Bruce A. McFadden

4.4k total citations
162 papers, 3.7k citations indexed

About

Bruce A. McFadden is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Bruce A. McFadden has authored 162 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 122 papers in Molecular Biology, 49 papers in Biochemistry and 40 papers in Materials Chemistry. Recurrent topics in Bruce A. McFadden's work include Enzyme Structure and Function (40 papers), Amino Acid Enzymes and Metabolism (38 papers) and Photosynthetic Processes and Mechanisms (34 papers). Bruce A. McFadden is often cited by papers focused on Enzyme Structure and Function (40 papers), Amino Acid Enzymes and Metabolism (38 papers) and Photosynthetic Processes and Mechanisms (34 papers). Bruce A. McFadden collaborates with scholars based in United States, United Kingdom and Australia. Bruce A. McFadden's co-authors include F. Robert Tabita, Sarla Purohit, Glenn D. Kuehn, Young Hee Ko, Thakor R. Patel, Ashok K. Saluja, G. Ramananda Rao, T.E. Roche, Thomas E. Roche and Henry Daniell 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

Bruce A. McFadden

161 papers receiving 3.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Bruce A. McFadden United States 34 2.7k 919 807 418 369 162 3.7k
H.L. Kornberg United Kingdom 43 4.0k 1.5× 1.4k 1.5× 1.3k 1.6× 546 1.3× 248 0.7× 181 6.1k
J. R. Guest United Kingdom 46 3.5k 1.3× 1.0k 1.1× 1.4k 1.8× 340 0.8× 406 1.1× 107 5.8k
Fredrik Åslund Sweden 26 4.3k 1.6× 534 0.6× 653 0.8× 729 1.7× 192 0.5× 29 5.4k
Francesco Bossa Italy 43 3.5k 1.3× 1.3k 1.4× 1.2k 1.5× 700 1.7× 111 0.3× 187 6.1k
David M. Bonner United States 19 3.6k 1.3× 589 0.6× 459 0.6× 211 0.5× 119 0.3× 57 4.7k
Tatsuo Kurihara Japan 41 2.9k 1.1× 785 0.9× 519 0.6× 236 0.6× 779 2.1× 154 4.5k
Helmut Holzer Germany 49 5.2k 1.9× 857 0.9× 1.1k 1.4× 977 2.3× 174 0.5× 261 7.2k
P. Terpstra Netherlands 29 2.7k 1.0× 567 0.6× 350 0.4× 169 0.4× 86 0.2× 58 3.8k
Yasuhiro Anraku Japan 39 4.1k 1.5× 403 0.4× 310 0.4× 945 2.3× 160 0.4× 136 4.9k
Joseph D. Schrag Canada 40 5.8k 2.1× 760 0.8× 616 0.8× 736 1.8× 104 0.3× 71 7.4k

