Susan Bailey

1.3k total citations
20 papers, 1.1k citations indexed

About

Susan Bailey is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Inorganic Chemistry. According to data from OpenAlex, Susan Bailey has authored 20 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 11 papers in Renewable Energy, Sustainability and the Environment and 9 papers in Inorganic Chemistry. Recurrent topics in Susan Bailey's work include Metalloenzymes and iron-sulfur proteins (11 papers), Metal-Catalyzed Oxygenation Mechanisms (8 papers) and Enzyme Structure and Function (5 papers). Susan Bailey is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (11 papers), Metal-Catalyzed Oxygenation Mechanisms (8 papers) and Enzyme Structure and Function (5 papers). Susan Bailey collaborates with scholars based in United Kingdom, Australia and United States. Susan Bailey's co-authors include Ulrike Kappler, Peter F. Lindley, S.S. Hasnain, Robert W. Evans, B. Gorinsky, Richard Charles Garratt, Harren Jhoti, William N. Hunter, Alan H. Fairlamb and Brian Bennett and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Susan Bailey

19 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Susan Bailey United Kingdom 14 403 376 243 143 130 20 1.1k
Lydie Martin France 25 599 1.5× 918 2.4× 275 1.1× 59 0.4× 116 0.9× 47 1.9k
Yves Pétillot France 19 513 1.3× 234 0.6× 170 0.7× 55 0.4× 69 0.5× 35 1.0k
Lilian Jacquamet France 25 680 1.7× 176 0.5× 255 1.0× 334 2.3× 196 1.5× 35 1.7k
Michael D. Sintchak United States 17 1.2k 3.1× 208 0.6× 179 0.7× 67 0.5× 258 2.0× 19 1.7k
Sofia Macedo Portugal 15 680 1.7× 82 0.2× 193 0.8× 73 0.5× 113 0.9× 31 1.6k
E Pontis Sweden 17 888 2.2× 257 0.7× 440 1.8× 32 0.2× 165 1.3× 23 1.2k
R. Kiefersauer Germany 10 751 1.9× 229 0.6× 135 0.6× 34 0.2× 358 2.8× 21 1.4k
Angelo Gallo Italy 18 1.1k 2.6× 298 0.8× 139 0.6× 212 1.5× 64 0.5× 42 1.6k
Luca Signor France 21 773 1.9× 140 0.4× 69 0.3× 65 0.5× 77 0.6× 46 1.3k
David Lemaire France 20 596 1.5× 55 0.1× 173 0.7× 146 1.0× 83 0.6× 42 1.3k

Countries citing papers authored by Susan Bailey

Since Specialization
Citations

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

Fields of papers citing papers by Susan Bailey

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Susan Bailey. 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 Susan Bailey. The network helps show where Susan Bailey may publish in the future.

