Jeffrey A. Mattis

1.6k total citations
25 papers, 1.2k citations indexed

About

Jeffrey A. Mattis is a scholar working on Radiology, Nuclear Medicine and Imaging, Molecular Biology and Oncology. According to data from OpenAlex, Jeffrey A. Mattis has authored 25 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Radiology, Nuclear Medicine and Imaging, 8 papers in Molecular Biology and 6 papers in Oncology. Recurrent topics in Jeffrey A. Mattis's work include Radiopharmaceutical Chemistry and Applications (10 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and Medical Imaging Techniques and Applications (3 papers). Jeffrey A. Mattis is often cited by papers focused on Radiopharmaceutical Chemistry and Applications (10 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and Medical Imaging Techniques and Applications (3 papers). Jeffrey A. Mattis collaborates with scholars based in United States, Belgium and Italy. Jeffrey A. Mattis's co-authors include M. Laskowski, Gene A. Homandberg, Zenon Steplewski, Hilary Koprowski, Dorothee Herlyn, Carolyn S. Ernst, Barbara Atkinson, P Häyry, H. William Strausś and David J. Shealy and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Lancet and Journal of Biological Chemistry.

In The Last Decade

Jeffrey A. Mattis

23 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jeffrey A. Mattis United States 15 634 540 261 157 134 25 1.2k
Koon Y. Pak United States 22 501 0.8× 594 1.1× 182 0.7× 215 1.4× 70 0.5× 77 1.3k
K.M. Barone United States 8 190 0.3× 634 1.2× 139 0.5× 415 2.6× 72 0.5× 10 1.3k
Marc Van Regenmortel France 8 704 1.1× 797 1.5× 308 1.2× 523 3.3× 31 0.2× 9 1.6k
Shannon Marshall United States 21 250 0.4× 726 1.3× 320 1.2× 283 1.8× 32 0.2× 40 1.2k
Jacquin Jones United States 8 359 0.6× 212 0.4× 449 1.7× 390 2.5× 255 1.9× 10 1.1k
Claudia De Lorenzo Italy 29 589 0.9× 929 1.7× 897 3.4× 430 2.7× 426 3.2× 88 2.1k
Alicia V. Palleroni United States 14 270 0.4× 435 0.8× 262 1.0× 324 2.1× 15 0.1× 19 1.1k
Rachel Kroe‐Barrett United States 19 311 0.5× 654 1.2× 107 0.4× 231 1.5× 72 0.5× 34 1.1k
Raymond T. Camphausen United States 21 252 0.4× 1.1k 2.0× 268 1.0× 658 4.2× 105 0.8× 27 2.3k
Mark P. O'Connell United States 10 380 0.6× 671 1.2× 125 0.5× 168 1.1× 25 0.2× 10 951

Countries citing papers authored by Jeffrey A. Mattis

Since Specialization
Citations

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

Fields of papers citing papers by Jeffrey A. Mattis

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jeffrey A. Mattis. 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 Jeffrey A. Mattis. The network helps show where Jeffrey A. Mattis may publish in the future.

