O. Epp

8.9k total citations · 6 hit papers
27 papers, 6.9k citations indexed

About

O. Epp is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, O. Epp has authored 27 papers receiving a total of 6.9k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 11 papers in Materials Chemistry and 7 papers in Cell Biology. Recurrent topics in O. Epp's work include Enzyme Structure and Function (11 papers), Protein Structure and Dynamics (7 papers) and Hemoglobin structure and function (7 papers). O. Epp is often cited by papers focused on Enzyme Structure and Function (11 papers), Protein Structure and Dynamics (7 papers) and Hemoglobin structure and function (7 papers). O. Epp collaborates with scholars based in Germany, United States and Austria. O. Epp's co-authors include Robert Huber, J. Deisenhofer, Hartmut Michel, Kunio Miki, Albrecht Wendel, Rudolf Ladenstein, H. Michel, H. Formanek, I. Sinning and M. Schiffer and has published in prestigious journals such as Nature, The EMBO Journal and Journal of Molecular Biology.

In The Last Decade

O. Epp

27 papers receiving 6.5k citations

Hit Papers

Structure of the protein subunits in the photosynthetic r... 1975 2026 1992 2009 1985 1984 1983 1995 1986 500 1000 1.5k 2.0k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
    1985 2.2k citations J. Deisenhofer, O. Epp et al. Nature profile →
  2. X-ray structure analysis of a membrane protein complex
    1984 1.4k citations J. Deisenhofer, O. Epp et al. Journal of Molecular Biology profile →
  3. The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution
    1983 558 citations O. Epp, Rudolf Ladenstein et al. European Journal of Biochemistry profile →
  4. Crystallographic refinement at 2.3 Å Resolution and Refined Model of the Photosynthetic Reaction Centre fromRhodopseudomonas viridis
    1995 508 citations J. Deisenhofer, O. Epp et al. Journal of Molecular Biology profile →
  5. Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis
    1986 401 citations H. Michel, O. Epp et al. The EMBO Journal profile →
  6. Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution
    1975 226 citations O. Epp, Eaton E. Lattman et al. Biochemistry profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
O. Epp Germany 22 5.4k 1.7k 1.5k 1.1k 680 27 6.9k
D. Mauzerall United States 39 4.2k 0.8× 1.7k 1.0× 766 0.5× 839 0.7× 480 0.7× 127 6.5k
Neil W. Isaacs United Kingdom 46 6.4k 1.2× 1.9k 1.1× 2.4k 1.6× 2.0k 1.8× 567 0.8× 140 9.3k
Miroslav Z. Papiz United Kingdom 26 4.5k 0.8× 1.8k 1.0× 1.4k 1.0× 1.2k 1.1× 387 0.6× 49 6.3k
E. Margoliash United States 54 7.5k 1.4× 1.0k 0.6× 1.0k 0.7× 963 0.8× 502 0.7× 134 10.5k
M. Schiffer United States 43 5.5k 1.0× 990 0.6× 1.0k 0.7× 768 0.7× 495 0.7× 135 6.8k
M. Y. Okamura United States 47 6.3k 1.2× 1.2k 0.7× 3.0k 2.0× 2.0k 1.7× 1.3k 2.0× 117 7.3k
Gordon G. Hammes United States 54 7.2k 1.3× 1.9k 1.1× 760 0.5× 650 0.6× 521 0.8× 241 10.0k
M. R. Gunner United States 42 5.1k 0.9× 1.4k 0.8× 1.9k 1.3× 1.5k 1.3× 654 1.0× 100 6.9k
Christopher C. Moser United States 41 5.8k 1.1× 1.8k 1.0× 1.4k 1.0× 1.3k 1.1× 1.0k 1.5× 95 9.2k
Gerard W. Canters Netherlands 52 5.0k 0.9× 2.3k 1.3× 918 0.6× 413 0.4× 498 0.7× 264 8.8k

Countries citing papers authored by O. Epp

Since Specialization
Citations

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

Fields of papers citing papers by O. Epp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of O. Epp

