Alfred F. Esser

1.3k total citations
31 papers, 1.0k citations indexed

About

Alfred F. Esser is a scholar working on Molecular Biology, Immunology and Physiology. According to data from OpenAlex, Alfred F. Esser has authored 31 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 18 papers in Immunology and 7 papers in Physiology. Recurrent topics in Alfred F. Esser's work include Complement system in diseases (13 papers), Lipid Membrane Structure and Behavior (10 papers) and Erythrocyte Function and Pathophysiology (6 papers). Alfred F. Esser is often cited by papers focused on Complement system in diseases (13 papers), Lipid Membrane Structure and Behavior (10 papers) and Erythrocyte Function and Pathophysiology (6 papers). Alfred F. Esser collaborates with scholars based in United States, France and Australia. Alfred F. Esser's co-authors include Hans J. Müller‐Eberhard, Richard M. Bartholomew, Philippe Lesavre, Tony E. Hugli, Roney O. Laine, Kenneth A. Souza, John R. Dankert, Janos Κ. Lanyi, Nicole M. Thielens and Gérard J. Arlaud and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Alfred F. Esser

31 papers receiving 971 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alfred F. Esser United States 20 569 397 209 161 124 31 1.0k
Alan Munro United Kingdom 23 1.1k 1.9× 631 1.6× 158 0.8× 134 0.8× 119 1.0× 68 1.9k
Sadaaki Iwanaga Japan 16 353 0.6× 467 1.2× 240 1.1× 49 0.3× 268 2.2× 23 1.2k
J. Michael Kehoe United States 17 419 0.7× 602 1.5× 193 0.9× 113 0.7× 69 0.6× 47 1.2k
A. S. Kelus United Kingdom 21 651 1.1× 675 1.7× 233 1.1× 105 0.7× 86 0.7× 48 1.5k
Felix Haurowitz United States 19 393 0.7× 480 1.2× 84 0.4× 71 0.4× 48 0.4× 90 1.2k
Hiroshi Amanuma Japan 21 304 0.5× 852 2.1× 192 0.9× 162 1.0× 66 0.5× 67 1.6k
Masaharu Naiki Japan 24 450 0.8× 1.2k 3.1× 185 0.9× 326 2.0× 31 0.3× 71 1.8k
J. Pye Australia 16 915 1.6× 401 1.0× 91 0.4× 82 0.5× 38 0.3× 23 1.6k
G Medgyesi Hungary 15 191 0.3× 467 1.2× 93 0.4× 57 0.4× 28 0.2× 59 846
Jean‐Claude Jaton Switzerland 27 810 1.4× 1.2k 3.0× 166 0.8× 105 0.7× 56 0.5× 93 2.0k

Countries citing papers authored by Alfred F. Esser

Since Specialization
Citations

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

Fields of papers citing papers by Alfred F. Esser

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Alfred F. Esser. 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 Alfred F. Esser. The network helps show where Alfred F. Esser may publish in the future.