Co-authorship network of co-authors of Jeffrey A. Mattis

This figure shows the co-authorship network connecting the top 25 collaborators of Jeffrey A. Mattis. A scholar is included among the top collaborators of Jeffrey A. Mattis 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 Jeffrey A. Mattis. Jeffrey A. Mattis 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.
Vangestel, Christel, Leonie Wyffels, Tim Van den Wyngaert, et al.. (2023). First-in-human study of a novel cell death tracer [99mTc]Tc-Duramycin: safety, biodistribution and radiation dosimetry in healthy volunteers. EJNMMI Radiopharmacy and Chemistry. 8(1). 20–20.
2.
Chaudhry, Farhan, Hideki Kawai, Kipp W. Johnson, et al.. (2020). Molecular Imaging of Apoptosis in Atherosclerosis by Targeting Cell Membrane Phospholipid Asymmetry. Journal of the American College of Cardiology. 76(16). 1862–1874. 21 indexed citations
3.
Woo, David, et al.. (2015). Auger Electron Damage Induced by Radioiodinated Iodine-125 Monoclonal Antibodies. Frontiers of radiation therapy and oncology. 24. 47–63.
4.
Hudacek, Andrew W., Fetweh H. Al‐Saleem, Travis Eisemann, et al.. (2014). Recombinant rabies virus particles presenting botulinum neurotoxin antigens elicit a protective humoral response in vivo. Molecular Therapy — Methods & Clinical Development. 1. 14046–14046. 9 indexed citations
5.
Paudyal, Bishnuhari, Chang-Po Chen, Edith P. Mitchell, et al.. (2013). Determining efficacy of breast cancer therapy by PET imaging of HER2 mRNA. Nuclear Medicine and Biology. 40(8). 994–999. 12 indexed citations
7.
Faber, Mirko, et al.. (2004). In vitro growth and stability of recombinant rabies viruses designed for vaccination of wildlife. Vaccine. 23(4). 518–524. 36 indexed citations
8.
Pak, Koon Y., Mark Nedelman, Ban An Khaw, et al.. (1992). An instant kit method for labeling antimyosin Fab' with technetium-99m: evaluation in an experimental myocardial infarct model.. PubMed. 33(1). 144–9. 16 indexed citations
9.
Johnson, Lynne L., David W. Seldin, Lewis C. Becker, et al.. (1989). Antimyosin imaging in acute transmural myocardial infarctions: Results of a multicenter clinical trial. Journal of the American College of Cardiology. 13(1). 27–35. 79 indexed citations
10.
Dean, Richard T., et al.. (1989). Practical considerations in the production, purification, and formulation of monoclonal antibodies for immunoscintigraphy and immunotherapy. Seminars in Nuclear Medicine. 19(3). 202–220. 15 indexed citations
11.
Woo, David, Derui Li, Jeffrey A. Mattis, & Zenon Steplewski. (1989). Selective chromosomal damage and cytotoxicity of 125I-labeled monoclonal antibody 17-1a in human cancer cells.. PubMed. 49(11). 2952–8. 51 indexed citations
12.
Woo, David, Arnold M. Markoe, Luther W. Brady, et al.. (1988). Monoclonal Antibodies for Use in Radiotherapy and Diagnosis. American Journal of Clinical Oncology. 11(3). 355–361. 7 indexed citations
13.
Hnatowich, D.J., Maurissa Gionet, Mary Rusckowski, et al.. (1987). Pharmacokinetics of 111In-labeled OC-125 antibody in cancer patients compared with the 19-9 antibody.. PubMed. 47(22). 6111–7. 30 indexed citations
14.
Hnatowich, D.J., Thomas W. Griffin, Mary Rusckowski, et al.. (1985). Pharmacokinetics of an indium-111-labeled monoclonal antibody in cancer patients.. PubMed. 26(8). 849–58. 110 indexed citations
15.
Khaw, Ban-An, et al.. (1984). Monoclonal Antibody to Cardiac Myosin: Imaging of Experimental Myocardial Infarction. Hybridoma. 3(1). 11–23. 124 indexed citations
16.
Mattis, Jeffrey A., et al.. (1979). Interaction of papain with derivatives of phenylalanylglycinal: fluorescence studies.. Proceedings of the National Academy of Sciences. 76(3). 1131–1134. 11 indexed citations
17.
Homandberg, Gene A., Jeffrey A. Mattis, & M. Laskowski. (1978). Synthesis of peptide bonds by proteinases. Addition of organic cosolvents shifts peptide bond equilibriums toward synthesis. Biochemistry. 17(24). 5220–5227. 196 indexed citations
18.
Mattis, Jeffrey A., et al.. (1977). Interaction of papain with derivatives of phenylalanylglycinal.. Journal of Biological Chemistry. 252(19). 6776–6782. 14 indexed citations
19.
Mattis, Jeffrey A. & Joseph S. Fruton. (1976). Kinetics of the action of papain on fluorescent peptide substrates. Biochemistry. 15(10). 2191–2194. 24 indexed citations
20.
Mattis, Jeffrey A. & M. Laskowski. (1973). pH dependence of the equilibrium constant for the hydrolysis of the Arg63-Ile reactive-site peptide bond in soybean trypsin inhibitor (Kunitz). Biochemistry. 12(12). 2239–2245. 33 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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