Douglas C. Rees

35.7k total citations · 14 hit papers
231 papers, 27.2k citations indexed

About

Douglas C. Rees is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Inorganic Chemistry. According to data from OpenAlex, Douglas C. Rees has authored 231 papers receiving a total of 27.2k indexed citations (citations by other indexed papers that have themselves been cited), including 129 papers in Molecular Biology, 76 papers in Renewable Energy, Sustainability and the Environment and 46 papers in Inorganic Chemistry. Recurrent topics in Douglas C. Rees's work include Metalloenzymes and iron-sulfur proteins (73 papers), Metal-Catalyzed Oxygenation Mechanisms (42 papers) and Electrocatalysts for Energy Conversion (27 papers). Douglas C. Rees is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (73 papers), Metal-Catalyzed Oxygenation Mechanisms (42 papers) and Electrocatalysts for Energy Conversion (27 papers). Douglas C. Rees collaborates with scholars based in United States, Germany and France. Douglas C. Rees's co-authors include James B. Howard, G. Fehér, Jongsun Kim, Oliver Einsle, Allen T. Lee, James P. Allen, H. Komiya, Oded Lewinson, Kaspar P. Locher and Eric F. Johnson and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Douglas C. Rees

227 papers receiving 26.6k citations

Hit Papers

ABC transporters: the power to change 1987 2026 2000 2013 2009 2002 1996 2002 1998 250 500 750 1000
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.

  1. ABC transporters: the power to change
    2009 1.1k citations Douglas C. Rees, Eric F. Johnson et al. profile →
  2. Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor
    2002 875 citations Oliver Einsle, F. Akif Tezcan et al. Science profile →
  3. Structural Basis of Biological Nitrogen Fixation
    1996 866 citations James B. Howard, Douglas C. Rees profile →
  4. The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism
    2002 857 citations Kaspar P. Locher, Allen T. Lee et al. Science profile →
  5. Structure of the MscL Homolog from Mycobacterium tuberculosis : A Gated Mechanosensitive Ion Channel
    1998 820 citations Allen T. Lee, Douglas C. Rees et al. Science profile →
  6. Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor
    2011 728 citations Thomas Spatzal, Susana L. A. Andrade et al. Science profile →
  7. Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors.
    1987 685 citations Douglas C. Rees et al. Proceedings of the National Academy of Sciences profile →
  8. Heparin Structure and Interactions with Basic Fibroblast Growth Factor
    1996 673 citations Douglas C. Rees et al. Science profile →
  9. Structural basis of biological nitrogen fixation
    2005 673 citations Douglas C. Rees, F. Akif Tezcan et al. Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences profile →
  10. Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer
    1997 610 citations Michael H. B. Stowell, Douglas C. Rees et al. Science profile →
  11. Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein
    1992 605 citations Douglas C. Rees et al. Science profile →
  12. Structure and function of bacterial photosynthetic reaction centres
    1989 602 citations Douglas C. Rees et al. profile →
  13. Crystallographic Structure of the Nitrogenase Iron Protein from Azotobacter vinelandii
    1992 507 citations Douglas C. Rees et al. Science profile →
  14. Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii
    1992 460 citations Douglas C. Rees et al. profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Douglas C. Rees United States 81 13.8k 9.5k 5.0k 4.6k 3.4k 231 27.2k
Brian M. Hoffman United States 85 9.2k 0.7× 11.4k 1.2× 11.8k 2.4× 9.9k 2.2× 2.5k 0.7× 694 33.1k
Keith O. Hodgson United States 83 5.5k 0.4× 5.6k 0.6× 8.5k 1.7× 10.1k 2.2× 4.5k 1.3× 418 25.7k
Wolfgang Lubitz Germany 81 9.9k 0.7× 12.8k 1.4× 6.5k 1.3× 5.2k 1.1× 1.2k 0.3× 477 26.2k
Michael W. W. Adams United States 82 12.9k 0.9× 7.8k 0.8× 5.1k 1.0× 3.4k 0.7× 1.2k 0.4× 491 24.2k
Harry B. Gray United States 112 11.8k 0.9× 14.1k 1.5× 18.7k 3.7× 12.4k 2.7× 7.5k 2.2× 850 53.1k
Edward I. Solomon United States 120 13.7k 1.0× 9.5k 1.0× 20.5k 4.1× 30.0k 6.5× 15.1k 4.4× 726 59.1k
James Barber United Kingdom 92 18.2k 1.3× 11.8k 1.2× 7.0k 1.4× 2.2k 0.5× 1.6k 0.5× 459 34.9k
Dennis R. Dean United States 75 5.1k 0.4× 13.1k 1.4× 3.5k 0.7× 3.5k 0.8× 628 0.2× 228 17.9k
Eric Oldfield United States 82 11.4k 0.8× 1.6k 0.2× 6.1k 1.2× 2.2k 0.5× 1.8k 0.5× 435 25.2k
Philip J. Stephens United States 77 8.9k 0.6× 2.0k 0.2× 6.9k 1.4× 4.6k 1.0× 7.4k 2.2× 346 41.0k

Countries citing papers authored by Douglas C. Rees

Since Specialization
Citations

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

Fields of papers citing papers by Douglas C. Rees

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Douglas C. Rees. 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 Douglas C. Rees. The network helps show where Douglas C. Rees may publish in the future.

