Robert A. Scott

9.9k total citations · 1 hit paper
191 papers, 7.8k citations indexed

About

Robert A. Scott is a scholar working on Molecular Biology, Materials Chemistry and Inorganic Chemistry. According to data from OpenAlex, Robert A. Scott has authored 191 papers receiving a total of 7.8k indexed citations (citations by other indexed papers that have themselves been cited), including 81 papers in Molecular Biology, 54 papers in Materials Chemistry and 47 papers in Inorganic Chemistry. Recurrent topics in Robert A. Scott's work include Metal-Catalyzed Oxygenation Mechanisms (37 papers), Metalloenzymes and iron-sulfur proteins (34 papers) and Enzyme Structure and Function (23 papers). Robert A. Scott is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (37 papers), Metalloenzymes and iron-sulfur proteins (34 papers) and Enzyme Structure and Function (23 papers). Robert A. Scott collaborates with scholars based in United States, United Kingdom and Germany. Robert A. Scott's co-authors include A. Grant Mauk, Nathaniel J. Cosper, Jacob E. Shokes, David Giedroc, Keith O. Hodgson, Marly K. Eidsness, Donald M. Kurtz, Michael W. W. Adams, David M. Dooley and Edward I. Solomon and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Robert A. Scott

190 papers receiving 7.5k citations

Hit Papers

align trajectories sort by overperformance

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.

Cytochrome C : A Multidisciplinary Approach

1996 499 citations Robert A. Scott, A. Grant Mauk profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Robert A. Scott	3.4k	1.8k	1.5k	1.3k	945	191	7.8k
J. A. Cowan	5.0k 1.5×	1.4k 0.8×	1.2k 0.8×	1.7k 1.3×	1.8k 1.9×	249	9.0k
Wilfred R. Hagen	3.1k 0.9×	1.6k 0.9×	1.9k 1.2×	3.1k 2.4×	632 0.7×	245	8.2k
Wolfram Meyer‐Klaucke	2.4k 0.7×	1.4k 0.8×	1.6k 1.1×	1.7k 1.3×	925 1.0×	143	7.2k
Thomas M. Loehr	3.1k 0.9×	1.9k 1.1×	2.4k 1.5×	780 0.6×	1.1k 1.1×	145	6.9k
Stefano Ciurli	2.6k 0.8×	1.7k 0.9×	843 0.5×	736 0.6×	1.0k 1.1×	177	6.4k
Bo G. Malmström	5.4k 1.6×	1.1k 0.6×	1.5k 1.0×	613 0.5×	898 1.0×	173	8.9k
S.S. Hasnain	2.6k 0.8×	1.1k 0.6×	976 0.6×	599 0.5×	510 0.5×	181	5.6k
Donald M. Kurtz	2.8k 0.8×	1.4k 0.8×	3.1k 2.0×	1.2k 0.9×	1.2k 1.3×	172	6.7k
Anne Volbeda	2.2k 0.6×	1.9k 1.1×	1.5k 1.0×	5.3k 4.0×	796 0.8×	83	8.1k
Richard Cammack	3.6k 1.1×	1.5k 0.8×	1.6k 1.1×	3.9k 3.0×	449 0.5×	233	8.7k

Countries citing papers authored by Robert A. Scott

Since Specialization

Citations

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

Fields of papers citing papers by Robert A. Scott

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert A. Scott

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

Reyes-Caballero, Hermes, Alfredo J. Guerra, F.E. Jacobsen, et al.. (2010). The Metalloregulatory Zinc Site in Streptococcus pneumoniae AdcR, a Zinc-activated MarR Family Repressor. Journal of Molecular Biology. 403(2). 197–216. 72 indexed citations

Ma, Zhen, Darin M. Cowart, Robert A. Scott, & David Giedroc. (2009). Molecular Insights into the Metal Selectivity of the Copper(I)-Sensing Repressor CsoR from Bacillus subtilis. Biochemistry. 48(15). 3325–3334. 88 indexed citations