This figure shows the co-authorship network connecting the top 25 collaborators of O. Epp. A scholar is included among the top collaborators of O. Epp 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 O. Epp. O. Epp 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.
Deisenhofer, J., O. Epp, I. Sinning, & Hartmut Michel. (1995). Crystallographic refinement at 2.3 Å Resolution and Refined Model of the Photosynthetic Reaction Centre fromRhodopseudomonas viridis. Journal of Molecular Biology. 246(3). 429–457. 508 indexed citations breakdown →
2.
Wiegand, Georg, O. Epp, & Robert Huber. (1995). The Crystal Structure of Porcine Pancreatic α-Amylase in Complex with the Microbial Inhibitor Tendamistat. Journal of Molecular Biology. 247(1). 99–110. 112 indexed citations
3.
Braun, Werner, O. Epp, Kurt Wüthrich, & Robert Huber. (1989). Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial model. Journal of Molecular Biology. 206(4). 669–676. 29 indexed citations
4.
Meyer, Emmanuel A., Garry T. Cole, R. Radhakrishnan, & O. Epp. (1988). Structure of native porcine pancreatic elastase at 1.65 Å resolution. Acta Crystallographica Section B Structural Science. 44(1). 26–38. 151 indexed citations
5.
Huber, Robert, Monika Schneider, O. Epp, et al.. (1987). Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. Journal of Molecular Biology. 195(2). 423–434. 148 indexed citations
6.
Michel, H., O. Epp, & J. Deisenhofer. (1986). Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis. The EMBO Journal. 5(10). 2445–2451. 401 indexed citations breakdown →
7.
Deisenhofer, J., O. Epp, Kunio Miki, Robert Huber, & Hartmut Michel. (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution. Nature. 318(6047). 618–624. 2240 indexed citations breakdown →
8.
Bode, Wolfram, O. Epp, Robert Huber, M. Laskowski, & Wojciech Ardelt. (1985). The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). European Journal of Biochemistry. 147(2). 387–395. 110 indexed citations
9.
Epp, O., Rudolf Ladenstein, & Albrecht Wendel. (1983). The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution. European Journal of Biochemistry. 133(1). 51–69. 558 indexed citations breakdown →
10.
Appelt, Krzysztof, Jan Dijk, & O. Epp. (1979). The crystallization of protein BL17 from the 50 S ribosomal subunit of Bacillus stearothermophilus. FEBS Letters. 103(1). 66–70. 18 indexed citations
11.
Huber, Robert, J. Deisenhofer, Peter M. Colman, et al.. (1976). Proceedings: X-ray diffraction analysis of immunoglobulin structure.. PubMed. 357(5). 614–5. 4 indexed citations
12.
Deisenhofer, J., Peter M. Colman, O. Epp, & Robert Huber. (1976). Crystallographic Structural Studies of a Human Fc Fragment. II. A Complete Model Based on a Fourier Map at 3.5 Å Resolution. Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 357(2). 1421–1434. 111 indexed citations
13.
Epp, O., Eaton E. Lattman, M. Schiffer, Robert Huber, & Walter Palm. (1975). Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution. Biochemistry. 14(22). 4943–4952. 226 indexed citations breakdown →
14.
Epp, O., Peter M. Colman, Heinz Fehlhammer, et al.. (1974). Crystal and Molecular Structure of a Dimer Composed of the Variable Portions of the Bence-Jones Protein REI. European Journal of Biochemistry. 45(2). 513–524. 191 indexed citations
15.
Epp, O., Walter Palm, Heinz Fehlhammer, et al.. (1972). Crystallographic evidence for structurally similar domains in the human κ-type Bence-Jones protein Rei. Journal of Molecular Biology. 69(2). 315–318. 5 indexed citations
16.
Epp, O., W. Steigemann, H. Formanek, & Robert Huber. (1971). Crystallographic Evidence for the Tetrameric Subunit Structure of l‐Asparaginase from Escherichia coli. European Journal of Biochemistry. 20(3). 432–437. 49 indexed citations
17.
Huber, Robert, O. Epp, W. Steigemann, & H. Formanek. (1971). The Atomic Structure of Erythrocruorin in the Light of the Chemical Sequence and its Comparison with Myoglobin. European Journal of Biochemistry. 19(1). 42–50. 133 indexed citations
18.
Huber, Robert, et al.. (1970). The basic trypsin inhibitor of bovine pancreas. Die Naturwissenschaften. 57(8). 389–392. 139 indexed citations
19.
Huber, Robert, O. Epp, & H. Formanek. (1969). Aufkl�rung der Molek�lstruktur des Insektenh�moglobins. Die Naturwissenschaften. 56(7). 362–367. 30 indexed citations
20.
Huber, Robert, H. Formanek, & O. Epp. (1968). Kristallstrukturanalyse des Met-Erythrocruorins bei 5,5 � Aufl�sung. Die Naturwissenschaften. 55(2). 75–77. 23 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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