Sara E. Bari

1.2k total citations
45 papers, 913 citations indexed

About

Sara E. Bari is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Sara E. Bari has authored 45 papers receiving a total of 913 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 22 papers in Cell Biology and 12 papers in Physiology. Recurrent topics in Sara E. Bari's work include Hemoglobin structure and function (20 papers), Heme Oxygenase-1 and Carbon Monoxide (16 papers) and Nitric Oxide and Endothelin Effects (12 papers). Sara E. Bari is often cited by papers focused on Hemoglobin structure and function (20 papers), Heme Oxygenase-1 and Carbon Monoxide (16 papers) and Nitric Oxide and Endothelin Effects (12 papers). Sara E. Bari collaborates with scholars based in Argentina, Italy and Brazil. Sara E. Bari's co-authors include Darío A. Estrı́n, Fabio Doctorovich, Marcelo A. Martí, V. T. Amorebieta, Damián E. Bikiel, Leonardo Boechi, José A. Olabe, Juan Pellegrino, Benjamín Frydman and Julián Faivovich and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Sara E. Bari

43 papers receiving 896 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sara E. Bari Argentina 18 320 286 219 193 164 45 913
Juan López‐Garriga Puerto Rico 22 160 0.5× 846 3.0× 550 2.5× 176 0.9× 400 2.4× 69 1.6k
Andrew S. Dutton United States 16 488 1.5× 215 0.8× 62 0.3× 566 2.9× 224 1.4× 23 1.5k
A. Andrew Pacheco United States 21 108 0.3× 444 1.6× 101 0.5× 207 1.1× 127 0.8× 40 1.4k
Vandna Sharma United States 13 457 1.4× 538 1.9× 507 2.3× 97 0.5× 105 0.6× 27 1.1k
Susan E. Boggs United States 11 270 0.8× 238 0.8× 65 0.3× 135 0.7× 59 0.4× 14 786
A. R. BUTLER United Kingdom 15 366 1.1× 133 0.5× 66 0.3× 104 0.5× 144 0.9× 36 803
Alain Desbois France 21 101 0.3× 605 2.1× 464 2.1× 253 1.3× 23 0.1× 46 1.1k
Estelle M. Maes United States 13 139 0.4× 361 1.3× 292 1.3× 374 1.9× 20 0.1× 17 941
Colin R. Andrew United States 20 178 0.6× 675 2.4× 429 2.0× 215 1.1× 25 0.2× 45 1.1k
M.T. Wilson United Kingdom 18 349 1.1× 707 2.5× 354 1.6× 50 0.3× 89 0.5× 39 1.3k

Countries citing papers authored by Sara E. Bari

Since Specialization
Citations

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

Fields of papers citing papers by Sara E. Bari

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Sara E. Bari. 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 Sara E. Bari. The network helps show where Sara E. Bari may publish in the future.

Co-authorship network of co-authors of Sara E. Bari

This figure shows the co-authorship network connecting the top 25 collaborators of Sara E. Bari. A scholar is included among the top collaborators of Sara E. Bari 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 Sara E. Bari. Sara E. Bari 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.
Simone, Giovanna De, et al.. (2025). Mechanistic aspects of the binding of acid–base ligands to ferric heme proteins. Biophysical Reviews. 17(2). 293–300.
2.
Bari, Sara E., et al.. (2025). Coordination of inorganic disulfide species to ferric N-acetyl microperoxidase 11. Biochemical and Biophysical Research Communications. 748. 151319–151319. 1 indexed citations
3.
Bok, Marina, Gisela Marcoppido, Diego Franco, et al.. (2024). SARS-CoV-2 Specific Nanobodies Neutralize Different Variants of Concern and Reduce Virus Load in the Brain of h-ACE2 Transgenic Mice. Viruses. 16(2). 185–185. 2 indexed citations
4.
Murgida, Daniel H., et al.. (2023). Reduction of metmyoglobin by inorganic disulfide species. Journal of Inorganic Biochemistry. 245. 112256–112256. 5 indexed citations
5.
Murgida, Daniel H., et al.. (2023). Autocatalytic Mechanism in the Anaerobic Reduction of Metmyoglobin by Sulfide Species. Inorganic Chemistry. 62(29). 11304–11317. 2 indexed citations
6.
Estrı́n, Darío A., et al.. (2023). Binding mechanism of disulfide species to ferric hemeproteins: The case of metmyoglobin. Journal of Inorganic Biochemistry. 247. 112313–112313. 4 indexed citations
7.
Capece, Luciana, et al.. (2022). Computational evaluation of relevant species in inorganic sulfur biochemistry. Electronic Structure. 4(4). 44006–44006. 8 indexed citations
8.
Rouco, Santiago Oviedo, et al.. (2021). Reactivity of inorganic sulfide species towards a pentacoordinated heme model system. Journal of Inorganic Biochemistry. 220. 111459–111459. 1 indexed citations
9.
Bringas, Mauro, et al.. (2019). Hemeproteins as Targets for Sulfide Species. Antioxidants and Redox Signaling. 32(4). 247–257. 27 indexed citations
10.
Bari, Sara E., et al.. (2012). Reactivity of iron(II)-bound nitrosyl hydride (HNO, nitroxyl) in aqueous solution. Journal of Inorganic Biochemistry. 118. 108–114. 13 indexed citations
11.
Suárez, S., et al.. (2011). A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media. Journal of Inorganic Biochemistry. 105(8). 1044–1049. 16 indexed citations
12.
Amorebieta, V. T., Leonardo D. Slep, Federico Roncaroli, et al.. (2009). Three Redox States of Nitrosyl: NO+, NO., and NO−/HNO Interconvert Reversibly on the Same Pentacyanoferrate(II) Platform. Angewandte Chemie International Edition. 48(23). 4213–4216. 58 indexed citations
13.
Estrı́n, Darío A., et al.. (2008). Theoretical insight into the hydroxylamine oxidoreductase mechanism. Journal of Inorganic Biochemistry. 102(7). 1523–1530. 41 indexed citations
14.
Bikiel, Damián E., Sara E. Bari, Fabio Doctorovich, & Darío A. Estrı́n. (2007). DFT study on the reactivity of iron porphyrins tuned by ring substitution. Journal of Inorganic Biochemistry. 102(1). 70–76. 23 indexed citations
15.
Sáenz, Daniel A., et al.. (2007). Effect of nitroxyl on the hamster retinal nitridergic pathway. Neurochemistry International. 51(6-7). 424–432. 4 indexed citations
16.
Bermejo, Emilsé, et al.. (2005). Effect of nitroxyl on human platelets function. Thrombosis and Haemostasis. 94(9). 578–584. 49 indexed citations
17.
Bari, Sara E., et al.. (2003). On how the conformation of biliverdins influences their reduction to bilirubins: A biological and molecular modeling study. Bioorganic & Medicinal Chemistry. 11(21). 4661–4672. 4 indexed citations
18.
Fernández, Marcelo, Rosalía B. Frydman, Sara E. Bari, & Benjamín Frydman. (1992). Reconstitution of apomyoglobin with extended biliverdins. Biochemical and Biophysical Research Communications. 183(3). 1209–1215. 2 indexed citations
19.
Bari, Sara E., et al.. (1992). The interplay between basicity, conformation, and enzymatic reduction in biliverdins. Biochemical and Biophysical Research Communications. 188(1). 48–56. 8 indexed citations
20.
Frydman, Rosalía B., Sara E. Bari, Marı́a L. Tomaro, & Benjamín Frydman. (1990). The enzymatic and chemical reduction of extended biliverdins. Biochemical and Biophysical Research Communications. 171(1). 465–473. 10 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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