R.E. Fenna

2.6k total citations · 1 hit paper
26 papers, 2.1k citations indexed

About

R.E. Fenna is a scholar working on Molecular Biology, Materials Chemistry and Immunology. According to data from OpenAlex, R.E. Fenna has authored 26 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 16 papers in Materials Chemistry and 8 papers in Immunology. Recurrent topics in R.E. Fenna's work include Enzyme Structure and Function (12 papers), Neutrophil, Myeloperoxidase and Oxidative Mechanisms (8 papers) and Photosynthetic Processes and Mechanisms (7 papers). R.E. Fenna is often cited by papers focused on Enzyme Structure and Function (12 papers), Neutrophil, Myeloperoxidase and Oxidative Mechanisms (8 papers) and Photosynthetic Processes and Mechanisms (7 papers). R.E. Fenna collaborates with scholars based in United States, United Kingdom and Japan. R.E. Fenna's co-authors include Brian W. Matthews, Curt A. Davey, Jie Zeng, Tristan J. Fiedler, J.M. Olson, Michael F. Schmid, Martino Bolognesi, David I. Stuart, D.C. Phillips and K. Ravi Acharya and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Accounts of Chemical Research.

In The Last Decade

R.E. Fenna

26 papers receiving 2.0k citations

Hit Papers

Chlorophyll arrangement in a bacteriochlorophyll protein ... 1975 2026 1992 2009 1975 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
R.E. Fenna United States 18 1.2k 592 506 413 380 26 2.1k
Badry Bursulaya United States 31 1.5k 1.2× 149 0.3× 396 0.8× 287 0.7× 147 0.4× 57 3.4k
Norman J. Oppenheimer United States 34 2.2k 1.9× 602 1.0× 83 0.2× 443 1.1× 143 0.4× 93 4.4k
Anke C. Terwisscha van Scheltinga Netherlands 21 2.5k 2.1× 212 0.4× 219 0.4× 266 0.6× 70 0.2× 29 3.0k
Betty J. Gaffney United States 28 1.3k 1.1× 80 0.1× 231 0.5× 270 0.7× 185 0.5× 68 2.6k
Tohru Terada Japan 29 1.9k 1.6× 133 0.2× 148 0.3× 459 1.1× 86 0.2× 134 2.6k
A. Weichsel United States 31 1.8k 1.5× 143 0.2× 91 0.2× 387 0.9× 662 1.7× 55 3.1k
Pascale Debey France 27 2.2k 1.9× 198 0.3× 67 0.1× 195 0.5× 501 1.3× 92 3.4k
R. Heiner Schirmer Germany 20 2.1k 1.8× 89 0.2× 83 0.2× 673 1.6× 196 0.5× 28 2.9k
Abel Schejter Israel 31 2.3k 1.9× 59 0.1× 531 1.0× 413 1.0× 208 0.5× 89 3.3k
Heinz Rüterjans Germany 37 3.1k 2.6× 109 0.2× 188 0.4× 946 2.3× 102 0.3× 144 4.2k

Countries citing papers authored by R.E. Fenna

Since Specialization
Citations

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

Fields of papers citing papers by R.E. Fenna

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by R.E. Fenna. 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 R.E. Fenna. The network helps show where R.E. Fenna may publish in the future.