Countries citing papers authored by Bruce A. McFadden

Since Specialization
Citations

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

Fields of papers citing papers by Bruce A. McFadden

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Bruce A. McFadden

This figure shows the co-authorship network connecting the top 25 collaborators of Bruce A. McFadden. A scholar is included among the top collaborators of Bruce A. McFadden 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 Bruce A. McFadden. Bruce A. McFadden 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.
Britton, K.L., I. Sarath B. Abeysinghe, Patrick J. Baker, et al.. (2001). The structure and domain organization ofEscherichia coliisocitrate lyase. Acta Crystallographica Section D Biological Crystallography. 57(9). 1209–1218. 40 indexed citations
2.
McFadden, Bruce A., et al.. (1998). A study of conserved in-loop and out-of-loop glycine residues in the large subunit of ribulose bisphosphate carboxylase/oxygenase by directed mutagenesis. Protein Engineering Design and Selection. 11(6). 457–465. 9 indexed citations
3.
McFadden, Bruce A., et al.. (1998). [12] Chaperonin 6014 and co-chaperonin 107 from Chromatium vinosum. Methods in enzymology on CD-ROM/Methods in enzymology. 290. 147–154. 1 indexed citations
4.
McFadden, Bruce A., et al.. (1997). Activity and carboxylation specificity factor of mutant ribulose 1,5‐bisphosphate carboxylase/oxygenase from Anacystis Nidulans. IUBMB Life. 42(2). 299–307. 3 indexed citations
5.
Xu, Weidong & Bruce A. McFadden. (1997). Sequence Analysis of Plasmid pCC5.2 from CyanobacteriumSynechocystisPCC 6803 That Replicates by a Rolling Circle Mechanism. Plasmid. 37(2). 95–104. 24 indexed citations
6.
Rehman, Abdur & Bruce A. McFadden. (1997). Lysine 194 Is Functional in Isocitrate Lyase from Escherichia coli. Current Microbiology. 35(1). 14–17. 13 indexed citations
7.
Rehman, Abdur & Bruce A. McFadden. (1996). The Consequences of Replacing Histidine 356 in Isocitrate Lyase fromEscherichia coli. Archives of Biochemistry and Biophysics. 336(2). 309–315. 12 indexed citations
8.
9.
Yang, Xiaoyu & Bruce A. McFadden. (1994). The Complete DNA Sequence and Replication Analysis of the Plasmid pCB2.4 from the Cyanobacterium Synechocystis PCC 6803. Plasmid. 31(2). 131–137. 26 indexed citations
10.
McFadden, Bruce A., et al.. (1992). Serine-376 contributes to the binding of substrate by ribulose-bisphosphate carboxylase/oxygenase from Anacystis nidulans. Biochemistry. 31(8). 2304–2308. 15 indexed citations
11.
Ko, Young Hee, Paolo Vanni, Gerhard R. Munske, & Bruce A. McFadden. (1991). Substrate-decreased modification by diethyl pyrocarbonate of two histidines in isocitrate lyase from Escherichia coli. Biochemistry. 30(30). 7451–7456. 18 indexed citations
12.
Baker, Patrick J., David W. Rice, Timothy J. Stillman, et al.. (1991). Use of chemical modification in the crystallization of isocitrate lyase from Escherichia coli. Journal of Molecular Biology. 220(1). 13–16. 9 indexed citations
13.
McFadden, Bruce A., et al.. (1990). Chemiluminescence of the manganese(2+)-activated ribulose-1,5-bisphosphate oxygenase reaction: evidence for singlet oxygen production. Biochemistry. 29(36). 8333–8337. 20 indexed citations
14.
McFadden, Bruce A., et al.. (1989). Photomodification of a serine at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by vanadate. Biochemistry. 28(13). 5428–5431. 15 indexed citations
15.
16.
Daniell, Henry, et al.. (1988). Amplified expression of ribulose bisphosphate carboxylase/oxygenase in pBR322-transformants of Anacystis nidulans. Archives of Microbiology. 151(1). 59–64. 10 indexed citations
17.
McFadden, Bruce A., et al.. (1983). The response to ribulose bisphosphate4? (RuBP4?) and RuBP-Mg2? in catalysis by structurally divergent RuBP carboxylase/oxygenases. Photosynthesis Research. 4(2). 111–117. 3 indexed citations
18.
Berhow, Mark A. & Bruce A. McFadden. (1983). Ribulose 1,5-bisphosphate carboxylase and phosphoribulokinase in Prochloron. Planta. 158(4). 281–287. 9 indexed citations
19.
Khan, Fazal & Bruce A. McFadden. (1979). Enzyme Profiles in Seedling Development and the Effect of Itaconate, an Isocitrate Lyase-directed Reagent. PLANT PHYSIOLOGY. 64(2). 228–231. 21 indexed citations
20.
Reid, Tony, et al.. (1964). SJT volume 17 issue 1 Cover and Front matter. Scottish Journal of Theology. 17(1). f1–f13. 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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