L.E.S. Netto

1.4k total citations
17 papers, 361 citations indexed

About

L.E.S. Netto is a scholar working on Molecular Biology, Cell Biology and Biochemistry. According to data from OpenAlex, L.E.S. Netto has authored 17 papers receiving a total of 361 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 5 papers in Cell Biology and 4 papers in Biochemistry. Recurrent topics in L.E.S. Netto's work include Redox biology and oxidative stress (9 papers), Endoplasmic Reticulum Stress and Disease (5 papers) and Sulfur Compounds in Biology (4 papers). L.E.S. Netto is often cited by papers focused on Redox biology and oxidative stress (9 papers), Endoplasmic Reticulum Stress and Disease (5 papers) and Sulfur Compounds in Biology (4 papers). L.E.S. Netto collaborates with scholars based in Brazil, Germany and United States. L.E.S. Netto's co-authors include Alicia J. Kowaltowski, Anı́bal E. Vercesi, Sue Goo Rhee, Ohára Augusto, Gisele Monteiro, Roger F. Castilho, Fernando José Zara, Marcos Antônio de Oliveira, Mário H. Barros and Carlos A. Tairum and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and FEBS Letters.

In The Last Decade

L.E.S. Netto

17 papers receiving 357 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L.E.S. Netto Brazil 10 262 48 41 35 32 17 361
Kristen A. Jeffries United States 10 258 1.0× 49 1.0× 46 1.1× 33 0.9× 12 0.4× 12 353
Irina Gostimskaya United Kingdom 10 397 1.5× 43 0.9× 63 1.5× 45 1.3× 17 0.5× 12 485
Maria Novichkova Russia 9 227 0.9× 54 1.1× 13 0.3× 43 1.2× 30 0.9× 21 407
Caroline Noyon Belgium 9 230 0.9× 37 0.8× 28 0.7× 60 1.7× 32 1.0× 13 438
Hyuck Jun Mok South Korea 11 327 1.2× 39 0.8× 49 1.2× 45 1.3× 26 0.8× 13 488
Weigang Huang United States 14 243 0.9× 17 0.4× 58 1.4× 39 1.1× 16 0.5× 26 465
Shahana Sharmin Japan 6 249 1.0× 143 3.0× 43 1.0× 38 1.1× 22 0.7× 7 398
Emma J. Collinson Australia 9 440 1.7× 44 0.9× 66 1.6× 13 0.4× 43 1.3× 9 547
Peter A. Glascott United States 10 288 1.1× 24 0.5× 37 0.9× 50 1.4× 54 1.7× 11 512
Hans Jörnvall Sweden 12 239 0.9× 49 1.0× 91 2.2× 33 0.9× 17 0.5× 16 436

Countries citing papers authored by L.E.S. Netto

Since Specialization
Citations

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

Fields of papers citing papers by L.E.S. Netto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by L.E.S. Netto. 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 L.E.S. Netto. The network helps show where L.E.S. Netto may publish in the future.

Co-authorship network of co-authors of L.E.S. Netto

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

All Works

17 of 17 papers shown
1.
Inague, Alex, Zhiyi Chen, Thamara Nishida Xavier da Silva, et al.. (2023). A Non-canonical Activity of Peroxiredoxin 6 Protects Cells from Lipid Peroxidation and Ferroptosis. Free Radical Biology and Medicine. 208. S124–S124. 1 indexed citations
2.
Palma, Flávio R., et al.. (2022). Absence of Gem1 (mammalian Miro/Rhot) mitigates alpha-synuclein toxicity in a yeast model of Parkinson's disease. Molecular and Cellular Neuroscience. 122. 103757–103757. 3 indexed citations
3.
Gomes, Fernando, Thiago Gerônimo Pires Alegria, L.E.S. Netto, et al.. (2021). Coq3p relevant residues for protein activity and stability. FEMS Yeast Research. 21(7). 2 indexed citations
4.
Wittig, Ilka, Brandon Schickling, Christoph Schürmann, et al.. (2019). Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47 phox in Vascular Smooth Muscle Cells. Arteriosclerosis Thrombosis and Vascular Biology. 39(2). 224–236. 29 indexed citations
5.
Truzzi, Daniela R., Fernando Rodrigues Coelho, Verônica Paviani, et al.. (2018). Bicarbonate increases peroxiredoxin 1 susceptibility to hyperoxidation. Free Radical Biology and Medicine. 120. S37–S37. 1 indexed citations
6.
Carvalho, Larissa Anastácio da Costa, Daniela R. Truzzi, Simone Alves, et al.. (2017). Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2. Journal of Biological Chemistry. 292(21). 8705–8715. 47 indexed citations
7.
Gomes, Fernando, Ralf Lopes, Louise Cerdeira, et al.. (2017). Tn 6350 , a Novel Transposon Carrying Pyocin S8 Genes Encoding a Bacteriocin with Activity against Carbapenemase-Producing Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy. 61(5). 8 indexed citations
10.
Tairum, Carlos A., Marcos Antônio de Oliveira, Bruno Brasil Horta, Fernando José Zara, & L.E.S. Netto. (2012). Disulfide Biochemistry in 2-Cys Peroxiredoxin: Requirement of Glu50 and Arg146 for the Reduction of Yeast Tsa1 by Thioredoxin. Journal of Molecular Biology. 424(1-2). 28–41. 42 indexed citations
11.
Budu, Alexandre, Carlos A. H. Fernandes, Paloma Mieko Sato, et al.. (2010). In vivo uptake of a haem analogue Zn protoporphyrin IX by the human malaria parasite P. falciparum‐infected red blood cells. Cell Biology International. 34(8). 859–865. 14 indexed citations
12.
Medina‐Silva, Renata, Marcelo P. Barros, Rodrigo S. Galhardo, et al.. (2005). Heat stress promotes mitochondrial instability and oxidative responses in yeast deficient in thiazole biosynthesis. Research in Microbiology. 157(3). 275–281. 35 indexed citations
13.
Monteiro, Gisele, Alicia J. Kowaltowski, Mário H. Barros, & L.E.S. Netto. (2004). Glutathione and thioredoxin peroxidases mediate susceptibility of yeast mitochondria to Ca2+-induced damage. Archives of Biochemistry and Biophysics. 425(1). 14–24. 32 indexed citations
14.
Netto, L.E.S., Alicia J. Kowaltowski, Roger F. Castilho, & Anı́bal E. Vercesi. (2002). [25] Thiol enzymes protecting mitochondria against oxidative damage. Methods in enzymology on CD-ROM/Methods in enzymology. 348. 260–270. 38 indexed citations
15.
Kowaltowski, Alicia J., Anı́bal E. Vercesi, Sue Goo Rhee, & L.E.S. Netto. (2000). Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against Ca2+‐induced mitochondrial membrane permeabilization and cell death. FEBS Letters. 473(2). 177–182. 60 indexed citations
16.
Netto, L.E.S., N. V. S. Ramakrishna, Carol Kolar, et al.. (1992). Identification of C8-methylguanine in the hydrolysates of DNA from rats administered 1,2-dimethylhydrazine. Evidence for in vivo DNA alkylation by methyl radicals.. Journal of Biological Chemistry. 267(30). 21524–21527. 26 indexed citations
17.
Augusto, Ohára, et al.. (1992). DNA alkylation by carbon-centered radicals.. PubMed. 25(12). 1171–83. 2 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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