Co-authorship network of co-authors of R.E. Fenna

This figure shows the co-authorship network connecting the top 25 collaborators of R.E. Fenna. A scholar is included among the top collaborators of R.E. Fenna 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 R.E. Fenna. R.E. Fenna 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.
Fiedler, Tristan J., Curt A. Davey, & R.E. Fenna. (2000). X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution. Journal of Biological Chemistry. 275(16). 11964–11971. 312 indexed citations
2.
Fiedler, Tristan J., et al.. (1999). Crystallization and characterization of a fragment of pseudouridine synthase RluC fromEscherichia coli. Acta Crystallographica Section D Biological Crystallography. 55(1). 302–304. 8 indexed citations
4.
Fenna, R.E., Jie Zeng, & Curt A. Davey. (1995). Structure of the Green Heme in Myeloperoxidase. Archives of Biochemistry and Biophysics. 316(1). 653–656. 119 indexed citations
5.
Jacquet, Alain, et al.. (1994). Site-Directed Mutagenesis of Human Myeloperoxidase: Further Identification of Residues Involved in Catalytic Activity and Heme Interaction. Biochemical and Biophysical Research Communications. 202(1). 73–81. 18 indexed citations
6.
Zeng, Jie & R.E. Fenna. (1992). X-ray crystal structure of canine myeloperoxidase at 3 Å resolution. Journal of Molecular Biology. 226(1). 185–207. 252 indexed citations
7.
Acharya, K. Ravi, Jingshan Ren, David I. Stuart, D.C. Phillips, & R.E. Fenna. (1991). Crystal structure of human α-lactalbumin at 1·7 Å resolution. Journal of Molecular Biology. 221(2). 571–581. 166 indexed citations
8.
Zeng, Jie, et al.. (1990). Crystallization of a calcium-binding lysozyme from horse milk.. Journal of Biological Chemistry. 265(25). 14886–14887. 6 indexed citations
9.
Zeng, Jie & R.E. Fenna. (1989). Tetragonal crystals of canine myeloperoxidase suitable for X-ray structural analysis. Journal of Molecular Biology. 210(3). 681–683. 6 indexed citations
10.
Fenna, R.E.. (1987). Crystallization and subunit structure of canine myeloperoxidase. Journal of Molecular Biology. 196(4). 919–925. 9 indexed citations
11.
Smith, Samuel G., M. Lewis, R. Aschaffenburg, et al.. (1987). Crystallographic analysis of the three-dimensional structure of baboon α-lactalbumin at low resolution. Homology with lysozyme. Biochemical Journal. 242(2). 353–360. 30 indexed citations
12.
Brew, Keith, et al.. (1986). The complete amino acid sequence of a bacteriochlorophyll a-protein from Prosthecochloris aestuarii.. Journal of Biological Chemistry. 261(8). 3607–3615. 22 indexed citations
13.
Fenna, R.E.. (1982). Crystallization of human α-lactalbumin. Journal of Molecular Biology. 161(1). 211–215. 10 indexed citations
14.
Fenna, R.E.. (1982). Crystallization of cow α-lactalbumin. Journal of Molecular Biology. 161(1). 203–210. 7 indexed citations
15.
Frey, Terrence, Jürgen Held, Larry J. Weissman, et al.. (1978). New crystal forms of glutamine synthetase and implications for the molecular structure. Journal of Molecular Biology. 122(2). 163–173. 17 indexed citations
16.
Fenna, R.E., Lynn F. Ten Eyck, & B.W. Matthews. (1977). Atomic coordinates for the chlorophyll core of a bacteriochlorophyll a-protein from green photosynthetic bacteria. Biochemical and Biophysical Research Communications. 75(3). 751–756. 33 indexed citations
17.
Matthews, Brian W., R.E. Fenna, & S. James Remington. (1977). An evaluation of electron micrographs of bacteriochlorophyll a-protein crystals in terms of the structure determined by X-ray crystallography. Journal of Ultrastructure Research. 58(3). 316–330. 9 indexed citations
18.
Fenna, R.E. & Brian W. Matthews. (1975). Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola. Nature. 258(5536). 573–577. 421 indexed citations breakdown →
19.
Aschaffenburg, R., R.E. Fenna, & D. C. Phillips. (1972). Crystallography of α-lactalbumin. Journal of Molecular Biology. 67(3). 529–531. 18 indexed citations
20.
Aschaffenburg, R., et al.. (1972). Crystallography of α-lactalbumin. Journal of Molecular Biology. 67(3). 525–528. 17 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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