David M. Dooley

7.4k total citations
148 papers, 6.0k citations indexed

About

David M. Dooley is a scholar working on Molecular Biology, Biochemistry and Inorganic Chemistry. According to data from OpenAlex, David M. Dooley has authored 148 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 111 papers in Molecular Biology, 45 papers in Biochemistry and 43 papers in Inorganic Chemistry. Recurrent topics in David M. Dooley's work include Microbial metabolism and enzyme function (83 papers), Porphyrin Metabolism and Disorders (58 papers) and Metal-Catalyzed Oxygenation Mechanisms (42 papers). David M. Dooley is often cited by papers focused on Microbial metabolism and enzyme function (83 papers), Porphyrin Metabolism and Disorders (58 papers) and Metal-Catalyzed Oxygenation Mechanisms (42 papers). David M. Dooley collaborates with scholars based in United States, United Kingdom and Australia. David M. Dooley's co-authors include Michele A. McGuirl, Doreen E. Brown, Peter F. Knowles, Eric M. Shepard, J.M. Guss, Walter G. Zumft, John A. Bollinger, Judith P. Klinman, Robert A. Scott and Harry B. Gray and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

David M. Dooley

147 papers receiving 5.9k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
David M. Dooley United States	46	3.8k	1.8k	1.5k	739	614	148	6.0k
Albrecht Messerschmidt Germany	41	3.6k 1.0×	1.8k 1.0×	482 0.3×	747 1.0×	575 0.9×	100	7.1k
Joann Sanders–Loehr United States	44	2.3k 0.6×	2.1k 1.1×	318 0.2×	974 1.3×	448 0.7×	91	4.7k
Ylva Lindqvist Sweden	53	5.4k 1.4×	773 0.4×	2.5k 1.7×	562 0.8×	618 1.0×	146	8.3k
Hans Eklund Sweden	52	6.5k 1.7×	3.4k 1.8×	686 0.5×	1.4k 1.9×	1.3k 2.0×	109	10.0k
Elinor T. Adman United States	41	3.1k 0.8×	1.3k 0.7×	313 0.2×	610 0.8×	433 0.7×	78	5.3k
Shinnichiro Suzuki Japan	32	1.7k 0.4×	810 0.4×	374 0.3×	514 0.7×	384 0.6×	176	3.5k
Victor L. Davidson United States	43	4.9k 1.3×	1.8k 1.0×	1.2k 0.8×	151 0.2×	805 1.3×	223	5.9k
James W. Whittaker United States	42	2.1k 0.6×	2.8k 1.5×	238 0.2×	1.2k 1.7×	216 0.4×	91	5.8k
I.J. Clifton United Kingdom	34	3.8k 1.0×	1.5k 0.8×	295 0.2×	680 0.9×	343 0.6×	79	5.8k
Carrie M. Wilmot United States	32	3.1k 0.8×	947 0.5×	465 0.3×	240 0.3×	416 0.7×	93	4.0k

Countries citing papers authored by David M. Dooley

Since Specialization

Citations

This map shows the geographic impact of David M. Dooley'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. Dooley 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. Dooley more than expected).

Fields of papers citing papers by David M. Dooley

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

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

Dooley, David M., Seunghyun Ryu, Richard J. Giannone, et al.. (2024). Expanded genome and proteome reallocation in a novel, robust Bacillus coagulans strain capable of utilizing pentose and hexose sugars. mSystems. 9(11). e0095224–e0095224. 2 indexed citations

Mills, Stephen A., et al.. (2012). Cobalt substitution supports an inner-sphere electron transfer mechanism for oxygen reduction in pea seedling amine oxidase. JBIC Journal of Biological Inorganic Chemistry. 17(4). 507–515. 12 indexed citations

McGrath, Aaron P., Kimberly M. Hilmer, Charles A. Collyer, David M. Dooley, & J.M. Guss. (2010). A new crystal form of human diamine oxidase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(2). 137–142. 11 indexed citations

