Leonardo Boechi

1.3k total citations
40 papers, 1.1k citations indexed

About

Leonardo Boechi is a scholar working on Molecular Biology, Cell Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, Leonardo Boechi has authored 40 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 33 papers in Cell Biology and 10 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in Leonardo Boechi's work include Hemoglobin structure and function (33 papers), Protein Structure and Dynamics (19 papers) and Heme Oxygenase-1 and Carbon Monoxide (13 papers). Leonardo Boechi is often cited by papers focused on Hemoglobin structure and function (33 papers), Protein Structure and Dynamics (19 papers) and Heme Oxygenase-1 and Carbon Monoxide (13 papers). Leonardo Boechi collaborates with scholars based in Argentina, Italy and United States. Leonardo Boechi's co-authors include Darío A. Estrı́n, Marcelo A. Martí, Damián E. Bikiel, F. Javier Luque, Giulietta Smulevich, Luciana Capece, Flavio Forti, Sara E. Bari, Alessandro Feis and Pau Arroyo and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Bioinformatics.

In The Last Decade

Leonardo Boechi

39 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Leonardo Boechi Argentina 23 757 631 149 144 115 40 1.1k
Jotaro Igarashi Japan 24 760 1.0× 553 0.9× 114 0.8× 380 2.6× 83 0.7× 67 1.5k
Leslie W.‐M. Fung United States 23 712 0.9× 555 0.9× 179 1.2× 511 3.5× 100 0.9× 65 1.4k
Gary Silkstone United Kingdom 19 667 0.9× 431 0.7× 115 0.8× 170 1.2× 21 0.2× 29 958
Johannes P. M. Schelvis United States 21 683 0.9× 241 0.4× 47 0.3× 322 2.2× 88 0.8× 41 1.3k
Vandna Sharma United States 13 538 0.7× 507 0.8× 194 1.3× 457 3.2× 105 0.9× 27 1.1k
Yi Dou United States 18 710 0.9× 810 1.3× 195 1.3× 282 2.0× 21 0.2× 21 1.1k
Yutaka Orii Japan 23 1.1k 1.4× 582 0.9× 100 0.7× 185 1.3× 52 0.5× 83 1.6k
Masako Nagai Japan 17 449 0.6× 477 0.8× 147 1.0× 180 1.3× 17 0.1× 45 794
Jordi Cohen United States 11 656 0.9× 304 0.5× 52 0.3× 65 0.5× 30 0.3× 14 1.0k
Ernesto E. Di Iorio Switzerland 16 570 0.8× 440 0.7× 139 0.9× 203 1.4× 29 0.3× 35 918

Countries citing papers authored by Leonardo Boechi

Since Specialization
Citations

This map shows the geographic impact of Leonardo Boechi'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 Leonardo Boechi with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Leonardo Boechi more than expected).

Fields of papers citing papers by Leonardo Boechi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leonardo Boechi. 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 Leonardo Boechi. The network helps show where Leonardo Boechi may publish in the future.