Solomon, Edward I., Robert A. Scott, & R. Bruce King. (2009). Computational inorganic and bioinorganic chemistry. Wiley eBooks. 33 indexed citations

Scott, Robert A. & W. C. Sullivan. (2008). Ecology of fermented foods. 15(1). 25–31. 23 indexed citations

Lukehart, Charles M. & Robert A. Scott. (2008). Nanomaterials : inorganic and bioinorganic perspectives. Wiley eBooks. 56 indexed citations

Lipscomb, Gina L., Darin M. Cowart, Gerrit J. Schut, et al.. (2008). SurR: a transcriptional activator and repressor controlling hydrogen and elemental sulphur metabolism in Pyrococcus furiosus. Molecular Microbiology. 71(2). 332–349. 57 indexed citations

Shokes, Jacob E., Evert C. Duin, Carsten Bauer, et al.. (2005). Direct interaction of coenzyme M with the active‐site Fe–S cluster of heterodisulfide reductase. FEBS Letters. 579(7). 1741–1744. 12 indexed citations

Cole, Ewart T., Robert A. Scott, Alyson Connor, et al.. (2002). Enteric coated HPMC capsules designed to achieve intestinal targeting. International Journal of Pharmaceutics. 231(1). 83–95. 180 indexed citations

Bonomi, Francesco, Amy E. Burden, Marly K. Eidsness, et al.. (2001). Thermal stability of the [Fe(SCys)4] site in Clostridium pasteurianum rubredoxin: contributions of the local environment and Cys ligand protonation. JBIC Journal of Biological Inorganic Chemistry. 7(4-5). 427–436. 12 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.

Cosper, Nathaniel J., et al.. (1999). X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase. JBIC Journal of Biological Inorganic Chemistry. 4(1). 122–129. 21 indexed citations

12.

Yamaguchi, Kenji, Nathaniel J. Cosper, Robert A. Scott, et al.. (1999). Characterization of metal-substituted Klebsiella aerogenes urease. JBIC Journal of Biological Inorganic Chemistry. 4(4). 468–477. 29 indexed citations

13.

New, A., et al.. (1998). An in vitro study of a new design of acetabular cement pressurizer. The Journal of Arthroplasty. 13(2). 200–206. 14 indexed citations

14.

Blackburn, Ninian J., S. de Vries, Robert A. Scott, et al.. (1996). XAS studies of the Cu_Acenters of cytochromecoxidase: a unique binuclear copper cluster. Acta Crystallographica Section A Foundations of Crystallography. 52(a1). C70–C70. 6 indexed citations

15.

Michel, Linda O., M.A. Pearson, Evelyn Jabri, et al.. (1996). Characterization of the Mononickel Metallocenter in H134A Mutant Urease. Journal of Biological Chemistry. 271(31). 18632–18637. 31 indexed citations

16.

Eidsness, Marly K., et al.. (1992). Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin. Protein Engineering Design and Selection. 5(4). 367–371. 38 indexed citations

17.

Scott, Robert A., Shengke Wang, Marly K. Eidsness, et al.. (1992). X-ray absorption spectroscopic studies of the high-spin iron(II) active site of isopenicillin N synthase: evidence for iron-sulfur interaction in the enzyme-substrate complex. Biochemistry. 31(19). 4596–4601. 37 indexed citations

18.

Brenner, Mitchell C., et al.. (1992). Spectroscopic characterization of the alternate form of S-methylcoenzyme M reductase from Methanobacterium thermoautotrophicum (strain ΔH). Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1120(2). 160–166. 10 indexed citations

19.

Scott, Robert A., Richard Sullivan, Walter E. DeWolf, Roland E. Dolle, & Lawrence I. Kruse. (1988). The copper sites of dopamine .beta.-hydroxylase: an x-ray absorption spectroscopic study. Biochemistry. 27(15). 5411–5417. 46 indexed citations

20.

Mauk, A. Grant & Robert A. Scott. (1981). A calculator program for determination of phosphate buffer composition. Computers & Chemistry. 5(1). 67–69. 2 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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