Co-authorship network of co-authors of Douglas C. Rees

This figure shows the co-authorship network connecting the top 25 collaborators of Douglas C. Rees. A scholar is included among the top collaborators of Douglas C. Rees 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 Douglas C. Rees. Douglas C. Rees 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.
Stemmler, Timothy L., et al.. (2025). Nucleotide- and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA. Proceedings of the National Academy of Sciences. 122(35). e2506440122–e2506440122.
2.
Rees, Douglas C., et al.. (2024). The nitrogenase mechanism: new roles for the dangler?. JBIC Journal of Biological Inorganic Chemistry. 30(2). 125–133. 1 indexed citations
3.
Rees, Douglas C., et al.. (2023). Nitrogenase beyond the Resting State: A Structural Perspective. Molecules. 28(24). 7952–7952. 12 indexed citations
4.
Henthorn, Justin T., Sergey Koroidov, Thomas Kröll, et al.. (2019). Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-Edge High Resolution X-ray Absorption Spectroscopy. Journal of the American Chemical Society. 141(34). 13676–13688. 58 indexed citations
5.
Herrera, Nadia, Grigory Maksaev, Elizabeth S. Haswell, & Douglas C. Rees. (2018). Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance. Scientific Reports. 8(1). 14566–14566. 7 indexed citations
6.
Spatzal, Thomas, Kathryn Perez, Oliver Einsle, James B. Howard, & Douglas C. Rees. (2014). Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science. 345(6204). 1620–1623. 343 indexed citations
7.
Yang, Janet G., et al.. (2014). Structural Basis for Heavy Metal Detoxification by an Atm1-Type ABC Exporter. Science. 343(6175). 1133–1136. 136 indexed citations
8.
Basta, Tamara, Mary Morphew, Nilanjan Ghosh, et al.. (2013). Self-assembled lipid and membrane protein polyhedral nanoparticles. Proceedings of the National Academy of Sciences. 111(2). 670–674. 13 indexed citations
9.
Lewinson, Oded, Allen T. Lee, & Douglas C. Rees. (2009). A P-type ATPase importer that discriminates between essential and toxic transition metals. Proceedings of the National Academy of Sciences. 106(12). 4677–4682. 78 indexed citations
10.
Kaiser, Jens T., et al.. (2008). The High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation. Science. 321(5886). 250–253. 178 indexed citations
11.
Pinkett, Heather W., et al.. (2006). An Inward-Facing Conformation of a Putative Metal-Chelate-Type ABC Transporter. Science. 315(5810). 373–377. 228 indexed citations
12.
Rees, Douglas C., F. Akif Tezcan, Chad Haynes, et al.. (2005). Structural basis of biological nitrogen fixation. Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences. 363(1829). 971–984. 673 indexed citations breakdown →
13.
Corbett, Mary C., F. Akif Tezcan, Oliver Einsle, et al.. (2004). MoK- andL-edge X-ray absorption spectroscopic study of the ADP·AlF4−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal. Journal of Synchrotron Radiation. 12(1). 28–34. 11 indexed citations
14.
Rees, Douglas C., et al.. (2003). Structure of BtuCD, the ABC transporter for Vitamin B12. The FASEB Journal. 17. 7482. 1 indexed citations
15.
Borths, Elizabeth L., Kaspar P. Locher, Allen T. Lee, & Douglas C. Rees. (2002). The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proceedings of the National Academy of Sciences. 99(26). 16642–16647. 169 indexed citations
16.
Locher, Kaspar P., Allen T. Lee, & Douglas C. Rees. (2002). The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism. Science. 296(5570). 1091–1098. 857 indexed citations breakdown →
17.
Bass, Randal B., et al.. (2002). Crystal Structure of Escherichia coli MscS, a Voltage-Modulated and Mechanosensitive Channel. Science. 298(5598). 1582–1587. 465 indexed citations
18.
Schlessman, J.L., et al.. (1998). Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum. Journal of Molecular Biology. 280(4). 669–685. 118 indexed citations
19.
Stowell, Michael H. B., S. Michael Soltis, Caroline Kisker, et al.. (1996). A simple device for studying macromolecular crystals under moderate gas pressures (0.1–10 MPa). Journal of Applied Crystallography. 29(5). 608–613. 21 indexed citations
20.
Howard, James B. & Douglas C. Rees. (1994). NITROGENASE: A Nucleotide-Dependent Molecular Switch. Annual Review of Biochemistry. 63(1). 235–264. 169 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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