Oscar Juárez

1.3k total citations
47 papers, 1.0k citations indexed

About

Oscar Juárez is a scholar working on Molecular Biology, Plant Science and Endocrinology. According to data from OpenAlex, Oscar Juárez has authored 47 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 10 papers in Plant Science and 9 papers in Endocrinology. Recurrent topics in Oscar Juárez's work include Photosynthetic Processes and Mechanisms (15 papers), Vibrio bacteria research studies (8 papers) and ATP Synthase and ATPases Research (7 papers). Oscar Juárez is often cited by papers focused on Photosynthetic Processes and Mechanisms (15 papers), Vibrio bacteria research studies (8 papers) and ATP Synthase and ATPases Research (7 papers). Oscar Juárez collaborates with scholars based in United States, France and Mexico. Oscar Juárez's co-authors include Blanca Barquera, Joel E. Morgan, Sara Rodríguez‐Enríquez, José S. Rodríguez‐Zavala, Rafael Moreno‐Sánchez, Karina Tuz, Adrián Reyes‐Prieto, Mark J. Nilges, Portia M. Gillespie and Juan Pablo Pardo 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

Oscar Juárez

45 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
Oscar Juárez United States 20 672 137 117 115 84 47 1.0k
Mark Shepherd United Kingdom 20 609 0.9× 63 0.5× 78 0.7× 83 0.7× 28 0.3× 48 969
Elamparithi Jayamani United States 17 743 1.1× 35 0.3× 41 0.4× 47 0.4× 142 1.7× 23 1.2k
George T. Rasmussen United States 14 385 0.6× 57 0.4× 95 0.8× 77 0.7× 17 0.2× 19 682
Lori J. Templeton United States 6 691 1.0× 120 0.9× 71 0.6× 349 3.0× 70 0.8× 8 1.4k
Jürgen Moser Germany 22 1.0k 1.6× 32 0.2× 96 0.8× 126 1.1× 44 0.5× 48 1.4k
Teresa Keng Canada 19 1.2k 1.8× 32 0.2× 171 1.5× 173 1.5× 26 0.3× 32 1.7k
Britta Søballe United Kingdom 10 684 1.0× 69 0.5× 77 0.7× 384 3.3× 21 0.3× 10 917
Deyu Zhu China 24 962 1.4× 110 0.8× 101 0.9× 103 0.9× 14 0.2× 72 1.6k
Irina A. Rodionova United States 22 883 1.3× 32 0.2× 118 1.0× 226 2.0× 72 0.9× 36 1.3k
Victor Chubukov United States 17 1.3k 1.9× 23 0.2× 71 0.6× 307 2.7× 26 0.3× 20 1.7k