Co-authorship network of co-authors of Alfred F. Esser

This figure shows the co-authorship network connecting the top 25 collaborators of Alfred F. Esser. A scholar is included among the top collaborators of Alfred F. Esser 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 Alfred F. Esser. Alfred F. Esser 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.
Rossi, Véronique, Yunxia Wang, & Alfred F. Esser. (2010). Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification. Molecular Immunology. 47(7-8). 1553–1560. 6 indexed citations
2.
Wang, Yunxia, Edward S. Bjes, & Alfred F. Esser. (2000). Molecular Aspects of Complement-mediated Bacterial Killing. Journal of Biological Chemistry. 275(7). 4687–4692. 22 indexed citations
3.
Thielens, Nicole M., Monique Lacroix, Michel Jaquinod, et al.. (1999). The N-terminal CUB-Epidermal Growth Factor Module Pair of Human Complement Protease C1r Binds Ca2+ with High Affinity and Mediates Ca2+-dependent Interaction with C1s. Journal of Biological Chemistry. 274(14). 9149–9159. 50 indexed citations
4.
Rossi, Véronique, Isabelle Bally, Nicole M. Thielens, Alfred F. Esser, & Gérard J. Arlaud. (1998). Baculovirus-mediated Expression of Truncated Modular Fragments from the Catalytic Region of Human Complement Serine Protease C1s. Journal of Biological Chemistry. 273(2). 1232–1239. 65 indexed citations
5.
Esser, Alfred F., et al.. (1996). Horse complement protein C9: Primary structure and cytotoxic activity. Molecular Immunology. 33(7-8). 725–733. 2 indexed citations
6.
Esser, Alfred F.. (1994). The membrane attack complex of complement. Assembly, structure and cytotoxic activity. Toxicology. 87(1-3). 229–247. 94 indexed citations
7.
Tomlinson, Stephen, Keith K. Stanley, & Alfred F. Esser. (1993). Domain structure, functional activity, and polymerization of trout complement protein C9. Developmental & Comparative Immunology. 17(1). 67–76. 39 indexed citations
8.
Esser, Alfred F.. (1991). Big MAC attack: complement proteins cause leaky patches. Immunology Today. 12(9). 316–318. 72 indexed citations
9.
Lohner, Karl & Alfred F. Esser. (1991). Thermal unfolding and aggregation of human complement protein C9: a differential scanning calorimetry study. Biochemistry. 30(26). 6620–6625. 30 indexed citations
10.
Laine, Roney O. & Alfred F. Esser. (1989). Detection of refolding conformers of complement protein C9 during insertion into membranes. Nature. 341(6237). 63–65. 30 indexed citations
11.
Laine, Roney O., B. Paul Morgan, & Alfred F. Esser. (1988). Comparison between complement and melittin hemolysis: anti-melittin antibodies inhibit complement lysis. Biochemistry. 27(14). 5308–5314. 40 indexed citations
12.
Parce, J. Wallace, Harden M. McConnell, Richard M. Bartholomew, & Alfred F. Esser. (1980). Kinetics of antibody-dependent activation of the first component of complement on lipid bilayer membranes. Biochemical and Biophysical Research Communications. 93(1). 235–242. 7 indexed citations
13.
Podack, Eckhard R., William P. Kolb, Alfred F. Esser, & Hans J. Müller‐Eberhard. (1979). Structural Similarities between C6 and C7 of Human Complement. The Journal of Immunology. 123(3). 1071–1077. 59 indexed citations
14.
Russell, Stephen W. & Alfred F. Esser. (1979). Activated macrophages kill tumor cells independent of membrane fluidity. Biochemical and Biophysical Research Communications. 89(2). 520–525. 3 indexed citations
15.
Bartholomew, Richard M., Eckhard R. Podack, & Alfred F. Esser. (1979). Quantitation of the membrane attack complex of complement in an air-driven ultracentrifuge. Journal of Immunological Methods. 31(3-4). 351–360. 1 indexed citations
16.
Esser, Alfred F., et al.. (1978). Temperature‐dependent morphological changes in membranes of bacillus stearothermophilus. Journal of Supramolecular Structure. 8(2). 129–138. 10 indexed citations
17.
Bartholomew, Richard M. & Alfred F. Esser. (1977). The First Complement Component: Evidence for an Equilibrium between C1s Free in Serum and C1s Bound in the C1 Complex. The Journal of Immunology. 119(6). 1916–1922. 31 indexed citations
18.
Esser, Alfred F. & Kenneth A. Souza. (1974). Correlation between Thermal Death and Membrane Fluidity in Bacillus stearothermophilus. Proceedings of the National Academy of Sciences. 71(10). 4111–4115. 47 indexed citations
19.
Esser, Alfred F.. (1974). ELECTRON PARAMAGNETIC RESONANCE SIGNAL II IN SPINACH CHLOROPLASTS—II. INFLUENCE OF PHOSPHORYLATION AND ELECTRON‐TRANSPORT INHIBITORS. Photochemistry and Photobiology. 20(2). 173–181. 8 indexed citations
20.
Esser, Alfred F. & Janos Κ. Lanyi. (1973). Structure of the lipid phase in cell envelope vesicles from Halobacterium cutirubrum. Biochemistry. 12(10). 1933–1939. 48 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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