Mary Erman

1.8k total citations · 1 hit paper
27 papers, 1.5k citations indexed

About

Mary Erman is a scholar working on Molecular Biology, Materials Chemistry and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Mary Erman has authored 27 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 9 papers in Materials Chemistry and 7 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Mary Erman's work include Enzyme Structure and Function (8 papers), Steroid Chemistry and Biochemistry (6 papers) and Estrogen and related hormone effects (5 papers). Mary Erman is often cited by papers focused on Enzyme Structure and Function (8 papers), Steroid Chemistry and Biochemistry (6 papers) and Estrogen and related hormone effects (5 papers). Mary Erman collaborates with scholars based in United States, Sweden and Chile. Mary Erman's co-authors include Debashis Ghosh, Walter Pangborn, Jennifer Griswold, William L. Duax, Charles M. Weeks, Z. Wawrzak, Mark W. Sawicki, James C. Orr, Paweł Grochulski and В. З. Плетнев and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Mary Erman

27 papers receiving 1.5k citations

Hit Papers

Structural basis for androgen specificity and oestrogen s... 2009 2026 2014 2020 2009 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
Mary Erman United States 15 835 476 338 262 245 27 1.5k
Angelo D. Favia United Kingdom 17 925 1.1× 218 0.5× 145 0.4× 165 0.6× 144 0.6× 29 1.7k
Paula R. Davis-Searles United States 8 665 0.8× 235 0.5× 200 0.6× 192 0.7× 351 1.4× 9 1.2k
А. А. Гилеп Belarus 23 680 0.8× 260 0.5× 423 1.3× 56 0.2× 743 3.0× 110 1.7k
TOSHIO NAMBARA Japan 21 841 1.0× 294 0.6× 173 0.5× 54 0.2× 127 0.5× 220 1.9k
Charlotta Filling Sweden 10 981 1.2× 157 0.3× 325 1.0× 342 1.3× 193 0.8× 12 1.5k
Erwin von Angerer Germany 29 713 0.9× 591 1.2× 116 0.3× 57 0.2× 64 0.3× 94 2.4k
Gary H. Rasmusson United States 24 808 1.0× 256 0.5× 896 2.7× 28 0.1× 188 0.8× 45 1.9k
Paolo Lombardi Italy 26 1.2k 1.4× 252 0.5× 66 0.2× 48 0.2× 396 1.6× 76 2.2k
Marianne Ridderström Sweden 19 927 1.1× 103 0.2× 47 0.1× 153 0.6× 463 1.9× 28 1.7k
David L. Corina United Kingdom 14 460 0.6× 228 0.5× 109 0.3× 64 0.2× 344 1.4× 39 1.0k

Countries citing papers authored by Mary Erman

Since Specialization
Citations

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

Fields of papers citing papers by Mary Erman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mary Erman. 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 Mary Erman. The network helps show where Mary Erman may publish in the future.

