Edith Mihaesco

1.4k total citations
47 papers, 1.1k citations indexed

About

Edith Mihaesco is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Edith Mihaesco has authored 47 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 30 papers in Radiology, Nuclear Medicine and Imaging and 17 papers in Immunology. Recurrent topics in Edith Mihaesco's work include Monoclonal and Polyclonal Antibodies Research (30 papers), Glycosylation and Glycoproteins Research (29 papers) and T-cell and B-cell Immunology (6 papers). Edith Mihaesco is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (30 papers), Glycosylation and Glycoproteins Research (29 papers) and T-cell and B-cell Immunology (6 papers). Edith Mihaesco collaborates with scholars based in France, United States and Tunisia. Edith Mihaesco's co-authors include Maxime Seligmann, Jean‐Louis Preud'homme, D Hurez, F Danon, Constantin Mihaesco, B Frangione, Jean‐Claude Brouet, Blas Frangione, M Séligmann and J C Brouet and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Edith Mihaesco

46 papers receiving 937 citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Edith Mihaesco 475 437 371 247 176 47 1.1k
Peggy Lymberi 387 0.8× 798 1.8× 697 1.9× 68 0.3× 74 0.4× 50 1.4k
S Avraméas 342 0.7× 648 1.5× 632 1.7× 54 0.2× 58 0.3× 30 1.2k
M. Brüggemann 671 1.4× 689 1.6× 921 2.5× 109 0.4× 44 0.3× 24 1.4k
H Mostowski 443 0.9× 1.2k 2.7× 337 0.9× 73 0.3× 124 0.7× 22 1.9k
M. Durm 236 0.5× 1.2k 2.7× 264 0.7× 308 1.2× 250 1.4× 9 1.7k
Nobuyuki Tanigaki 237 0.5× 741 1.7× 424 1.1× 25 0.1× 38 0.2× 48 1.1k
Zoltan A. Nagy 340 0.7× 814 1.9× 412 1.1× 42 0.2× 64 0.4× 45 1.1k
Patricia K. A. Mongini 339 0.7× 1.3k 2.9× 442 1.2× 172 0.7× 124 0.7× 58 1.7k
Michael D. Solga 177 0.4× 556 1.3× 296 0.8× 182 0.7× 154 0.9× 24 1.1k
Pleuni Ooijevaar‐de Heer 432 0.9× 428 1.0× 584 1.6× 70 0.3× 46 0.3× 44 1.2k

Countries citing papers authored by Edith Mihaesco

Since Specialization
Citations

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

Fields of papers citing papers by Edith Mihaesco

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Edith Mihaesco

This figure shows the co-authorship network connecting the top 25 collaborators of Edith Mihaesco. A scholar is included among the top collaborators of Edith Mihaesco 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 Edith Mihaesco. Edith Mihaesco 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.
Silvain, Christine, et al.. (1993). A human myeloma IgA with a hybrid heavy chain resulting from putative somatic gene conversion. European Journal of Immunology. 23(2). 364–368. 5 indexed citations
2.
Mihaesco, Constantin, et al.. (1990). A new extra sequence at the amino terminal of a μ heavy chain disease protein (DAG). Molecular Immunology. 27(8). 771–776. 3 indexed citations
4.
Bentaboulet, M, Edith Mihaesco, Marie‐Claude Gendron, Jean‐Claude Brouet, & Andréas Tsapis. (1989). Genomic alterations in a case of α heavy chain disease leading to the generation of composite exons from the jh region. European Journal of Immunology. 19(11). 2093–2098. 13 indexed citations
5.
Aucouturier, Pièrre, et al.. (1989). Jacalin: A new laboratory tool in immunochemistry and cellular immunology. Journal of Clinical Laboratory Analysis. 3(4). 244–251. 27 indexed citations
6.
Ohbayashi, Hirokazu, et al.. (1989). Structural studies of the asparagine-linked sugar chains of two immunoglobulin M's purified from a patient with Waldenström's macroglobulinemia. Archives of Biochemistry and Biophysics. 269(2). 463–475. 18 indexed citations
7.
Mihaesco, Edith, et al.. (1988). Protein Rou. A human IgA hybrid.. The Journal of Immunology. 140(4). 1236–1238. 3 indexed citations
8.
Aucouturier, Pièrre, et al.. (1988). Jacalin, the human IgA1 and IgD precipitating lectin, also binds IgA2 of both allotypes. Journal of Immunological Methods. 113(2). 185–191. 34 indexed citations
9.
Rudich, Steven M., Edith Mihaesco, Robert Winchester, & Patricia K. A. Mongini. (1987). Analysis of the domain specificity of various murine anti-human IgM monoclonal antibodies differing in human B lymphocyte signaling activity. Molecular Immunology. 24(8). 809–820. 17 indexed citations
10.
Schmitt, Caroline, Koussay Dellagi, Edith Mihaesco, & J C Brouet. (1987). Detection of cross-reactive determinants shared by human monoclonal IgM reacting with myelin-associated glycoprotein.. The Journal of Immunology. 138(5). 1442–1446. 14 indexed citations
11.
Barnikol-Watanabe, Shitsu, et al.. (1984). The Primary Structure of μ-Chain-Disease Protein BOT. Peculiar Amino-Acid Sequence of the N-Terminal 42 Positions. Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 365(1). 105–118. 9 indexed citations
12.
Mariuzza, Roy A., Roberto J. Poljak, Constantin Mihaesco, & Edith Mihaesco. (1983). Crystals of the human heavy chain disease protein riv and human Fc fragment are isomorphous: Further evidence for conformational flexibility in the hinge region of immunoglobulins. Journal of Molecular Biology. 165(3). 559–561. 7 indexed citations
13.
Městecký, Jiří, J L Preud'homme, S. S. Crago, et al.. (1980). Presence of J chain in human lymphoid cells.. PubMed Central. 39(2). 371–85. 39 indexed citations
14.
Mihaesco, Constantin, et al.. (1976). Physicochemical and immunological properties of a μ chain disease protein. Immunochemistry. 13(1). 39–45. 14 indexed citations
15.
Seligmann, Maxime & Edith Mihaesco. (1974). Current Knowledge on Alpha Chain Disease. PubMed. 45(0). 365–372. 1 indexed citations
16.
Wolfenstein‐Todel, Carlota, Edith Mihaesco, & Blas Frangione. (1974). “Alpha Chain Disease” Protein Def: Internal Deletion of a Human Immunoglobulin A 1 Heavy Chain. Proceedings of the National Academy of Sciences. 71(3). 974–978. 31 indexed citations
17.
Segond, P, et al.. (1973). [Alpha heavy chain disease. Apropos of a case].. PubMed. 12(3). 333–49. 1 indexed citations
18.
Frangione, Blas, et al.. (1971). Structure of immunoglobulin A. I. Interchain disulfide bridges of a γAl myeloma protein. Biochemistry. 10(22). 4140–4145. 27 indexed citations
19.
Frangione, B, et al.. (1971). STRUCTURAL STUDIES OF IMMUNOGLOBULIN G, M AND A HEAVY CHAINS. Annals of the New York Academy of Sciences. 190(1). 71–82. 9 indexed citations
20.
Rambaud, J C, Claude Matuchansky, C Bognel, et al.. (1970). [A further case of alpha chain disease in a Eurasian].. PubMed. 121(2). 135–48. 11 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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