregase from Arabidopsis thaliana by Parcerisa, Ivana L., Rosano, Germán L., Ceccarelli, Eduardo A.

“…Key message The first biochemical characterization of a chloroplastic disaggregase is reported ( Arabidopsis thaliana ClpB3). ClpB3 oligomerizes into active…”
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Toward a unified model of the action of CLP/HSP100 chaperones in chloroplasts by Rosano, Germán L., Bruch, Eduardo M., Colombo, Clara V., Ceccarelli, Eduardo A.

“…In chloroplasts, Hsp70 and Hsp100 chaperones have been long suspected to be the motors that provide the necessary energy for the import of precursor proteins…”
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Structural features of the plant N‐recognin ClpS1 and sequence determinants in its targets that govern substrate selection by Aguilar Lucero, Dianela, Cantoia, Alejo, Sánchez‐López, Carolina, Binolfi, Andrés, Mogk, Axel, Ceccarelli, Eduardo A., Rosano, Germán L., Flügge, Ulf‐Ingo

“…In the N‐degron pathway of protein degradation of Escherichia coli, the N‐recognin ClpS identifies substrates bearing N‐terminal phenylalanine, tyrosine,…”
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