Rogers, Melanie S., Ejan M. Tyler, Sarah E. Deacon, et al.. (2007). The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis ^,. Biochemistry. 46(15). 4606–4618. 88 indexed citations

Abdelhamid, Rehab F., Yoshiko Uchida, Takamitsu Kohzuma, et al.. (2006). π–π interaction between aromatic ring and copper-coordinated His81 imidazole regulates the blue copper active-site structure. JBIC Journal of Biological Inorganic Chemistry. 12(2). 165–173. 46 indexed citations

Duff, Anthony P., Aina E. Cohen, P.J. Ellis, et al.. (2006). The 1.23 Å structure ofPichia pastorislysyl oxidase reveals a lysine–lysine cross-link. Acta Crystallographica Section D Biological Crystallography. 62(9). 1073–1084. 13 indexed citations

Hess, Corinna R., David M. Dooley, Ricky Amii, et al.. (2003). Gold Electrodes Wired for Coupling with the Deeply Buried Active Site of Arthrobacter globiformis Amine Oxidase. Journal of the American Chemical Society. 125(24). 7156–7157. 52 indexed citations

Lee, Mihwa, David B. Langley, Megan J. Maher, et al.. (2002). Crystallization ofPichia pastorislysyl oxidase. Acta Crystallographica Section D Biological Crystallography. 58(12). 2177–2179. 3 indexed citations

Elmore, Bradley O., John A. Bollinger, & David M. Dooley. (2002). Human kidney diamine oxidase: heterologous expression, purification, and characterization. JBIC Journal of Biological Inorganic Chemistry. 7(6). 565–579. 108 indexed citations

10.

McGuirl, Michele A., John A. Bollinger, Nathaniel J. Cosper, Robert A. Scott, & David M. Dooley. (2001). Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster. JBIC Journal of Biological Inorganic Chemistry. 6(2). 189–195. 39 indexed citations

11.

Bollinger, John A., et al.. (2001). Construction, Overexpression, and Purification of Arthrobacter globiformis Amine Oxidase–Strep-Tag II Fusion Protein. Protein Expression and Purification. 22(3). 455–461. 21 indexed citations

12.

Dooley, David M.. (1999). Structure and biogenesis of topaquinone and related cofactors. JBIC Journal of Biological Inorganic Chemistry. 4(1). 1–11. 73 indexed citations

13.

McGuirl, Michele A. & David M. Dooley. (1999). Copper-containing oxidases. Current Opinion in Chemical Biology. 3(2). 138–144. 129 indexed citations

14.

McGuirl, Michele A., Laura K. Nelson, John A. Bollinger, Yiu-Kwok Chan, & David M. Dooley. (1998). The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: Cloning, sequence analysis, and expression. Journal of Inorganic Biochemistry. 70(3-4). 155–169. 17 indexed citations

15.

Dooley, David M. & Doreen E. Brown. (1995). [10] Resonance Raman spectroscopy of quinoproteins. Methods in enzymology on CD-ROM/Methods in enzymology. 258. 132–140. 5 indexed citations

16.

McGuirl, Michele A., et al.. (1994). Purification and active-site characterization of equine plasma amine oxidase. Journal of Inorganic Biochemistry. 56(2). 127–141. 18 indexed citations

17.

McGuirl, Michele A., et al.. (1994). Purification and Characterization of Pea Seedling Amine Oxidase for Crystallization Studies. PLANT PHYSIOLOGY. 106(3). 1205–1211. 45 indexed citations

18.

Dooley, David M., et al.. (1993). Crystallization and Preliminary Crystallographic Characterization of the Copper-containing Amine Oxidase from Pea Seedlings. Journal of Molecular Biology. 229(1). 243–245. 15 indexed citations

19.

Janes, Susan, Monica M. Palcic, Christine H. Scaman, et al.. (1992). Identification of topaquinone and its consensus sequence in copper amine oxidases. Biochemistry. 31(48). 12147–12154. 129 indexed citations

20.

McIntire, William S., et al.. (1990). Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase. PubMed. 32. 315–318. 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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