Leda S. Chubatsu

3.1k total citations
87 papers, 2.2k citations indexed

About

Leda S. Chubatsu is a scholar working on Molecular Biology, Genetics and Plant Science. According to data from OpenAlex, Leda S. Chubatsu has authored 87 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 29 papers in Genetics and 29 papers in Plant Science. Recurrent topics in Leda S. Chubatsu's work include Bacterial Genetics and Biotechnology (29 papers), Legume Nitrogen Fixing Symbiosis (20 papers) and Genomics and Phylogenetic Studies (18 papers). Leda S. Chubatsu is often cited by papers focused on Bacterial Genetics and Biotechnology (29 papers), Legume Nitrogen Fixing Symbiosis (20 papers) and Genomics and Phylogenetic Studies (18 papers). Leda S. Chubatsu collaborates with scholars based in Brazil, United Kingdom and United States. Leda S. Chubatsu's co-authors include Emanuel Maltempi de Souza, R. Meneghini, Fábio O. Pedrosa, Rose Adele Monteiro, Luciano F. Huergo, Maria Berenice Reynaud Steffens, M. G. Yates, Mike Merrick, L. U. Rigo and Roseli Wassem and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Leda S. Chubatsu

86 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Leda S. Chubatsu Brazil 26 1.0k 891 266 239 227 87 2.2k
David Cánovas Spain 25 1.1k 1.1× 517 0.6× 92 0.3× 158 0.7× 296 1.3× 53 2.2k
F. Reyes Spain 28 1.1k 1.1× 1.1k 1.2× 142 0.5× 121 0.5× 160 0.7× 83 2.2k
Rakesh Sharma India 25 1.5k 1.4× 323 0.4× 468 1.8× 283 1.2× 271 1.2× 91 2.7k
Bernd Masepohl Germany 26 895 0.9× 427 0.5× 129 0.5× 224 0.9× 297 1.3× 56 2.0k
Xinwei Wang China 28 1.3k 1.2× 970 1.1× 106 0.4× 175 0.7× 371 1.6× 89 2.6k
Ralf Mattes Germany 29 1.7k 1.6× 412 0.5× 195 0.7× 314 1.3× 92 0.4× 63 2.6k
Shigeyuki Kawai Japan 31 1.6k 1.5× 491 0.6× 181 0.7× 154 0.6× 57 0.3× 86 2.6k
Satoshi Harashima Japan 40 4.0k 3.8× 1.4k 1.5× 181 0.7× 283 1.2× 116 0.5× 186 5.0k
Yanfen Xue China 34 1.8k 1.7× 446 0.5× 211 0.8× 88 0.4× 182 0.8× 121 2.7k
Hideshi Yanase Japan 23 1.0k 1.0× 346 0.4× 196 0.7× 127 0.5× 99 0.4× 90 1.8k

Countries citing papers authored by Leda S. Chubatsu

Since Specialization
Citations

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

Fields of papers citing papers by Leda S. Chubatsu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leda S. Chubatsu. 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 Leda S. Chubatsu. The network helps show where Leda S. Chubatsu may publish in the future.