Co-authorship network of co-authors of Susan Bailey

This figure shows the co-authorship network connecting the top 25 collaborators of Susan Bailey. A scholar is included among the top collaborators of Susan Bailey 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 Susan Bailey. Susan Bailey 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.
Bailey, Susan, Trevor D. Rapson, Kayunta Johnson‐Winters, et al.. (2008). Molecular Basis for Enzymatic Sulfite Oxidation. Journal of Biological Chemistry. 284(4). 2053–2063. 29 indexed citations
2.
Bailey, Susan, et al.. (2006). Agrobacterium tumefaciens VirB8 structure reveals potential protein–protein interaction sites. Proceedings of the National Academy of Sciences. 103(8). 2582–2587. 64 indexed citations
3.
Kappler, Ulrike, Susan Bailey, Changjian Feng, et al.. (2006). Kinetic and Structural Evidence for the Importance of Tyr236 for the Integrity of the Mo Active Site in a Bacterial Sulfite Dehydrogenase. Biochemistry. 45(32). 9696–9705. 38 indexed citations
4.
5.
Kappler, Ulrike & Susan Bailey. (2004). Crystallization and preliminary X-ray analysis of sulfite dehydrogenase fromStarkeya novella. Acta Crystallographica Section D Biological Crystallography. 60(11). 2070–2072. 9 indexed citations
6.
Hagedoorn, Peter‐Leon, Wilfred R. Hagen, Elizabeth Stewart, et al.. (2003). Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus. FEBS Letters. 555(3). 606–610. 25 indexed citations
7.
Macedo, Sofia, Célia V. Romão, R. Coelho, et al.. (2002). Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 Å resolution using synchrotron radiation. JBIC Journal of Biological Inorganic Chemistry. 7(4-5). 514–525. 27 indexed citations
8.
Stewart, Elizabeth, et al.. (2001). In Vivo Oxo Transfer: Reactions of Native and W-Substituted Dimethyl Sulfoxide Reductase Monitored by 1H NMR Spectroscopy. ChemBioChem. 2(9). 703–706. 7 indexed citations
9.
Bray, Robert C., Benjamin Adams, Andrew Smith, et al.. (2001). Reactions of Dimethylsulfoxide Reductase in the Presence of Dimethyl Sulfide and the Structure of the Dimethyl Sulfide-Modified Enzyme,. Biochemistry. 40(33). 9810–9820. 31 indexed citations
10.
Stewart, Elizabeth, Susan Bailey, Brian Bennett, et al.. (2000). Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site 1 1Edited by P. E. Wright. Journal of Molecular Biology. 299(3). 593–600. 76 indexed citations
11.
Bray, Robert C., Benjamin Adams, Andrew Smith, Brian Bennett, & Susan Bailey. (2000). Reversible Dissociation of Thiolate Ligands from Molybdenum in an Enzyme of the Dimethyl Sulfoxide Reductase Family,. Biochemistry. 39(37). 11258–11269. 64 indexed citations
12.
Adams, Benjamin, Andrew Smith, Susan Bailey, Alastair G. McEwan, & Robert C. Bray. (1999). Reactions of Dimethylsulfoxide Reductase from Rhodobacter capsulatus with Dimethyl Sulfide and with Dimethyl Sulfoxide:  Complexities Revealed by Conventional and Stopped-Flow Spectrophotometry. Biochemistry. 38(26). 8501–8511. 32 indexed citations
13.
Arendsen, Alexander F., Jonathan M. Hadden, G.L. Card, et al.. (1998). The "prismane" protein resolved: X-ray structure at 1.7 Å and multiple spectroscopy of two novel 4Fe clusters. JBIC Journal of Biological Inorganic Chemistry. 3(1). 81–95. 50 indexed citations
14.
Zhang, Yihong, Charles S. Bond, Susan Bailey, et al.. (1996). The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 Å resolution. Protein Science. 5(1). 52–61. 87 indexed citations
15.
Bailey, Susan, et al.. (1994). Crystallization and Preliminary X-ray Analysis of C-reactive Protein from Rat. Journal of Molecular Biology. 235(2). 767–771. 4 indexed citations
16.
Zhang, Yihong, Susan Bailey, James H. Naismith, et al.. (1993). Trypanosoma cruzi Trypanothione Reductase Crystallization, Unit Cell Dimensions and Structure Solution. Journal of Molecular Biology. 232(4). 1217–1220. 7 indexed citations
17.
Naismith, James H., Joseph D. Ferrara, Susan Bailey, et al.. (1992). Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase. Journal of Molecular Biology. 225(4). 1137–1141. 13 indexed citations
18.
Hunter, William N., Susan Bailey, J. Habash, et al.. (1992). Active site of trypanothione reductase. Journal of Molecular Biology. 227(1). 322–333. 107 indexed citations
19.
Bailey, Susan, Robert W. Evans, Richard Charles Garratt, et al.. (1988). Molecular structure of serum transferrin at 3.3-.ANG. resolution. Biochemistry. 27(15). 5804–5812. 319 indexed citations
20.
Lindley, Peter F., Susan Bailey, Robert W. Evans, et al.. (1986). Transferrin: a study of the iron-binding sites using extended X-ray absorption fine structure and anomalous dispersion techniques. Biochemical Society Transactions. 14(3). 542–545. 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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