James E. Erman

3.9k total citations
117 papers, 3.3k citations indexed

About

James E. Erman is a scholar working on Molecular Biology, Cell Biology and Electrical and Electronic Engineering. According to data from OpenAlex, James E. Erman has authored 117 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 96 papers in Molecular Biology, 47 papers in Cell Biology and 43 papers in Electrical and Electronic Engineering. Recurrent topics in James E. Erman's work include Photosynthetic Processes and Mechanisms (72 papers), Hemoglobin structure and function (43 papers) and Electrochemical sensors and biosensors (40 papers). James E. Erman is often cited by papers focused on Photosynthetic Processes and Mechanisms (72 papers), Hemoglobin structure and function (43 papers) and Electrochemical sensors and biosensors (40 papers). James E. Erman collaborates with scholars based in United States and United Kingdom. James E. Erman's co-authors include Lidia B. Vitello, James D. Satterlee, Takashi Yonetani, J. Kraut, J. Matthew Mauro, George H. Reed, J.S. Leigh, Hirokazu Yamamoto, Andrew F.W. Coulson and Gordon G. Hammes and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

James E. Erman

117 papers receiving 3.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
James E. Erman United States 32 2.3k 1.1k 785 506 424 117 3.3k
David B. Goodin United States 36 2.7k 1.2× 646 0.6× 500 0.6× 447 0.9× 968 2.3× 81 4.1k
Francis Millett United States 40 3.0k 1.3× 582 0.5× 576 0.7× 166 0.3× 421 1.0× 128 4.0k
B.F. Van Gelder Netherlands 32 2.6k 1.1× 990 0.9× 578 0.7× 256 0.5× 213 0.5× 82 3.9k
Abel Schejter Israel 31 2.3k 1.0× 1.0k 0.9× 354 0.5× 270 0.5× 150 0.4× 89 3.3k
Gianantonio Battistuzzi Italy 32 1.7k 0.7× 391 0.4× 952 1.2× 329 0.7× 473 1.1× 143 3.2k
L. Powers United States 28 1.3k 0.6× 605 0.5× 198 0.3× 168 0.3× 395 0.9× 72 2.3k
Carlos Gómez‐Moreno Spain 36 2.8k 1.2× 281 0.3× 323 0.4× 427 0.8× 1.1k 2.5× 129 3.6k
Lars‐Erik Andréasson Sweden 29 1.6k 0.7× 199 0.2× 290 0.4× 392 0.8× 357 0.8× 49 2.3k
Victor L. Davidson United States 43 4.9k 2.1× 805 0.7× 415 0.5× 188 0.4× 1.8k 4.3× 223 5.9k
James T. Hazzard United States 27 1.1k 0.5× 238 0.2× 428 0.5× 264 0.5× 313 0.7× 46 1.8k

Countries citing papers authored by James E. Erman

Since Specialization
Citations

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

Fields of papers citing papers by James E. Erman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of James E. Erman

This figure shows the co-authorship network connecting the top 25 collaborators of James E. Erman. A scholar is included among the top collaborators of James E. 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 James E. Erman. James E. 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.
Ayala, Caitlan E., et al.. (2015). Apolar distal pocket mutants of yeast cytochrome c peroxidase: Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(8). 919–929. 1 indexed citations
2.
Erman, James E., et al.. (2015). Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L). Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(8). 869–881. 7 indexed citations
3.
Chinchilla, Diana, et al.. (2013). Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I. Biochemical and Biophysical Research Communications. 443(1). 200–204. 4 indexed citations
4.
Vitello, Lidia B. & James E. Erman. (2001). Oxidation of bis(terpyridine)cobalt(II) chloride by cytochrome c peroxidase compounds I and II. JBIC Journal of Biological Inorganic Chemistry. 6(5-6). 578–589. 5 indexed citations
5.
Vitello, Lidia B., et al.. (1999). Metmyoglobin/Azide: The Effect of Heme-Linked Ionizations on the Rate of Complex Formation. Archives of Biochemistry and Biophysics. 362(1). 148–158. 11 indexed citations
6.
Erman, James E. & Lidia B. Vitello. (1998). Cytochrome c Peroxidase: A Model Heme Protein. BMB Reports. 31(4). 307–327. 19 indexed citations
7.
Vitello, Lidia B., et al.. (1998). Imidazole Binding to Horse Metmyoglobin: Dependence upon pH and Ionic Strength. Archives of Biochemistry and Biophysics. 352(2). 214–228. 14 indexed citations
8.
Vitello, Lidia B., et al.. (1998). Metmyoglobin/Fluoride: Effect of Distal Histidine Protonation on the Association and Dissociation Rate Constants. Archives of Biochemistry and Biophysics. 358(2). 359–368. 19 indexed citations
9.
10.
Matthis, Andrea L., Lidia B. Vitello, & James E. Erman. (1995). Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength. Biochemistry. 34(31). 9991–9999. 12 indexed citations
11.
12.
Miller, Mark A., Lidia B. Vitello, & James E. Erman. (1995). Regulation of Interprotein Electron Transfer By Trp 191 of Cytochrome c Peroxidase. Biochemistry. 34(37). 12048–12058. 31 indexed citations
13.
Satterlee, James D., et al.. (1994). The Effect of the Asn82→Asp Mutation in Yeast Cytochrome c Peroxidase Studied by Proton NMR Spectroscopy. European Journal of Biochemistry. 224(1). 81–87. 17 indexed citations
14.
Erman, James E., et al.. (1993). Proton NMR studies of noncovalent complexes of cytochrome c peroxidase-cyanide with horse and yeast ferricytochromes c. Biochemistry. 32(41). 10988–10994. 17 indexed citations
15.
Moench, Susan J., James E. Erman, & James D. Satterlee. (1993). Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C. International Journal of Biochemistry. 25(9). 1335–1342. 4 indexed citations
16.
Vitello, Lidia B., James E. Erman, Mark A. Miller, Jimin Wang, & J. Kraut. (1993). Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide. Biochemistry. 32(37). 9807–9818. 103 indexed citations
17.
Vitello, Lidia B., James E. Erman, Mark A. Miller, J. Matthew Mauro, & Joseph Kraut. (1992). Effect of Asp-235 .fwdarw. Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase. Biochemistry. 31(46). 11524–11535. 46 indexed citations
18.
Vitello, Lidia B., et al.. (1990). pH-Dependent spectral and kinetic properties of cytochrome c peroxidase: comparison of freshly isolated and stored enzyme. Biochemistry. 29(18). 4283–4288. 52 indexed citations
19.
Hazzard, James T., Susan J. Moench, James E. Erman, James D. Satterlee, & Gordon Tollin. (1988). Kinetics of intracomplex electron transfer and of reduction of the components of covalent and noncovalent complexes of cytochrome c and cytochrome c peroxidase by free flavin semiquinones. Biochemistry. 27(6). 2002–2008. 44 indexed citations
20.
Kresheck, Gordon C. & James E. Erman. (1988). Calorimetric studies of the thermal denaturation of cytochrome c peroxidase. Biochemistry. 27(7). 2490–2496. 31 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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