Eduardo A. Ceccarelli

5.5k total citations · 2 hit papers
73 papers, 4.2k citations indexed

About

Eduardo A. Ceccarelli is a scholar working on Molecular Biology, Inorganic Chemistry and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Eduardo A. Ceccarelli has authored 73 papers receiving a total of 4.2k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 16 papers in Inorganic Chemistry and 12 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Eduardo A. Ceccarelli's work include Photosynthetic Processes and Mechanisms (36 papers), Metal-Catalyzed Oxygenation Mechanisms (16 papers) and Enzyme Structure and Function (11 papers). Eduardo A. Ceccarelli is often cited by papers focused on Photosynthetic Processes and Mechanisms (36 papers), Metal-Catalyzed Oxygenation Mechanisms (16 papers) and Enzyme Structure and Function (11 papers). Eduardo A. Ceccarelli collaborates with scholars based in Argentina, United States and Spain. Eduardo A. Ceccarelli's co-authors include Germán L. Rosano, Néstor Carrillo, Adrián K. Arakaki, Daniela V. Rial, Elena G. Orellano, Jorgelina Ottado, Rubén H. Vallejos, Nora B. Calcaterra, Raquel L. Chan and Néstor Cortez and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Biochemistry.

In The Last Decade

Eduardo A. Ceccarelli

73 papers receiving 4.1k citations

Hit Papers

2 papers align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Recombinant protein expression in Escherichia coli: advances and challenges

2014 1.7k citations Germán L. Rosano, Eduardo A. Ceccarelli Frontiers in Microbiology profile →
New tools for recombinant protein production in Escherichia coli: A 5‐year update

2019 256 citations Germán L. Rosano, Eduardo A. Ceccarelli et al. profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Eduardo A. Ceccarelli Argentina	26	3.2k	528	513	447	399	73	4.2k
Uwe Linne Germany	44	3.8k 1.2×	624 1.2×	434 0.8×	197 0.4×	409 1.0×	126	5.9k
Fredrik Åslund Sweden	26	4.3k 1.3×	329 0.6×	729 1.4×	424 0.9×	194 0.5×	29	5.4k
Satish K. Nair United States	48	5.9k 1.8×	552 1.0×	656 1.3×	380 0.9×	707 1.8×	167	8.2k
Hans‐Jürgen Hecht Germany	32	2.4k 0.7×	567 1.1×	192 0.4×	423 0.9×	314 0.8×	70	5.0k
J.A. Hermoso Spain	45	4.1k 1.3×	414 0.8×	758 1.5×	353 0.8×	591 1.5×	192	6.5k
Dirk W. Heinz Germany	42	3.6k 1.1×	295 0.6×	556 1.1×	180 0.4×	728 1.8×	101	5.3k
P. John Hart United States	44	2.9k 0.9×	721 1.4×	186 0.4×	406 0.9×	217 0.5×	115	6.3k
Luke W. Guddat Australia	48	4.6k 1.4×	1.4k 2.6×	352 0.7×	416 0.9×	206 0.5×	211	7.7k
David L. Ollis Australia	47	5.4k 1.7×	1.0k 1.9×	938 1.8×	295 0.7×	412 1.0×	140	7.9k
Wulf Blankenfeldt Germany	38	3.1k 1.0×	622 1.2×	470 0.9×	156 0.3×	297 0.7×	147	4.9k

Countries citing papers authored by Eduardo A. Ceccarelli

Since Specialization

Citations

This map shows the geographic impact of Eduardo A. Ceccarelli's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Eduardo A. Ceccarelli with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Eduardo A. Ceccarelli more than expected).

Fields of papers citing papers by Eduardo A. Ceccarelli

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eduardo A. Ceccarelli. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Eduardo A. Ceccarelli. The network helps show where Eduardo A. Ceccarelli may publish in the future.

Co-authorship network of co-authors of Eduardo A. Ceccarelli

This figure shows the co-authorship network connecting the top 25 collaborators of Eduardo A. Ceccarelli. A scholar is included among the top collaborators of Eduardo A. Ceccarelli based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Eduardo A. Ceccarelli. Eduardo A. Ceccarelli is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Ceccarelli, Eduardo A., et al.. (2019). A bacterial 2[4Fe 4S] ferredoxin as redox partner of the plastidic-type ferredoxin-NADP+ reductase from Leptospira interrogans. Biochimica et Biophysica Acta (BBA) - General Subjects. 1863(4). 651–660. 4 indexed citations

Balaban, Cecilia L., et al.. (2018). Proteome variation of the rat liver after static cold storage assayed in an ex vivo model. Cryobiology. 85. 47–55. 1 indexed citations

