M. Egger

641 total citations
8 papers, 520 citations indexed

About

M. Egger is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, M. Egger has authored 8 papers receiving a total of 520 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 5 papers in Atomic and Molecular Physics, and Optics and 3 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in M. Egger's work include Lipid Membrane Structure and Behavior (7 papers), Force Microscopy Techniques and Applications (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). M. Egger is often cited by papers focused on Lipid Membrane Structure and Behavior (7 papers), Force Microscopy Techniques and Applications (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). M. Egger collaborates with scholars based in Germany and United States. M. Egger's co-authors include S. P. Heyn, S. A. C. Gould, F. Ohnesorge, H. E. Gaub, Hermann E. Gaub, B. Drake, Paul K. Hansma, A. L. Weisenhorn, Craig Prater and H. E. Gaub and has published in prestigious journals such as Langmuir, The Journal of Physical Chemistry and Biophysical Journal.

In The Last Decade

M. Egger

8 papers receiving 501 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M. Egger Germany	8	369	289	144	108	44	8	520
S. P. Heyn Germany	9	375 1.0×	307 1.1×	156 1.1×	108 1.0×	45 1.0×	9	544
Robert Walder United States	15	250 0.7×	264 0.9×	101 0.7×	148 1.4×	25 0.6×	22	577
Mike J. Allen United States	6	258 0.7×	163 0.6×	128 0.9×	107 1.0×	35 0.8×	9	471
Chun Tang China	5	431 1.2×	267 0.9×	194 1.3×	196 1.8×	27 0.6×	8	658
R. Blankenburg Germany	5	206 0.6×	366 1.3×	265 1.8×	110 1.0×	231 5.3×	6	631
P. Meller Germany	9	227 0.6×	405 1.4×	280 1.9×	109 1.0×	236 5.4×	11	701
Keita Mitsui Japan	9	169 0.5×	165 0.6×	143 1.0×	179 1.7×	28 0.6×	21	435
Frank Zaugg Switzerland	7	147 0.4×	189 0.7×	187 1.3×	154 1.4×	31 0.7×	9	441
Chad Ray United States	10	281 0.8×	106 0.4×	139 1.0×	42 0.4×	35 0.8×	13	377
H. Wang United States	9	344 0.9×	229 0.8×	113 0.8×	89 0.8×	55 1.3×	20	519

Countries citing papers authored by M. Egger

Since Specialization

Citations

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

Fields of papers citing papers by M. Egger

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Egger

This figure shows the co-authorship network connecting the top 25 collaborators of M. Egger. A scholar is included among the top collaborators of M. Egger 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 M. Egger. M. Egger is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

8 of 8 papers shown

1.

Fischer, Birgit, S. P. Heyn, M. Egger, & H. E. Gaub. (1993). Antigen binding to a pattern of lipid-anchored antibody binding sites measured by surface plasmon microscopy. Langmuir. 9(1). 136–140. 37 indexed citations

2.

Egger, M., S. P. Heyn, & Hermann E. Gaub. (1992). Synthetic lipid-anchored receptors based on the binding site of a monoclonal antibody. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1104(1). 45–54. 23 indexed citations

3.

Heyn, S. P., Ralf W. Tillmann, M. Egger, & Hermann E. Gaub. (1991). A miniaturized micro-fluorescence film balance for protein-containing lipid monolayers spread from a vesicle suspension. Journal of Biochemical and Biophysical Methods. 22(2). 145–158. 18 indexed citations

4.

Egger, M., F. Ohnesorge, S. A. C. Gould, et al.. (1991). Molecular-resolution images of Langmuir-Blodgett films and DNA by atomic force microscopy. Langmuir. 7(1). 8–12. 148 indexed citations

5.

Weisenhorn, A. L., B. Drake, Craig Prater, et al.. (1990). Immobilized proteins in buffer imaged at molecular resolution by atomic force microscopy. Biophysical Journal. 58(5). 1251–1258. 146 indexed citations

6.

Heyn, S. P., M. Egger, & H. E. Gaub. (1990). Lipid and lipid-protein monolayers spread from a vesicle suspension: a microfluorescence film balance study. The Journal of Physical Chemistry. 94(12). 5073–5078. 40 indexed citations

7.

Egger, M., S. P. Heyn, & Hermann E. Gaub. (1990). Two-dimensional recognition pattern of lipid-anchored Fab' fragments. Biophysical Journal. 57(3). 669–673. 26 indexed citations

8.

Egger, M., F. Ohnesorge, A. L. Weisenhorn, et al.. (1990). Wet lipid-protein membranes imaged at submolecular resolution by atomic force microscopy. Journal of Structural Biology. 103(1). 89–94. 82 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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