E. Margoliash

1.9k total citations
39 papers, 1.6k citations indexed

About

E. Margoliash is a scholar working on Molecular Biology, Immunology and Electrical and Electronic Engineering. According to data from OpenAlex, E. Margoliash has authored 39 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 8 papers in Immunology and 7 papers in Electrical and Electronic Engineering. Recurrent topics in E. Margoliash's work include Photosynthetic Processes and Mechanisms (11 papers), Spectroscopy and Quantum Chemical Studies (5 papers) and T-cell and B-cell Immunology (5 papers). E. Margoliash is often cited by papers focused on Photosynthetic Processes and Mechanisms (11 papers), Spectroscopy and Quantum Chemical Studies (5 papers) and T-cell and B-cell Immunology (5 papers). E. Margoliash collaborates with scholars based in United States, Netherlands and Switzerland. E. Margoliash's co-authors include Susan K. Pierce, R H Schwartz, Hans Rudolf Bosshard, Anne M. VanBuskirk, Samuel H. Speck, Neil Osheroff, Charles Hannum, Brian M. Hoffman, Frederick S. Sherman and John Stewart and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

E. Margoliash

38 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E. Margoliash United States 24 1.1k 432 283 247 137 39 1.6k
Eugene C. Petrella United States 14 1.1k 1.0× 243 0.6× 161 0.6× 194 0.8× 94 0.7× 17 1.6k
Alain Bienvenüe France 24 1.2k 1.1× 171 0.4× 58 0.2× 215 0.9× 62 0.5× 68 1.8k
André Lopez France 22 1.1k 1.0× 161 0.4× 61 0.2× 92 0.4× 110 0.8× 38 1.6k
Tomasz Heyduk United States 36 3.1k 2.8× 77 0.2× 133 0.5× 196 0.8× 44 0.3× 87 3.7k
Deborah S. Wuttke United States 32 2.6k 2.4× 84 0.2× 88 0.3× 88 0.4× 163 1.2× 85 3.2k
Nanda K. Subbarao United States 8 1.5k 1.3× 77 0.2× 50 0.2× 133 0.5× 41 0.3× 8 1.8k
J.W. Becker United States 13 1.1k 1.0× 255 0.6× 111 0.4× 117 0.5× 17 0.1× 16 1.3k
Marcel Joniau Belgium 23 1.1k 1.0× 181 0.4× 102 0.4× 261 1.1× 36 0.3× 67 1.9k
Jorge Santoro Spain 29 1.9k 1.7× 230 0.5× 106 0.4× 162 0.7× 32 0.2× 62 2.4k
J.A. Forrester United Kingdom 19 627 0.6× 673 1.6× 228 0.8× 56 0.2× 26 0.2× 42 1.4k

Countries citing papers authored by E. Margoliash

Since Specialization
Citations

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

Fields of papers citing papers by E. Margoliash

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of E. Margoliash

This figure shows the co-authorship network connecting the top 25 collaborators of E. Margoliash. A scholar is included among the top collaborators of E. Margoliash 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 E. Margoliash. E. Margoliash 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.
Wang, Yu & E. Margoliash. (1995). Enzymic Activities of Covalent 1:1 Complexes of Cytochrome c and Cytochrome c Peroxidase. Biochemistry. 34(6). 1948–1958. 10 indexed citations
2.
Jemmerson, Ronald, et al.. (1994). Crystallization of two monoclonal Fab fragments of similar amino-acid sequence bound to the same area of horse cytochromecand interacting by potentially distinct mechanisms. Acta Crystallographica Section D Biological Crystallography. 50(1). 64–70. 3 indexed citations
3.
VanBuskirk, Anne M., et al.. (1989). A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family.. The Journal of Experimental Medicine. 170(6). 1799–1809. 217 indexed citations
4.
Margoliash, E., et al.. (1988). Time dependence of B cell processing and presentation of peptide and native protein antigens.. The Journal of Immunology. 140(10). 3309–3314. 36 indexed citations
5.
Rush, James D., Willem H. Koppenol, Eric A. E. Garber, & E. Margoliash. (1988). Conformational stability of ferrocytochrome c. Electrostatic aspects of the oxidation by tris(1,10-phenanthroline)cobalt(III) at low ionic strength.. Journal of Biological Chemistry. 263(16). 7514–7520. 21 indexed citations
6.
Smith, John A., et al.. (1987). A Peptide Binding Protein Which Plays a Role in Antigen Presentation. Advances in experimental medicine and biology. 225. 161–164. 3 indexed citations
7.
Margoliash, E., et al.. (1987). Identification of a peptide binding protein that plays a role in antigen presentation.. Proceedings of the National Academy of Sciences. 84(6). 1659–1663. 98 indexed citations
8.
Theodorakis, Janice L., Lyman G. Armes, & E. Margoliash. (1986). Preparation and characterization of singly-substituted sulfhydryl derivatives of cytochrome c. Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States). 9(49). 47–47. 1 indexed citations
9.
Hannum, Charles & E. Margoliash. (1985). Assembled topographic antigenic determinants of pigeon cytochrome c.. The Journal of Immunology. 135(5). 3303–3313. 12 indexed citations
10.
Ho, P Shing, et al.. (1985). Species specificity of long-range electron transfer within the complex between zinc-substituted cytochrome c peroxidase and cytochrome c. Journal of the American Chemical Society. 107(4). 1070–1071. 49 indexed citations
11.
Speck, Samuel H. & E. Margoliash. (1984). Characterization of the interaction of cytochrome c and mitochondrial ubiquinol-cytochrome c reductase.. Journal of Biological Chemistry. 259(2). 1064–1072. 33 indexed citations
12.
Speck, Samuel H., et al.. (1983). Role of phospholipid in the low affinity reactions between cytochrome c and cytochrome oxidase. FEBS Letters. 164(2). 379–382. 31 indexed citations
13.
Butler, J. A. V., D. Martin Davies, A. Geoffrey Sykes, et al.. (1981). Use of singly modified cytochrome c derivatives to determine the site for electron transfer in reactions with inorganic complexes. Journal of the American Chemical Society. 103(2). 469–471. 43 indexed citations
14.
Osheroff, Neil, David L. Brautigan, & E. Margoliash. (1980). Mapping of anion binding sites on cytochrome c by differential chemical modification of lysine residues.. Proceedings of the National Academy of Sciences. 77(8). 4439–4443. 56 indexed citations
16.
Jemmerson, Ronald, et al.. (1979). Six related protein products from a single patient with multiple myeloma. Biochemistry. 18(21). 4676–4683. 1 indexed citations
17.
Margoliash, E., et al.. (1977). Topographic Determinants on Cytochrome c. The Journal of Immunology. 118(4). 1170–1180. 81 indexed citations
18.
Sherman, Frederick S., et al.. (1970). The relationship of gene structure and protein structure of iso-I-cytochrome c from yeast.. PubMed. 24. 85–107. 16 indexed citations
19.
Sherman, Frederick S., John Stewart, E. Margoliash, Jennifer K. Parker, & William Campbell. (1966). The structural gene for yeast cytochrome C.. Proceedings of the National Academy of Sciences. 55(6). 1498–1504. 98 indexed citations
20.
Margoliash, E., et al.. (1955). SYNTHESIS OF N-α-(2,4-DINITROPHENYL)-D,L-HISTIDINE. The Journal of Organic Chemistry. 20(12). 1650–1653. 2 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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