Fred Karush

4.8k total citations
95 papers, 3.0k citations indexed

About

Fred Karush is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Fred Karush has authored 95 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 61 papers in Molecular Biology, 54 papers in Radiology, Nuclear Medicine and Imaging and 18 papers in Immunology. Recurrent topics in Fred Karush's work include Monoclonal and Polyclonal Antibodies Research (54 papers), Glycosylation and Glycoproteins Research (28 papers) and Protein purification and stability (25 papers). Fred Karush is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (54 papers), Glycosylation and Glycoproteins Research (28 papers) and Protein purification and stability (25 papers). Fred Karush collaborates with scholars based in United States, Italy and Austria. Fred Karush's co-authors include Norman R. Klinman, S Utsumi, Gabor Markus, P. Gopalakrishnan, Herman N. Eisen, John D. Rodwell, John H. Rockey, Robert Marks, Asoke C. Ghose and Patricia J. Gearhart and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Fred Karush

94 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Fred Karush United States 31 1.7k 1.3k 622 236 215 95 3.0k
Myron J. Waxdal United States 23 1.7k 1.0× 739 0.6× 932 1.5× 151 0.6× 188 0.9× 49 2.9k
Dietmar G. Braun Switzerland 29 1.3k 0.7× 742 0.6× 703 1.1× 146 0.6× 113 0.5× 103 2.6k
Roald Nezlin Israel 20 1.1k 0.6× 672 0.5× 888 1.4× 152 0.6× 182 0.8× 69 2.4k
Brigitte A. Askonas Tanzania 39 1.6k 0.9× 1.3k 1.0× 2.7k 4.3× 211 0.9× 169 0.8× 92 5.2k
Jean‐Claude Jaton Switzerland 27 1.2k 0.7× 950 0.7× 810 1.3× 166 0.7× 142 0.7× 93 2.0k
Malcolm L. Gefter United States 42 3.8k 2.2× 1.4k 1.1× 1.7k 2.7× 150 0.6× 134 0.6× 68 5.9k
Stephen C. Kinsky United States 35 2.2k 1.3× 333 0.3× 650 1.0× 78 0.3× 245 1.1× 72 3.4k
G. L. Ada Australia 31 876 0.5× 539 0.4× 1.1k 1.8× 120 0.5× 170 0.8× 80 2.8k
Jonathan M. Gershoni Israel 30 2.6k 1.5× 1.1k 0.9× 686 1.1× 80 0.3× 321 1.5× 87 4.1k
Paul P. Trotta United States 29 1.3k 0.8× 491 0.4× 1.4k 2.3× 105 0.4× 115 0.5× 75 3.5k

Countries citing papers authored by Fred Karush

Since Specialization
Citations

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

Fields of papers citing papers by Fred Karush

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Fred Karush

This figure shows the co-authorship network connecting the top 25 collaborators of Fred Karush. A scholar is included among the top collaborators of Fred Karush 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 Fred Karush. Fred Karush 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.
Andrews, Glenn C., et al.. (1992). Primary B-cell response to neuropeptide Y and bovine pancreatic polypeptide. Molecular Immunology. 29(7-8). 847–856. 9 indexed citations
2.
Cariello, Lucio, Pauline T. Velasco, J. H. P. Wilson, et al.. (1990). Probing the transglutaminase-mediated, posttranslational modification of proteins during development. Biochemistry. 29(21). 5103–5108. 19 indexed citations
3.
Udaka, Keiko, et al.. (1990). Bacterial expression of immunoglobulin VH proteins. Molecular Immunology. 27(1). 25–35. 7 indexed citations
4.
Ghose, Asoke C. & Fred Karush. (1988). Induction of polyclonal and monoclonal antibody responses to cholera toxin by the synthetic peptide approach. Molecular Immunology. 25(3). 223–230. 11 indexed citations
5.
Velasco, Pauline T., Fred Karush, & L. Lóránd. (1988). Transamidating activities of factor XIIIa and of transglutaminases, measured by an Elisa procedure. Biochemical and Biophysical Research Communications. 152(2). 505–511. 17 indexed citations
6.
Goodgal, Sol H., et al.. (1987). Germ-line affinity and germ-line variable-region genes in the B cell response.. The Journal of Immunology. 138(4). 1281–1288. 27 indexed citations
7.
Karush, Fred, et al.. (1984). Attachment of immunoglobulin to liposomal membrane via protein carbohydrate. Biochimica et Biophysica Acta (BBA) - General Subjects. 800(3). 291–300. 53 indexed citations
8.
Rodwell, John D., Patricia J. Gearhart, & Fred Karush. (1983). Restriction in IgM expression. IV. Affinity analysis of monoclonal anti-phosphorylcholine antibodies.. The Journal of Immunology. 130(1). 313–316. 67 indexed citations
9.
Sinha, Devarpita & Fred Karush. (1978). The Inhibition of the Mixed Lymphocyte Culture Reaction by Cyclic Adenosine 3',5'-Monophosphate. Experimental Biology and Medicine. 158(4). 590–594. 1 indexed citations
10.
Pilz, Ingrid, O. Kratky, & Fred Karush. (1974). Changes of the Conformation of Rabbit IgG Antibody Caused by the Specific Binding of a Hapten. European Journal of Biochemistry. 41(1). 91–96. 41 indexed citations
11.
Karush, Fred, et al.. (1973). Multivalence and Affinity of Antibody. International Archives of Allergy and Immunology. 45(1-2). 130–132. 5 indexed citations
12.
Klinman, Norman R., et al.. (1966). Equine Anti-Hapten Antibody. The Journal of Immunology. 96(4). 587–595. 42 indexed citations
13.
Fujio, Hajime & Fred Karush. (1966). Antibody Affinity. II. Effect of Immunization Interval on Antihapten Antibody in the Rabbit*. Biochemistry. 5(6). 1856–1863. 38 indexed citations
14.
Karush, Fred, et al.. (1965). EQUINE ANTIHAPTEN ANTIBODY II. THE GAMMA-G(7S-GAMMA) COMPONENTS AND THEIR SPECIFIC INTERACTION.. PubMed. 47. 51–60. 11 indexed citations
15.
Rockey, John H., Norman R. Klinman, & Fred Karush. (1964). EQUINE ANTIHAPTEN ANTIBODY. The Journal of Experimental Medicine. 120(4). 589–609. 53 indexed citations
16.
Karush, Fred, Norman R. Klinman, & Robert Marks. (1964). An assay method for disulfide groups by fluorescence quenching. Analytical Biochemistry. 9(1). 100–114. 110 indexed citations
17.
Óváry, Zoltán & Fred Karush. (1961). Studies on the Immunologic Mechanism of Anaphylaxis. The Journal of Immunology. 86(2). 146–150. 34 indexed citations
18.
Óváry, Zoltán & Fred Karush. (1960). Studies on the Immunologic Mechanism of Anaphylaxis,. The Journal of Immunology. 84(4). 409–415. 6 indexed citations
19.
Karush, Fred & Robert Marks. (1957). The Preparation and Properties of Purified Anti-Hapten Antibody. The Journal of Immunology. 78(4). 296–303. 27 indexed citations
20.
Karush, Fred. (1954). The Interaction of Optically Isomeric Dyes with Human Serum Albumin1. Journal of the American Chemical Society. 76(21). 5536–5542. 28 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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