Melissa W. Calhoun

1.2k total citations
17 papers, 1.0k citations indexed

About

Melissa W. Calhoun is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Melissa W. Calhoun has authored 17 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 6 papers in Cell Biology and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in Melissa W. Calhoun's work include Photosynthetic Processes and Mechanisms (14 papers), Hemoglobin structure and function (6 papers) and Photoreceptor and optogenetics research (5 papers). Melissa W. Calhoun is often cited by papers focused on Photosynthetic Processes and Mechanisms (14 papers), Hemoglobin structure and function (6 papers) and Photoreceptor and optogenetics research (5 papers). Melissa W. Calhoun collaborates with scholars based in United States, Germany and United Kingdom. Melissa W. Calhoun's co-authors include Robert B. Gennis, Jeffrey W. Thomas, Laura J. Lemieux, Kristine L. Oden, Oense M. Neijssel, W. John Ingledew, Mary M Tecklenburg, James O. Alben, Shelagh Ferguson‐Miller and Ǵerald Babcock and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Trends in Biochemical Sciences.

In The Last Decade

Melissa W. Calhoun

17 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Melissa W. Calhoun United States 13 912 239 238 116 92 17 1.0k
Margareta Svensson-Ek Sweden 6 803 0.9× 138 0.6× 339 1.4× 99 0.9× 76 0.8× 6 875
Dmitry A. Bloch Finland 23 1.2k 1.3× 184 0.8× 472 2.0× 88 0.8× 89 1.0× 39 1.4k
Oliver‐Matthias H. Richter Germany 16 711 0.8× 126 0.5× 275 1.2× 89 0.8× 67 0.7× 21 893
Marina Verkhovskaya Finland 27 1.6k 1.8× 194 0.8× 578 2.4× 126 1.1× 107 1.2× 48 1.9k
Denise A. Mills United States 26 1.3k 1.4× 193 0.8× 772 3.2× 91 0.8× 90 1.0× 40 1.5k
Chang-An Yu United States 13 1.3k 1.4× 123 0.5× 112 0.5× 210 1.8× 190 2.1× 16 1.5k
Sirpa Riistama Finland 6 544 0.6× 94 0.4× 212 0.9× 57 0.5× 55 0.6× 7 597
Celia F. Goodhew United Kingdom 15 530 0.6× 106 0.4× 83 0.3× 79 0.7× 83 0.9× 23 699
Irina A. Smirnova Russia 15 587 0.6× 75 0.3× 246 1.0× 41 0.4× 68 0.7× 29 697
Sergey A. Siletsky Russia 18 960 1.1× 212 0.9× 585 2.5× 67 0.6× 72 0.8× 32 1.2k

Countries citing papers authored by Melissa W. Calhoun

Since Specialization
Citations

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

Fields of papers citing papers by Melissa W. Calhoun

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Melissa W. Calhoun. 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 Melissa W. Calhoun. The network helps show where Melissa W. Calhoun may publish in the future.

Co-authorship network of co-authors of Melissa W. Calhoun

This figure shows the co-authorship network connecting the top 25 collaborators of Melissa W. Calhoun. A scholar is included among the top collaborators of Melissa W. Calhoun 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 Melissa W. Calhoun. Melissa W. Calhoun 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.
2.
Calhoun, Melissa W., Robert B. Gennis, W. John Ingledew, & John C. Salerno. (1994). Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1206(1). 143–154. 8 indexed citations
3.
Calhoun, Melissa W., Jeffrey W. Thomas, & Robert B. Gennis. (1994). The cytochrome oxidase superfamily of redox-driven proton pumps. Trends in Biochemical Sciences. 19(8). 325–330. 141 indexed citations
4.
Thomas, Jeffrey W., Melissa W. Calhoun, Laura J. Lemieux, et al.. (1994). Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand. Biochemistry. 33(44). 13013–13021. 22 indexed citations
5.
Ohnishi, Tomo̧ko, Vladimir D. Sled, Steven W. Meinhardt, et al.. (1994). Biophysical and Biochemical studies of bacterial NADH:quinone oxidoreductase (NDH-1). Biochemical Society Transactions. 22(1). 70S–70S. 5 indexed citations
6.
Calhoun, Melissa W., et al.. (1993). Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. Journal of Bacteriology. 175(10). 3020–3025. 152 indexed citations
7.
Lemon, Douglas D., et al.. (1993). The gateway to the active site of heme-copper oxidases. Biochemistry. 32(45). 11953–11956. 58 indexed citations
8.
Hosler, Jonathan P., Shelagh Ferguson‐Miller, Melissa W. Calhoun, et al.. (1993). Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo. Journal of Bioenergetics and Biomembranes. 25(2). 121–136. 228 indexed citations
9.
Calhoun, Melissa W. & Robert B. Gennis. (1993). Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. Journal of Bacteriology. 175(10). 3013–3019. 88 indexed citations
10.
Calhoun, Melissa W., John J. Hill, Laura J. Lemieux, et al.. (1993). Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: Amino acid substitutions for two histidines that are putative CuB ligands. Biochemistry. 32(43). 11524–11529. 28 indexed citations
11.
Calhoun, Melissa W., Laura J. Lemieux, Jeffrey W. Thomas, et al.. (1993). Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli. Biochemistry. 32(48). 13254–13261. 18 indexed citations
12.
13.
Sled, Vladimir D., Thorsten Friedrich, Hans Leif, et al.. (1993). Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems. Journal of Bioenergetics and Biomembranes. 25(4). 347–356. 75 indexed citations
14.
15.
Calhoun, Melissa W., Robert B. Gennis, & John C. Salerno. (1992). The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a ‘g = 12’ EPR feature analogous to that of ‘slow’ cytochrome oxidase. FEBS Letters. 309(2). 127–129. 11 indexed citations
16.
Lemieux, Laura J., Melissa W. Calhoun, Jeffrey W. Thomas, W. John Ingledew, & Robert B. Gennis. (1992). Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.. Journal of Biological Chemistry. 267(3). 2105–2113. 107 indexed citations
17.
Calhoun, Melissa W., Gail Newton, & Robert B. Gennis. (1991). E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli. Journal of Bacteriology. 173(5). 1569–1570. 18 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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