Co-authorship network of co-authors of Mary Erman

This figure shows the co-authorship network connecting the top 25 collaborators of Mary Erman. A scholar is included among the top collaborators of Mary Erman 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 Mary Erman. Mary Erman 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.
Ghosh, Debashis, Jennifer Griswold, Mary Erman, & Walter Pangborn. (2009). X-ray structure of human aromatase reveals an androgen-specific active site. The Journal of Steroid Biochemistry and Molecular Biology. 118(4-5). 197–202. 87 indexed citations
2.
Ghosh, Debashis, Jennifer Griswold, Mary Erman, & Walter Pangborn. (2009). Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature. 457(7226). 219–223. 452 indexed citations breakdown →
4.
Higashiyama, Tadayoshi, et al.. (2004). Suppression of human cytochrome P450 aromatase activity by monoclonal and recombinant antibody fragments and identification of a stable antigenic complex. The Journal of Steroid Biochemistry and Molecular Biology. 88(3). 235–245. 16 indexed citations
5.
Ghosh, Debashis, Mark W. Sawicki, Mary Erman, et al.. (2001). Multiple Conformations of Catalytic Serine and Histidine in Acetylxylan Esterase at 0.90 Å. Journal of Biological Chemistry. 276(14). 11159–11166. 54 indexed citations
6.
Ghosh, Debashis, Mark W. Sawicki, В. З. Плетнев, et al.. (2001). Porcine Carbonyl Reductase. Journal of Biological Chemistry. 276(21). 18457–18463. 83 indexed citations
7.
Weeks, Charles M., A.W. Roszak, Mary Erman, et al.. (1999). Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 Å resolution. Acta Crystallographica Section D Biological Crystallography. 55(1). 93–102. 11 indexed citations
8.
Ghosh, Debashis, Mary Erman, Mark W. Sawicki, et al.. (1999). Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase. Acta Crystallographica Section D Biological Crystallography. 55(4). 779–784. 40 indexed citations
9.
Sawicki, Mark W., Mary Erman, Terhi Puranen, Pirkko Vihko, & Debashis Ghosh. (1999). Structure of the ternary complex of human 17β-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP +. Proceedings of the National Academy of Sciences. 96(3). 840–845. 103 indexed citations
10.
Kaiser, Rudolf, Mary Erman, Charles M. Weeks, et al.. (1996). Fructose‐1,6‐bisphosphatase. Primary structure of the rabbit liver enzyme. ‘Intermediate’ variability of an oligomeric protein. FEBS Letters. 389(3). 249–252. 5 indexed citations
11.
Ghosh, Debashis, Z. Wawrzak, В. З. Плетнев, et al.. (1995). Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase. Structure. 3(3). 279–288. 94 indexed citations
12.
Ghosh, Debashis, Z. Wawrzak, В. З. Плетнев, et al.. (1995). Molecular Mechanism of Inhibition of Steroid Dehydrogenases by Licorice‐Derived Steroid Analogs in Modulation of Steroid Receptor Functiona. Annals of the New York Academy of Sciences. 761(1). 341–343. 10 indexed citations
13.
Ghosh, Debashis, Mary Erman, Z. Wawrzak, William L. Duax, & Walter Pangborn. (1994). Mechanism of inhibition of 3α,20β-hydroxysteroid dehydrogenaseby a licorice-derived steroidal inhibitor. Structure. 2(10). 973–980. 53 indexed citations
14.
Ghosh, Debashis, Z. Wawrzak, Charles M. Weeks, William L. Duax, & Mary Erman. (1994). The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure. 2(7). 629–640. 180 indexed citations
15.
Kaiser, Rudolf, Mary Erman, William L. Duax, Debashis Ghosh, & Hans Jörnvall. (1994). Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. FEBS Letters. 337(2). 123–127. 37 indexed citations
16.
Ghosh, Debashis, Mary Erman, Walter Pangborn, et al.. (1993). Crystallization and preliminary x-ray diffraction studies of a mammalian steroid dehydrogenase. The Journal of Steroid Biochemistry and Molecular Biology. 46(1). 103–104. 6 indexed citations
17.
Ghosh, Debashis, Mary Erman, Walter Pangborn, William L. Duax, & Michael E. Baker. (1992). Inhibition of Streptomyces hydrogenans 3α,20β-hydroxysteroid dehydrogenase by licorice-derived compounds and crystallization of an enzyme-cofactor-inhibitor complex. The Journal of Steroid Biochemistry and Molecular Biology. 42(8). 849–853. 24 indexed citations
18.
Ghosh, Debashis, Mary Erman, & William L. Duax. (1991). Crystallization and preliminary diffraction analysis of cholesterol esterase from Candida cylindracea. The Journal of Steroid Biochemistry and Molecular Biology. 38(5). 663–665. 12 indexed citations
19.
Ghosh, Debashis, Charles M. Weeks, Paweł Grochulski, et al.. (1991). Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.. Proceedings of the National Academy of Sciences. 88(22). 10064–10068. 213 indexed citations
20.
Langs, David A., Mary Erman, & George T. DeTitta. (1977). Conformations of Prostaglandin F and Recognition of Prostaglandins by Their Receptors. Science. 197(4307). 1003–1005. 19 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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