Countries citing papers authored by Oscar Juárez

Since Specialization
Citations

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

Fields of papers citing papers by Oscar Juárez

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Oscar Juárez

This figure shows the co-authorship network connecting the top 25 collaborators of Oscar Juárez. A scholar is included among the top collaborators of Oscar Juárez 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 Oscar Juárez. Oscar Juárez 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.
Yuan, Ming, et al.. (2025). NQR as a target for new antibiotics. Frontiers in Microbiology. 16. 1690572–1690572.
2.
Tuz, Karina, et al.. (2025). Molecular Dynamics Analysis of Inhibitor Binding Interactions in the Vibrio cholerae Respiratory Complex NQR. Proteins Structure Function and Bioinformatics. 94(2). 649–659. 1 indexed citations
3.
Yuan, Ming, et al.. (2025). Repurposing clofazimine as an antibiotic to treat cholera: Identification of cellular and structural targets. Journal of Biological Chemistry. 301(8). 110458–110458. 1 indexed citations
4.
Yao, Qi, et al.. (2024). Alternative production of pro-death Bax∆2 protein via ribosomal frameshift in Alzheimer’s disease. Scientific Reports. 14(1). 27288–27288.
5.
6.
Choi, Brian, Armando Hernández-García, Alba Romero-Rodríguez, et al.. (2024). Discovery of antimicrobial peptides clostrisin and cellulosin from Clostridium: insights into their structures, co-localized biosynthetic gene clusters, and antibiotic activity. Beilstein Journal of Organic Chemistry. 20. 1800–1816. 1 indexed citations
7.
Li, Ye, Joelle K. Salazar, Yingshu He, et al.. (2020). Mechanisms of Salmonella Attachment and Survival on In-Shell Black Peppercorns, Almonds, and Hazelnuts. Frontiers in Microbiology. 11. 582202–582202. 4 indexed citations
8.
Yuan, Ming, et al.. (2019). Role of Subunit D in Ubiquinone-Binding Site of Vibrio cholerae NQR: Pocket Flexibility and Inhibitor Resistance. ACS Omega. 4(21). 19324–19331. 7 indexed citations
9.
Osipiuk, J., Srinivas Chakravarthy, Ming Yuan, et al.. (2019). Conserved residue His-257 of Vibrio cholerae flavin transferase ApbE plays a critical role in substrate binding and catalysis. Journal of Biological Chemistry. 294(37). 13800–13810. 10 indexed citations
10.
Rosas‐Lemus, Mónica, et al.. (2018). Characterization of the Pseudomonas aeruginosa NQR complex, a bacterial proton pump with roles in autopoisoning resistance. Journal of Biological Chemistry. 293(40). 15664–15677. 26 indexed citations
11.
Tuz, Karina, et al.. (2017). Identification of the Catalytic Ubiquinone-binding Site of Vibrio cholerae Sodium-dependent NADH Dehydrogenase. Journal of Biological Chemistry. 292(7). 3039–3048. 13 indexed citations
12.
Rosas‐Lemus, Mónica, et al.. (2017). Kinetic characterization of Vibrio cholerae ApbE: Substrate specificity and regulatory mechanisms. PLoS ONE. 12(10). e0186805–e0186805. 12 indexed citations
13.
Tuz, Karina, et al.. (2015). The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase. Journal of Biological Chemistry. 290(33). 20009–20021. 27 indexed citations
14.
15.
Shea, Michael, Oscar Juárez, Jonathan Cho, & Blanca Barquera. (2013). Aspartic Acid 397 in Subunit B of the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae Forms Part of a Sodium-binding Site, Is Involved in Cation Selectivity, and Affects Cation-binding Site Cooperativity. Journal of Biological Chemistry. 288(43). 31241–31249. 16 indexed citations
16.
Juárez, Oscar & Blanca Barquera. (2012). Insights into the mechanism of electron transfer and sodium translocation of the Na+-pumping NADH:quinone oxidoreductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(10). 1823–1832. 64 indexed citations
17.
Pardo, Juan Pablo, Oscar Juárez, Federico Martı́nez, et al.. (2011). Atypical Cristae Morphology of Human Syncytiotrophoblast Mitochondria. Journal of Biological Chemistry. 286(27). 23911–23919. 56 indexed citations
18.
Juárez, Oscar, Mark J. Nilges, Portia M. Gillespie, Jennifer L. Cotton, & Blanca Barquera. (2008). Riboflavin Is an Active Redox Cofactor in the Na+-pumping NADH:Quinone Oxidoreductase (Na+-NQR) from Vibrio cholerae. Journal of Biological Chemistry. 283(48). 33162–33167. 53 indexed citations
19.
Juárez, Oscar, et al.. (2006). The physiologic role of alternative oxidase in Ustilago maydis. FEBS Journal. 273(20). 4603–4615. 34 indexed citations
20.
Rodríguez‐Enríquez, Sara, Oscar Juárez, José S. Rodríguez‐Zavala, & Rafael Moreno‐Sánchez. (2001). Multisite control of the Crabtree effect in ascites hepatoma cells. European Journal of Biochemistry. 268(8). 2512–2519. 110 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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