David A. Stroud

8.2k total citations · 2 hit papers
70 papers, 4.7k citations indexed

About

David A. Stroud is a scholar working on Molecular Biology, Clinical Biochemistry and Cell Biology. According to data from OpenAlex, David A. Stroud has authored 70 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 64 papers in Molecular Biology, 18 papers in Clinical Biochemistry and 11 papers in Cell Biology. Recurrent topics in David A. Stroud's work include Mitochondrial Function and Pathology (55 papers), ATP Synthase and ATPases Research (31 papers) and Metabolism and Genetic Disorders (18 papers). David A. Stroud is often cited by papers focused on Mitochondrial Function and Pathology (55 papers), ATP Synthase and ATPases Research (31 papers) and Metabolism and Genetic Disorders (18 papers). David A. Stroud collaborates with scholars based in Australia, United States and Germany. David A. Stroud's co-authors include Michael T. Ryan, Luke E. Formosa, Diana Stojanovski, Agus Salim, Nikolaus Pfanner, Laura D. Osellame, Nils Wiedemann, David R. Thorburn, Marris G. Dibley and Thomas Becker and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David A. Stroud

65 papers receiving 4.6k 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.

FunRich: An open access standalone functional enrichment and interaction network analysis tool

2015 980 citations Agus Salim, David A. Stroud et al. profile →
Accessory subunits are integral for assembly and function of human mitochondrial complex I

2016 382 citations David A. Stroud, Elliot Surgenor et al. Nature profile →

Peers

David A. Stroud

PHYSI

PFM

Norie Araki Japan

Zhiyin Song China

Timothy Wai France

Teruhisa Tsuzuki Japan

Xin Pan China

Svend O. Freytag United States

Yushan Zhu China

Frédéric Catez France

Hubert de Verneuil France

Gregory S. Ducker United States

Norie Araki Japan

David A. Stroud

2.1k ×0.6

1.2k ×1.3

283 ×0.5

530 ×1.3

PHYSI

391 ×1.0

PFM

Citations per year, relative to David A. Stroud David A. Stroud (= 1×) peers Norie Araki

Countries citing papers authored by David A. Stroud

Since Specialization

Citations

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

Fields of papers citing papers by David A. Stroud

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David A. Stroud. 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 David A. Stroud. The network helps show where David A. Stroud may publish in the future.

Co-authorship network of co-authors of David A. Stroud

This figure shows the co-authorship network connecting the top 25 collaborators of David A. Stroud. A scholar is included among the top collaborators of David A. Stroud 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 David A. Stroud. David A. Stroud 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

Sacharz, Joanna, Ann E. Frazier, Shuai Nie, et al.. (2025). Complex II assembly drives metabolic adaptation to OXPHOS dysfunction. Science Advances. 11(33). eadr6012–eadr6012.

Botella, Javier, Enrico Perri, Nikeisha J. Caruana, et al.. (2025). Sprint interval exercise disrupts mitochondrial ultrastructure driving a unique mitochondrial stress response and remodelling in men. Nature Communications. 17(1). 71–71.

Bezawork‐Geleta, Ayenachew, Stacey N. Keenan, Jieqiong Lou, et al.. (2025). Proximity proteomics reveals a mechanism of fatty acid transfer at lipid droplet-mitochondria- endoplasmic reticulum contact sites. Nature Communications. 16(1). 2135–2135. 5 indexed citations

Larson, Austin, Naomi Meeks, Marisa W. Friederich, et al.. (2024). An integrated multi-omics approach allowed ultra-rapid diagnosis of a deep intronic pathogenic variant in PDHX and precision treatment in a neonate critically ill with lactic acidosis. Mitochondrion. 79. 101973–101973. 2 indexed citations

Hove, Johan L.K. Van, Marisa W. Friederich, Daniella H. Hock, et al.. (2024). ACAD9 treatment with bezafibrate and nicotinamide riboside temporarily stabilizes cardiomyopathy and lactic acidosis. Mitochondrion. 78. 101905–101905. 3 indexed citations

