D.P. Barondeau

3.3k total citations · 1 hit paper
41 papers, 2.5k citations indexed

About

D.P. Barondeau is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Cellular and Molecular Neuroscience. According to data from OpenAlex, D.P. Barondeau has authored 41 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 19 papers in Renewable Energy, Sustainability and the Environment and 12 papers in Cellular and Molecular Neuroscience. Recurrent topics in D.P. Barondeau's work include Metalloenzymes and iron-sulfur proteins (18 papers), Mitochondrial Function and Pathology (10 papers) and Genetic Neurodegenerative Diseases (8 papers). D.P. Barondeau is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (18 papers), Mitochondrial Function and Pathology (10 papers) and Genetic Neurodegenerative Diseases (8 papers). D.P. Barondeau collaborates with scholars based in United States, Germany and New Zealand. D.P. Barondeau's co-authors include Elizabeth D. Getzoff, John A. Tainer, C.J. Kassmann, Chi-Lin Tsai, Jennifer Bridwell‐Rabb, Paul A. Lindahl, Nicholas G. Fox, C.K. Bruns, Shachin Patra and Christopher D. Putnam and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

D.P. Barondeau

40 papers receiving 2.5k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

FDX1-dependent and independent mechanisms of elesclomol-mediated intracellular copper delivery

2023 88 citations Mohammad Zulkifli, Shivatheja Soma et al. Proceedings of the National Academy of Sciences profile →

Peers

D.P. Barondeau

RESE

CMN

Jeffrey N. Agar United States

Mark L. Paddock United States

Tony A. Mattioli France

Örjan Hansson Sweden

Rieko Yaono Japan

S.V. Antonyuk United Kingdom

Jonathan P. Hosler United States

Barry D. Howes Italy

Lothar Gremer Germany

Shigetoshi Aono Japan

Jeffrey N. Agar United States

D.P. Barondeau

2.3k ×1.4

1.1k ×1.5

RESE

357 ×0.7

CMN

324 ×0.9

265 ×0.8

Citations per year, relative to D.P. Barondeau D.P. Barondeau (= 1×) peers Jeffrey N. Agar

Countries citing papers authored by D.P. Barondeau

Since Specialization

Citations

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

Fields of papers citing papers by D.P. Barondeau

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by D.P. Barondeau. 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 D.P. Barondeau. The network helps show where D.P. Barondeau may publish in the future.

Co-authorship network of co-authors of D.P. Barondeau

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

All Works

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20 of 20 papers shown

Meisel, Joshua D., Pallavi R. Joshi, María Miranda, et al.. (2025). Mutations in mitochondrial ferredoxin FDX2 suppress frataxin deficiency. Nature. 649(8097). 713–720. 1 indexed citations

Patra, Shachin, et al.. (2025). Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe–S Cluster Biosynthesis. Biochemistry. 64(4). 903–916. 1 indexed citations

Barondeau, D.P., et al.. (2024). Fe-S cluster biosynthesis and maturation: Mass spectrometry-based methods advancing the field. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1871(7). 119784–119784.

Zulkifli, Mohammad, Shivatheja Soma, Si Chen, et al.. (2023). FDX1-dependent and independent mechanisms of elesclomol-mediated intracellular copper delivery. Proceedings of the National Academy of Sciences. 120(10). e2216722120–e2216722120. 88 indexed citations breakdown →

Das, Deepika Sharma, Shachin Patra, Jennifer Bridwell‐Rabb, & D.P. Barondeau. (2019). Mechanism of frataxin “bypass” in human iron–sulfur cluster biosynthesis with implications for Friedreich’s ataxia. Journal of Biological Chemistry. 294(23). 9276–9284. 19 indexed citations

Ast, Tslil, Joshua D. Meisel, Shachin Patra, et al.. (2019). Hypoxia Rescues Frataxin Loss by Restoring Iron Sulfur Cluster Biogenesis. Cell. 177(6). 1507–1521.e16. 97 indexed citations

Patra, Shachin & D.P. Barondeau. (2019). Mechanism of activation of the human cysteine desulfurase complex by frataxin. Proceedings of the National Academy of Sciences. 116(39). 19421–19430. 67 indexed citations

Cory, Suzanne, Jonathan G. Van Vranken, Edward J. Brignole, et al.. (2017). Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP–ISD11 interactions. Proceedings of the National Academy of Sciences. 114(27). E5325–E5334. 121 indexed citations

Fox, Nicholas G., Deepika Sharma Das, Mrinmoy Chakrabarti, Paul A. Lindahl, & D.P. Barondeau. (2015). Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe–S Assembly Complex. Biochemistry. 54(25). 3880–3889. 60 indexed citations

10.

Bridwell‐Rabb, Jennifer, et al.. (2014). Human Frataxin Activates Fe–S Cluster Biosynthesis by Facilitating Sulfur Transfer Chemistry. Biochemistry. 53(30). 4904–4913. 126 indexed citations

11.

Tsai, Chi-Lin, Jennifer Bridwell‐Rabb, & D.P. Barondeau. (2011). Friedreich’s Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron–Sulfur Cluster Assembly Complex. Biochemistry. 50(29). 6478–6487. 49 indexed citations

12.

Tsai, Chi-Lin & D.P. Barondeau. (2010). Human Frataxin Is an Allosteric Switch That Activates the Fe−S Cluster Biosynthetic Complex. Biochemistry. 49(43). 9132–9139. 227 indexed citations

13.

Wood, Thammajun L., Jennifer Bridwell‐Rabb, Yong-Ick Kim, et al.. (2010). The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor. Proceedings of the National Academy of Sciences. 107(13). 5804–5809. 64 indexed citations

14.

Shin, David, Michael DiDonato, D.P. Barondeau, et al.. (2009). Superoxide Dismutase Structures, Stability, Mechanism and Insights into the Human Disease Amyotrophic Lateral Sclerosis from Eukaryotic Thermophile Alvinella pompejana. Journal of Molecular Biology. 385(5). 1534. 2 indexed citations

15.

Shin, David, Michael DiDonato, D.P. Barondeau, et al.. (2008). Superoxide Dismutase from the Eukaryotic Thermophile Alvinella pompejana: Structures, Stability, Mechanism, and Insights into Amyotrophic Lateral Sclerosis. Journal of Molecular Biology. 385(5). 1534–1555. 100 indexed citations

16.

Barondeau, D.P., John A. Tainer, & Elizabeth D. Getzoff. (2006). Structural Evidence for an Enolate Intermediate in GFP Fluorophore Biosynthesis. Journal of the American Chemical Society. 128(10). 3166–3168. 47 indexed citations

17.

Barondeau, D.P., et al.. (2005). Defining the Role of Arginine 96 in Green Fluorescent Protein Fluorophore Biosynthesis^,. Biochemistry. 44(49). 16211–16220. 58 indexed citations

18.

Barondeau, D.P. & Elizabeth D. Getzoff. (2004). Structural insights into protein–metal ion partnerships. Current Opinion in Structural Biology. 14(6). 765–774. 42 indexed citations

19.

Barondeau, D.P., Christopher D. Putnam, C.J. Kassmann, John A. Tainer, & Elizabeth D. Getzoff. (2003). Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proceedings of the National Academy of Sciences. 100(21). 12111–12116. 173 indexed citations

20.

Xia, Jinqiang, Mark E. Anderson, D.P. Barondeau, et al.. (1995). The nickel and iron-sulfur centers in carbon monoxide dehydrogenase. Journal of Inorganic Biochemistry. 59(2-3). 634–634. 1 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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