David M. Mueller

3.9k total citations · 1 hit paper
63 papers, 3.1k citations indexed

About

David M. Mueller is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Physical and Theoretical Chemistry. According to data from OpenAlex, David M. Mueller has authored 63 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 55 papers in Molecular Biology, 14 papers in Renewable Energy, Sustainability and the Environment and 4 papers in Physical and Theoretical Chemistry. Recurrent topics in David M. Mueller's work include ATP Synthase and ATPases Research (40 papers), Mitochondrial Function and Pathology (38 papers) and Metalloenzymes and iron-sulfur proteins (14 papers). David M. Mueller is often cited by papers focused on ATP Synthase and ATPases Research (40 papers), Mitochondrial Function and Pathology (38 papers) and Metalloenzymes and iron-sulfur proteins (14 papers). David M. Mueller collaborates with scholars based in United States, United Kingdom and France. David M. Mueller's co-authors include J. Symerský, Jacques Vaillier, Jean Velours, Vincent Soubannier, Patrick Paumard, Jean‐Paul di Rago, Jacques Schaëffer, Daniel Brèthes, Anurag P. Srivastava and D. Eric Walters and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

David M. Mueller

63 papers receiving 3.0k 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.

The ATP synthase is involved in generating mitochondrial cristae morphology

2002 638 citations David M. Mueller et al. profile →

Peers

David M. Mueller

IMMUN

PHYSI

M. Sundström Sweden

Brian H. Shilton Canada

Aviva Lapidot Israel

Bettina Sarg Austria

Tatyana Sandalova Sweden

Andrea Bernini Italy

G. Schatz United States

Christie G. Brouillette United States

Andrea Spitaleri Italy

Christian A. Olsen Denmark

M. Sundström Sweden

David M. Mueller

2.4k ×0.9

300 ×1.0

296 ×1.1

IMMUN

77 ×0.4

PHYSI

119 ×0.7

Citations per year, relative to David M. Mueller David M. Mueller (= 1×) peers M. Sundström

Countries citing papers authored by David M. Mueller

Since Specialization

Citations

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

Fields of papers citing papers by David M. Mueller

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David M. Mueller

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

Luo, Min, et al.. (2024). Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling. Nature Structural & Molecular Biology. 31(4). 657–666. 2 indexed citations

Chouhan, Surbhi, Cody Weimholt, Jingqin Luo, et al.. (2022). TNK2/ACK1-mediated phosphorylation of ATP5F1A (ATP synthase F1 subunit alpha) selectively augments survival of prostate cancer while engendering mitochondrial vulnerability. Autophagy. 19(3). 1000–1025. 34 indexed citations

Luo, Min, Wenchang Zhou, Hiral Patel, et al.. (2020). Bedaquiline inhibits the yeast and human mitochondrial ATP synthases. Communications Biology. 3(1). 452–452. 40 indexed citations

Narsaria, Utkarsh, Srijita Basak, Debashrito Deb, et al.. (2020). A candidate multi-epitope vaccine against SARS-CoV-2. Scientific Reports. 10(1). 10895–10895. 261 indexed citations

Srivastava, Anurag P., Min Luo, Wenchang Zhou, et al.. (2018). High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Science. 360(6389). 155 indexed citations

Strauß, Harald, Jagat Narula, Renu Virmani, et al.. (2013). Theragnostic potential of Sn-117m for the molecular targeting and therapy of vulnerable plaque. 54. 461. 3 indexed citations

Symerský, J., et al.. (2012). Oligomycin frames a common drug-binding site in the ATP synthase. Proceedings of the National Academy of Sciences. 109(35). 13961–13965. 204 indexed citations

Symerský, J., Vijayakanth Pagadala, Alexander Krah, et al.. (2012). Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Structural & Molecular Biology. 19(5). 485–491. 103 indexed citations

Pagadala, Vijayakanth, Luke Vistain, J. Symerský, & David M. Mueller. (2011). Characterization of the mitochondrial ATP synthase from yeast Saccharomyces cerevisae. Journal of Bioenergetics and Biomembranes. 43(4). 333–347. 11 indexed citations

10.

Little, Max A., Bradley C. Steel, Fan Bai, et al.. (2010). Steps and bumps: precision extraction of discrete states of molecular machines using physically-based, high-throughput time series analysis. arXiv (Cornell University). 21 indexed citations

11.

Notari, Luigi, et al.. (2010). Pigment epithelium‐derived factor binds to cell‐surface F₁‐ATP synthase. FEBS Journal. 277(9). 2192–2205. 50 indexed citations

12.

Symerský, J., et al.. (2010). Crystal Structures of Mutant Forms of the Yeast F1 ATPase Reveal Two Modes of Uncoupling. Journal of Biological Chemistry. 285(47). 36561–36569. 16 indexed citations

13.

Falson, Pierre, et al.. (2005). The Binding Mechanism of the Yeast F1-ATPase Inhibitory Peptide. Journal of Biological Chemistry. 280(11). 9927–9936. 18 indexed citations

14.

Xiao, Yan, Mark D. Metzl, & David M. Mueller. (2000). Partial Uncoupling of the Mitochondrial Membrane by a Heterozygous Null Mutation in the Gene Encoding the γ- or δ-Subunit of the Yeast Mitochondrial ATPase. Journal of Biological Chemistry. 275(10). 6963–6968. 21 indexed citations

15.

Mueller, David M.. (2000). Partial Assembly of the Yeast Mitochondrial ATP Synthase 1. Journal of Bioenergetics and Biomembranes. 32(4). 391–400. 33 indexed citations

16.

Mueller, David M., et al.. (1999). The Role of the Amino-Terminal β-Barrel Domain of the α and β Subunits in the Yeast F1-ATPase. Journal of Bioenergetics and Biomembranes. 31(2). 95–104. 4 indexed citations

17.

Sosa‐Peinado, Alejandro, et al.. (1996). Intragenic Suppressors of P-loop Mutations in the β-Subunit of the Mitochondrial ATPase in the Yeast Saccharomyces cerevisiae. Journal of Biological Chemistry. 271(20). 11844–11851. 4 indexed citations

18.

Mukhopadhyay, Arindam, et al.. (1994). Level of ATP synthase activity required for yeast Saccharomyces cerevisiae to grow on glycerol media. FEBS Letters. 343(2). 160–164. 40 indexed citations

19.

Davies, Joanna D., David M. Mueller, Darcy B. Wilson, & Daniel P. Gold. (1990). Nucleotide sequence of a eDNA encoding the rat T3 delta chain. Nucleic Acids Research. 18(15). 4617–4617. 6 indexed citations

20.

Mueller, David M.. (1989). Site directed mutagenesis of the β-subunit of the yeast mitochondrial ATPase. Biochemical and Biophysical Research Communications. 164(1). 381–386. 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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