Botella, Javier, Cheng Huang, Ralf B. Schittenhelm, et al.. (2024). Fibre-specific mitochondrial protein abundance is linked to resting and post-training mitochondrial content in the muscle of men. Nature Communications. 15(1). 7677–7677. 9 indexed citations

Kulawiak, Bogusz, et al.. (2023). Loss of the large conductance calcium-activated potassium channel causes an increase in mitochondrial reactive oxygen species in glioblastoma cells. Pflügers Archiv - European Journal of Physiology. 475(9). 1045–1060. 8 indexed citations

Hernández‐Camacho, Juan Diego, Thomas Cokelaer, Thibault Chaze, et al.. (2023). Mtfp1 ablation enhances mitochondrial respiration and protects against hepatic steatosis. Nature Communications. 14(1). 8474–8474. 16 indexed citations

Healy, Michael D., Joanna Sacharz, Kerrie E. McNally, et al.. (2022). Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins. Structure. 30(12). 1590–1602.e6. 6 indexed citations

10.

Liang, Chao, Shan Zhang, Rebecca J. Wilson, et al.. (2022). Mitochondrial microproteins link metabolic cues to respiratory chain biogenesis. Cell Reports. 40(7). 111204–111204. 26 indexed citations

11.

Formosa, Luke E., Boris Reljić, Alice J. Sharpe, et al.. (2021). Optic atrophy–associated TMEM126A is an assembly factor for the ND4-module of mitochondrial complex I. Proceedings of the National Academy of Sciences. 118(17). 20 indexed citations

12.

Lee, Cheryl, Sonia Chothani, Shan Zhang, et al.. (2021). Coding and non-coding roles of MOCCI (C15ORF48) coordinate to regulate host inflammation and immunity. Nature Communications. 12(1). 2130–2130. 64 indexed citations

13.

Bergen, Nicole J. Van, Syed Mukhtar Ahmed, Felicity Collins, et al.. (2020). Mutations in the exocyst component EXOC2 cause severe defects in human brain development. The Journal of Experimental Medicine. 217(10). 19 indexed citations

14.

Formosa, Luke E., Linden Muellner-Wong, Boris Reljić, et al.. (2020). Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly Complex Factors in the Biogenesis of Complex I. Cell Reports. 31(3). 107541–107541. 75 indexed citations

15.

Lake, Nicole J., Luke E. Formosa, David A. Stroud, et al.. (2019). A patient with homozygous nonsense variants in two Leigh syndrome disease genes: Distinguishing a dual diagnosis from a hypomorphic protein‐truncating variant. Human Mutation. 40(7). 893–898. 7 indexed citations

16.

Lindau, Caroline, Christophe Wirth, Jian Qiu, et al.. (2018). Membrane protein insertion through a mitochondrial β-barrel gate. Science. 359(6373). 109 indexed citations

17.

Stroud, David A., Elliot Surgenor, Luke E. Formosa, et al.. (2016). Accessory subunits are integral for assembly and function of human mitochondrial complex I. Nature. 538(7623). 123–126. 382 indexed citations breakdown →

18.

Bohnert, Maria, Ralf M. Zerbes, Susanne E. Horvath, et al.. (2012). Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane. Molecular Biology of the Cell. 23(20). 3948–3956. 103 indexed citations

19.

Gebert, Natalia, Amit Joshi, Stephan Kutik, et al.. (2009). Mitochondrial Cardiolipin Involved in Outer-Membrane Protein Biogenesis: Implications for Barth Syndrome. Current Biology. 19(24). 2133–2139. 197 indexed citations

20.

Baker, Michael J., Chaille T. Webb, David A. Stroud, et al.. (2008). Structural and Functional Requirements for Activity of the Tim9–Tim10 Complex in Mitochondrial Protein Import. Molecular Biology of the Cell. 20(3). 769–779. 52 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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