Klinke, Sebastián, et al.. (2017). Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism. PLoS ONE. 12(8). e0182535–e0182535. 4 indexed citations

Ceccarelli, Eduardo A., Charles L. Cantrell, Néstor Carrillo, et al.. (2016). Khellin and Visnagin, Furanochromones from Ammi visnaga (L.) Lam., as Potential Bioherbicides. Journal of Agricultural and Food Chemistry. 64(50). 9475–9487. 51 indexed citations

Rosano, Germán L. & Eduardo A. Ceccarelli. (2014). Recombinant protein expression in microbial systems. Frontiers in Microbiology. 5. 341–341. 68 indexed citations

Tondo, María Laura, et al.. (2014). Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837(10). 1730–1738. 13 indexed citations

Yao, Huili, et al.. (2014). Heme-iron utilization by Leptospira interrogans requires a heme oxygenase and a plastidic-type ferredoxin-NADP+ reductase. Biochimica et Biophysica Acta (BBA) - General Subjects. 1840(11). 3208–3217. 7 indexed citations

Rosano, Germán L. & Eduardo A. Ceccarelli. (2014). Recombinant protein expression in Escherichia coli: advances and challenges. Frontiers in Microbiology. 5. 172–172. 1726 indexed citations breakdown →

Ceccarelli, Eduardo A., et al.. (2013). Redox Proteins as Targets for Drugs Development Against Pathogens. Current Pharmaceutical Design. 19(14). 2594–2605. 8 indexed citations

10.

Rosano, Germán L., et al.. (2012). Toward a unified model of the action of CLP/HSP100 chaperones in chloroplasts. Plant Signaling & Behavior. 7(6). 672–674. 4 indexed citations

11.

Musumeci, Matías A., et al.. (2012). Structural backgrounds for the formation of a catalytically competent complex with NADP(H) during hydride transfer in ferredoxin–NADP+ reductases. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(7). 1063–1071. 11 indexed citations

12.

Musumeci, Matías A., et al.. (2011). A Highly Stable Plastidic-Type Ferredoxin-NADP(H) Reductase in the Pathogenic Bacterium Leptospira interrogans. PLoS ONE. 6(10). e26736–e26736. 13 indexed citations

13.

Carrillo, Néstor, Eduardo A. Ceccarelli, & Oscar A. Roveri. (2010). Usefulness of Kinetic Enzyme Parameters in Biotechnological Practice. Biotechnology and Genetic Engineering Reviews. 27(1). 367–382. 29 indexed citations

14.

Rial, Daniela V., Jorgelina Ottado, & Eduardo A. Ceccarelli. (2003). Precursors with Altered Affinity for Hsp70 in Their Transit Peptides Are Efficiently Imported into Chloroplasts. Journal of Biological Chemistry. 278(47). 46473–46481. 22 indexed citations

15.

Rial, Daniela V., Verónica A. Lombardo, Eduardo A. Ceccarelli, & Jorgelina Ottado. (2002). The import of ferredoxin–NADP⁺ reductase precursor into chloroplasts is modulated by the region between the transit peptide and the mature core of the protein. European Journal of Biochemistry. 269(22). 5431–5439. 17 indexed citations

16.

Karplus, P. Andrew, Zhan Deng, Alessandro Aliverti, et al.. (1999). A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies.. Nature Structural Biology. 6(9). 847–853. 173 indexed citations

17.

Orellano, Elena G., Javier E. Girardini, Julia A. Cricco, Eduardo A. Ceccarelli, & Alejandro J. Vila. (1998). Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase II. Biochemistry. 37(28). 10173–10180. 98 indexed citations

18.

Serra, Esteban, Adriana R. Krapp, Jorgelina Ottado, et al.. (1995). The Precursor of Pea Ferredoxin-NADP+ Reductase Synthesized in Escherichia coli Contains Bound FAD and Is Transported into Chloroplasts. Journal of Biological Chemistry. 270(34). 19930–19935. 21 indexed citations

19.

Serra, Esteban, Néstor Carrillo, Adriana R. Krapp, & Eduardo A. Ceccarelli. (1993). One-Step Purification of Plant Ferredoxin-NADP+ Oxidoreductase Expressed in Escherichia coli as Fusion with Glutathione S-Transferase. Protein Expression and Purification. 4(6). 539–546. 14 indexed citations

20.

Bullough, David A., Eduardo A. Ceccarelli, David Roise, & William S. Allison. (1989). Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 975(3). 377–383. 60 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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