James A. Roe

2.7k total citations · 2 hit papers
17 papers, 2.3k citations indexed

About

James A. Roe is a scholar working on Inorganic Chemistry, Molecular Biology and Neurology. According to data from OpenAlex, James A. Roe has authored 17 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Inorganic Chemistry, 5 papers in Molecular Biology and 4 papers in Neurology. Recurrent topics in James A. Roe's work include Metal-Catalyzed Oxygenation Mechanisms (9 papers), Amyotrophic Lateral Sclerosis Research (4 papers) and Neurological diseases and metabolism (3 papers). James A. Roe is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (9 papers), Amyotrophic Lateral Sclerosis Research (4 papers) and Neurological diseases and metabolism (3 papers). James A. Roe collaborates with scholars based in United States and Italy. James A. Roe's co-authors include Joan Selverstone Valentine, Román F. Macaya, Juli Feigon, Peter Schultze, F. W. Smith, Jun Goto, Edith B. Gralla, Dale E. Bredesen, Martina Wiedau‐Pazos and Shahrooz Rabizadeh 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

James A. Roe

17 papers receiving 2.2k citations

Hit Papers

Thrombin-binding DNA aptamer forms a unimolecular quadrup... 1993 2026 2004 2015 1993 1996 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James A. Roe United States 14 1.3k 791 297 264 235 17 2.3k
Armando Durazo United States 19 678 0.5× 730 0.9× 193 0.6× 276 1.0× 126 0.5× 23 1.7k
Aram M. Nersissian United States 22 801 0.6× 755 1.0× 261 0.9× 181 0.7× 361 1.5× 28 2.0k
Jun Goto Japan 25 879 0.7× 1.5k 1.9× 515 1.7× 540 2.0× 183 0.8× 64 2.6k
Ashutosh Tiwari United States 32 1.3k 1.1× 1.2k 1.6× 373 1.3× 372 1.4× 69 0.3× 46 3.5k
Bryan F. Shaw United States 21 623 0.5× 615 0.8× 114 0.4× 174 0.7× 63 0.3× 54 1.5k
Peter A. Doucette United States 13 780 0.6× 1.4k 1.8× 360 1.2× 354 1.3× 198 0.8× 13 2.2k
Daryl K. Eggers United States 13 701 0.6× 354 0.4× 119 0.4× 95 0.4× 44 0.2× 25 1.3k
Madhuri Chattopadhyay United States 14 532 0.4× 562 0.7× 272 0.9× 151 0.6× 32 0.1× 15 1.2k
Rishi Rakhit United States 13 650 0.5× 728 0.9× 181 0.6× 253 1.0× 34 0.1× 14 1.3k
David R. Boyer United States 19 1.7k 1.3× 766 1.0× 162 0.5× 78 0.3× 21 0.1× 32 2.6k

Countries citing papers authored by James A. Roe

Since Specialization
Citations

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

Fields of papers citing papers by James A. Roe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of James A. Roe

This figure shows the co-authorship network connecting the top 25 collaborators of James A. Roe. A scholar is included among the top collaborators of James A. Roe 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 James A. Roe. James A. Roe is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

17 of 17 papers shown
1.
Rodríguez, Jorge, Joan Selverstone Valentine, Daryl K. Eggers, et al.. (2002). Familial Amyotrophic Lateral Sclerosis-associated Mutations Decrease the Thermal Stability of Distinctly Metallated Species of Human Copper/Zinc Superoxide Dismutase. Journal of Biological Chemistry. 277(18). 15932–15937. 204 indexed citations
2.
Roe, James A., Martina Wiedau‐Pazos, Vanessa N. Moy, et al.. (2002). In vivo peroxidative activity of FALS-mutant human CuZnSODs expressed in yeast. Free Radical Biology and Medicine. 32(2). 169–174. 30 indexed citations
3.
Wiedau‐Pazos, Martina, Jun Goto, Shahrooz Rabizadeh, et al.. (1996). Cell death mechanisms in ALS. Neurology. 47(4_suppl_2). S36–8; discussion S38. 15 indexed citations
4.
Lyons, Thomas J., Jun Goto, Aram M. Nersissian, et al.. (1996). Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein.. Proceedings of the National Academy of Sciences. 93(22). 12240–12244. 152 indexed citations
5.
Lu, Yi, James A. Roe, Christopher J. Bender, et al.. (1996). New Type 2 Copper−Cysteinate Proteins. Copper Site Histidine-to-Cysteine Mutants of Yeast Copper−Zinc Superoxide Dismutase. Inorganic Chemistry. 35(6). 1692–1700. 34 indexed citations
6.
Wiedau‐Pazos, Martina, Jun Goto, Shahrooz Rabizadeh, et al.. (1996). Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis. Science. 271(5248). 515–518. 586 indexed citations breakdown →
7.
Ogihara, N.L., Hans E. Parge, P. John Hart, et al.. (1996). Unusual Trigonal-Planar Copper Configuration Revealed in the Atomic Structure of Yeast Copper−Zinc Superoxide Dismutase,. Biochemistry. 35(7). 2316–2321. 79 indexed citations
8.
Graden, Janet A., Lisa Ellerby, James A. Roe, & Joan Selverstone Valentine. (1994). Role of the Bridging Histidyl Imidazolate Ligand in Yeast Copper-Zinc Superoxide Dismutase. Characterization of the His63Ala Mutant. Journal of the American Chemical Society. 116(21). 9743–9744. 11 indexed citations
9.
Roe, James A. & David B. Goodin. (1993). Enhanced oxidation of aniline derivatives by two mutants of cytochrome c peroxidase at tryptophan 51.. Journal of Biological Chemistry. 268(27). 20037–20045. 24 indexed citations
10.
Macaya, Román F., Peter Schultze, F. W. Smith, James A. Roe, & Juli Feigon. (1993). Thrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution.. Proceedings of the National Academy of Sciences. 90(8). 3745–3749. 769 indexed citations breakdown →
11.
Lu, Yi, Louis B. LaCroix, Michael D. Lowery, et al.. (1993). Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase. Journal of the American Chemical Society. 115(14). 5907–5918. 59 indexed citations
12.
Lu, Yi, Edith B. Gralla, James A. Roe, & Joan Selverstone Valentine. (1992). The redesign of a type 2 into a type 1 copper protein: construction and characterization of yeast copper, zinc superoxide dismutase mutants. Journal of the American Chemical Society. 114(9). 3560–3562. 21 indexed citations
14.
Roe, James A. & Joan Selverstone Valentine. (1990). Complexometric titrations of protein-bound metal ions: A method for determining binding constants. Analytical Biochemistry. 186(1). 31–40. 2 indexed citations
15.
Roe, James A., et al.. (1990). Silver-binding properties of bovine cuprozinc superoxide dismutase and the overall stability of selected metal-ion derivatives. Journal of the American Chemical Society. 112(4). 1538–1545. 10 indexed citations
16.
Roe, James A., et al.. (1988). Differential scanning calorimetry of copper-zinc-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives. Biochemistry. 27(3). 950–958. 103 indexed citations
17.
Burstyn, Judith N., et al.. (1988). Magnetic and spectroscopic characterization of an iron porphyrin peroxide complex. Peroxoferrioctaethylporphyrin(1-). Journal of the American Chemical Society. 110(5). 1382–1388. 78 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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