Co-authorship network of co-authors of Leonardo Boechi

This figure shows the co-authorship network connecting the top 25 collaborators of Leonardo Boechi. A scholar is included among the top collaborators of Leonardo Boechi 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 Leonardo Boechi. Leonardo Boechi is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Boechi, Leonardo, et al.. (2022). Uncovering differential equations from data with hidden variables. Physical review. E. 105(5). 54209–54209. 10 indexed citations
2.
Boechi, Leonardo, et al.. (2020). Clustering high dimensional meteorological scenarios: results and\n performance index. arXiv (Cornell University).
3.
Bringas, Mauro, et al.. (2019). Hemeproteins as Targets for Sulfide Species. Antioxidants and Redox Signaling. 32(4). 247–257. 27 indexed citations
4.
Howes, Barry D., Leonardo Boechi, Alberto Boffi, Darío A. Estrı́n, & Giulietta Smulevich. (2015). Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins. Advances in microbial physiology. 67. 85–126. 5 indexed citations
5.
Bustamante, Juan P., Alessandra Bonamore, Alejandro D. Nadra, et al.. (2014). Molecular basis of thermal stability in truncated (2/2) hemoglobins. Biochimica et Biophysica Acta (BBA) - General Subjects. 1840(7). 2281–2288. 7 indexed citations
6.
Capece, Luciana, Leonardo Boechi, Laura L. Perissinotti, et al.. (2013). Small ligand–globin interactions: Reviewing lessons derived from computer simulation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(9). 1722–1738. 37 indexed citations
7.
Boechi, Leonardo, et al.. (2013). Hydrophobic Effect Drives Oxygen Uptake in Myoglobin via Histidine E7. Journal of Biological Chemistry. 288(9). 6754–6762. 28 indexed citations
8.
Oliveira, Ana, Sandeep Singh, Axel Bidon‐Chanal, et al.. (2012). Role of PheE15 Gate in Ligand Entry and Nitric Oxide Detoxification Function of Mycobacterium tuberculosis Truncated Hemoglobin N. PLoS ONE. 7(11). e49291–e49291. 25 indexed citations
9.
Boechi, Leonardo, et al.. (2012). The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin. Journal of Inorganic Biochemistry. 119. 75–84. 10 indexed citations
10.
Forti, Flavio, Leonardo Boechi, Darío A. Estrı́n, & Marcelo A. Martí. (2011). Comparing and combining implicit ligand sampling with multiple steered molecular dynamics to study ligand migration processes in heme proteins. Journal of Computational Chemistry. 32(10). 2219–2231. 34 indexed citations
11.
Boechi, Leonardo, Marcelo A. Martí, Alessandro Vergara, et al.. (2011). Protonation of histidine 55 affects the oxygen access to heme in the alpha chain of the hemoglobin from the Antarctic fish Trematomus bernacchii. IUBMB Life. 63(3). 175–182. 13 indexed citations
12.
Russo, Roberta, Leonardo Boechi, C.‐H. Christina Cheng, et al.. (2011). Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations. IUBMB Life. 63(3). 206–213. 11 indexed citations
13.
Moreno, Diego M., Marcelo A. Martí, Pablo M. De Biase, et al.. (2010). Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration. Archives of Biochemistry and Biophysics. 507(2). 304–309. 47 indexed citations
14.
Arroyo, Pau, Damián E. Bikiel, Leonardo Boechi, et al.. (2010). Protein dynamics and ligand migration interplay as studied by computer simulation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(8). 1054–1064. 31 indexed citations
15.
Howes, Barry D., Daniela Giordano, Leonardo Boechi, et al.. (2010). The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125. JBIC Journal of Biological Inorganic Chemistry. 16(2). 299–311. 20 indexed citations
16.
Giordano, Daniela, Leonardo Boechi, Alessandro Vergara, et al.. (2009). The hemoglobins of the sub‐Antarctic fish Cottoperca gobio, a phyletically basal species – oxygen‐binding equilibria, kinetics and molecular dynamics. FEBS Journal. 276(8). 2266–2277. 24 indexed citations
17.
Boechi, Leonardo, Pau Arroyo, F. Javier Luque, Marcelo A. Martí, & Darío A. Estrı́n. (2009). Unraveling the molecular basis for ligand binding in truncated hemoglobins: The trHbO Bacillus subtilis case. Proteins Structure Function and Bioinformatics. 78(4). 962–970. 32 indexed citations
18.
Boechi, Leonardo, Marcelo A. Martí, Mario Milani, et al.. (2008). Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O. Proteins Structure Function and Bioinformatics. 73(2). 372–379. 45 indexed citations
19.
Martí, Marcelo A., Alejandro Crespo, Luciana Capece, et al.. (2006). Dioxygen affinity in heme proteins investigated by computer simulation. Journal of Inorganic Biochemistry. 100(4). 761–770. 87 indexed citations
20.
Bikiel, Damián E., Leonardo Boechi, Luciana Capece, et al.. (2006). Modeling heme proteins using atomistic simulations. Physical Chemistry Chemical Physics. 8(48). 5611–5628. 68 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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