Co-authorship network of co-authors of Leda S. Chubatsu

This figure shows the co-authorship network connecting the top 25 collaborators of Leda S. Chubatsu. A scholar is included among the top collaborators of Leda S. Chubatsu 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 Leda S. Chubatsu. Leda S. Chubatsu 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.
Gerhardt, Edileusa C. M., Fábio O. Pedrosa, Maria Berenice Reynaud Steffens, et al.. (2020). NAD+ biosynthesis in bacteria is controlled by global carbon/nitrogen levels via PII signaling. Journal of Biological Chemistry. 295(18). 6165–6176. 15 indexed citations
2.
Santana-Filho, Arquimedes Paixão, et al.. (2020). 3-Hydroxybutyrate Derived from Poly-3-Hydroxybutyrate Mobilization Alleviates Protein Aggregation in Heat-Stressed Herbaspirillum seropedicae SmR1. Applied and Environmental Microbiology. 86(17). 12 indexed citations
3.
Oliveira, Marco Aurélio Schüler de, Emanuel Maltempi de Souza, Fábio O. Pedrosa, et al.. (2019). Regulation of Herbaspirillum seropedicae NifA by the GlnK PII signal transduction protein is mediated by effectors binding to allosteric sites. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1868(3). 140348–140348. 6 indexed citations
4.
Surek, Mônica, Bruno Stefanello Vizzotto, Vinícius Almir Weiss, et al.. (2018). Characteristics of an Aeromonas trota strain isolated from cerebrospinal fluid. Microbial Pathogenesis. 116. 109–112. 9 indexed citations
5.
Souza, Emanuel Maltempi de, et al.. (2017). Molecular characterisation ofSalmonellastrains isolated from outbreaks and sporadic cases of diarrhoea occurred in Paraná State, South of Brazil. Epidemiology and Infection. 145(9). 1953–1960. 3 indexed citations
6.
Pankievicz, Vânia C. S., Doumit Camilios‐Neto, Eduardo Balsanelli, et al.. (2016). RNA-seq transcriptional profiling of Herbaspirillum seropedicae colonizing wheat (Triticum aestivum) roots. Plant Molecular Biology. 90(6). 589–603. 47 indexed citations
7.
Donatti, Lucélia, Michelle Zibetti Tadra‐Sfeir, Maria Berenice Reynaud Steffens, et al.. (2016). Backup Expression of the PhaP2 Phasin Compensates for phaP1 Deletion in Herbaspirillum seropedicae, Maintaining Fitness and PHB Accumulation. Frontiers in Microbiology. 7. 739–739. 16 indexed citations
8.
Weiss, Vinícius Almir, Helisson Faoro, Valter A. Baura, et al.. (2015). Complete Genome Sequence of Herbaspirillum hiltneri N3 (DSM 17495), Isolated from Surface-Sterilized Wheat Roots. Genome Announcements. 3(5). 2 indexed citations
9.
Oliveira, Marco Aurélio Schüler de, Edileusa C. M. Gerhardt, Luciano F. Huergo, et al.. (2015). 2‐Oxoglutarate levels control adenosine nucleotide binding by Herbaspirillum seropedicae PII proteins. FEBS Journal. 282(24). 4797–4809. 10 indexed citations
10.
Balsanelli, Eduardo, Thalita Regina Tuleski, Valter A. Baura, et al.. (2013). Maize Root Lectins Mediate the Interaction with Herbaspirillum seropedicae via N-Acetyl Glucosamine Residues of Lipopolysaccharides. PLoS ONE. 8(10). e77001–e77001. 44 indexed citations
11.
Gerhardt, Edileusa C. M., Luíza M. Araújo, Ronny R. Ribeiro, et al.. (2012). Influence of the ADP/ATP ratio, 2-oxoglutarate and divalent ions on Azospirillum brasilense PII protein signalling. Microbiology. 158(6). 1656–1663. 14 indexed citations
12.
Weiss, Vinícius Almir, Helisson Faoro, Roberto Tadeu Raittz, et al.. (2012). Draft Genome Sequence of Herbaspirillum lusitanum P6-12, an Endophyte Isolated from Root Nodules of Phaseolus vulgaris. Journal of Bacteriology. 194(15). 4136–4137. 14 indexed citations
13.
Oliveira, Marco Aurélio Schüler de, Luciano F. Huergo, Leda S. Chubatsu, et al.. (2012). Interaction of GlnK with the GAF domain of Herbaspirillum seropedicae NifA mediates NH4+-regulation. Biochimie. 94(4). 1041–1047. 15 indexed citations
14.
Souza, Emanuel Maltempi de, Marco Aurélio Schüler de Oliveira, Rose Adele Monteiro, et al.. (2012). Uridylylation of Herbaspirillum seropedicae GlnB and GlnK proteins is differentially affected by ATP, ADP and 2-oxoglutarate in vitro. Archives of Microbiology. 194(8). 643–652. 10 indexed citations
15.
Monteiro, Rose Adele, et al.. (2011). Role of PII proteins in nitrogen fixation control of Herbaspirillum seropedicae strain SmR1. BMC Microbiology. 11(1). 8–8. 20 indexed citations
16.
Huergo, Luciano F., Leonardo M. Cruz, Rose Adele Monteiro, et al.. (2010). Proteomic analysis of Herbaspirillum seropedicae reveals ammonium-induced AmtB-dependent membrane sequestration of PII proteins. FEMS Microbiology Letters. 308(1). 40–47. 19 indexed citations
17.
Huergo, Luciano F., Mike Merrick, Fábio O. Pedrosa, et al.. (2007). Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria. Molecular Microbiology. 66(6). 1523–1535. 45 indexed citations
18.
Wassem, Roseli, et al.. (2002). Control of autogenous activation ofHerbaspirillum seropedicae nifApromoter by the IHF protein. FEMS Microbiology Letters. 212(2). 177–192. 13 indexed citations
19.
Kim, Joon, et al.. (1995). Implication of Mammalian Ribosomal Protein S3 in the Processing of DNA Damage. Journal of Biological Chemistry. 270(23). 13620–13629. 171 indexed citations
20.
Martins, Elizabeth A. L., Leda S. Chubatsu, & Rogério Meneghini. (1991). Role of antioxidants in protecting cellular DNA from damage by oxidative stress. Mutation research. Fundamental and molecular mechanisms of mutagenesis. 250(1-2). 95–101. 47 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026