John S. Babcook

1.9k total citations
18 papers, 927 citations indexed

About

John S. Babcook is a scholar working on Molecular Biology, Oncology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, John S. Babcook has authored 18 papers receiving a total of 927 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 6 papers in Oncology and 6 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in John S. Babcook's work include Monoclonal and Polyclonal Antibodies Research (6 papers), Glycosylation and Glycoproteins Research (4 papers) and T-cell and B-cell Immunology (4 papers). John S. Babcook is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (6 papers), Glycosylation and Glycoproteins Research (4 papers) and T-cell and B-cell Immunology (4 papers). John S. Babcook collaborates with scholars based in Canada, United States and Australia. John S. Babcook's co-authors include Palaniswami Rathanaswami, Luís Borges, Lara Stepan, Claire L. Sutherland, Esther S. Trueblood, Kari Hale, Kevin B. Leslie, John W. Schrader, Gary R. Fanger and Steven G. Reed and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Immunology and Cancer Research.

In The Last Decade

John S. Babcook

17 papers receiving 897 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John S. Babcook Canada 13 361 276 249 230 164 18 927
Brian Cao United States 17 638 1.8× 381 1.4× 230 0.9× 135 0.6× 92 0.6× 37 1.2k
Amy Ly United States 16 291 0.8× 231 0.8× 182 0.7× 149 0.6× 225 1.4× 63 1.1k
Silvia Behnke Switzerland 17 508 1.4× 251 0.9× 234 0.9× 62 0.3× 364 2.2× 24 1.2k
Stefan Störkel Germany 16 429 1.2× 379 1.4× 255 1.0× 79 0.3× 539 3.3× 30 1.2k
Claudia I. Vidal United States 13 408 1.1× 310 1.1× 167 0.7× 85 0.4× 58 0.4× 45 834
Derek Atkins Germany 20 568 1.6× 544 2.0× 299 1.2× 98 0.4× 478 2.9× 27 1.5k
Gary A. Pestano United States 12 502 1.4× 230 0.8× 481 1.9× 70 0.3× 153 0.9× 41 1.0k
Kelly McGlinchey United States 15 248 0.7× 603 2.2× 149 0.6× 134 0.6× 258 1.6× 30 1.1k
George R. Gunn United States 11 432 1.2× 475 1.7× 151 0.6× 379 1.6× 547 3.3× 21 1.3k
Michael A. Linden United States 20 562 1.6× 306 1.1× 133 0.5× 57 0.2× 165 1.0× 88 1.3k

Countries citing papers authored by John S. Babcook

Since Specialization
Citations

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

Fields of papers citing papers by John S. Babcook

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John S. Babcook. 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 John S. Babcook. The network helps show where John S. Babcook may publish in the future.

Co-authorship network of co-authors of John S. Babcook

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

All Works

18 of 18 papers shown
1.
Tran, Anh, et al.. (2023). Multivalent IgM scaffold enhances the therapeutic potential of variant-agnostic ACE2 decoys against SARS-CoV-2. mAbs. 15(1). 2212415–2212415. 5 indexed citations
2.
Babcook, John S., et al.. (2018). A novel drug conjugate platform: Redefining the therapeutic window for ADCs. Annals of Oncology. 29. iii6–iii6. 1 indexed citations
3.
Hamblett, Kevin J., R. H. Davies, Grant Wickman, et al.. (2018). Abstract 3914: ZW49, a HER2-targeted biparatopic antibody-drug conjugate for the treatment of HER2-expressing cancers. Cancer Research. 78(13_Supplement). 3914–3914. 37 indexed citations
4.
Babcook, John S., et al.. (2017). Abstract 61: Zymelink drug conjugate platform: redefining the therapeutic window for ADCs. Cancer Research. 77(13_Supplement). 61–61. 2 indexed citations
5.
Seiler, Roland, Htoo Zarni Oo, Thomas Mandel Clausen, et al.. (2016). 927 Effective treatment of cisplatin-resistant bladder cancer using a glycosaminoglycan binding malaria protein. European Urology Supplements. 15(3). e927–e927. 1 indexed citations
6.
Snyder, Kimberly, Michael R. Hughes, Peter Bergqvist, et al.. (2015). Podocalyxin enhances breast tumor growth and metastasis and is a target for monoclonal antibody therapy. Breast Cancer Research. 17(1). 46–46. 56 indexed citations
7.
Zhang, Ming, Gang Yu, Joshua T. Pearson, et al.. (2015). Interleukin‐21 Receptor Blockade Inhibits Secondary Humoral Responses and Halts the Progression of Preestablished Disease in the (NZB × NZW)F1 Systemic Lupus Erythematosus Model. Arthritis & Rheumatology. 67(10). 2723–2731. 28 indexed citations
8.
Bergqvist, Peter, Alireza Heravi‐Moussavi, Edie Dullaghan, et al.. (2014). A Pan-Cancer Analysis of Alternative Splicing Events Reveals Novel Tumor-Associated Splice Variants of Matriptase. Cancer Informatics. 13. CIN.S19435–CIN.S19435. 10 indexed citations
9.
Stepan, Lara, Esther S. Trueblood, Kari Hale, et al.. (2011). Expression of Trop2 Cell Surface Glycoprotein in Normal and Tumor Tissues. Journal of Histochemistry & Cytochemistry. 59(7). 701–710. 179 indexed citations
10.
Coughlin, Melissa M., John S. Babcook, & Bellur S. Prabhakar. (2009). Human monoclonal antibodies to SARS-coronavirus inhibit infection by different mechanisms. Virology. 394(1). 39–46. 24 indexed citations
11.
Rathanaswami, Palaniswami, John S. Babcook, & Michael Gallo. (2007). High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Analytical Biochemistry. 373(1). 52–60. 19 indexed citations
12.
Coughlin, Melissa M., Osvaldo Martinez, Ole Olsen, et al.. (2006). Generation and characterization of human monoclonal neutralizing antibodies with distinct binding and sequence features against SARS coronavirus using XenoMouse®. Virology. 361(1). 93–102. 51 indexed citations
13.
McLean, Gary R., Ole Olsen, Ian N. Watt, et al.. (2005). Recognition of Human Cytomegalovirus by Human Primary Immunoglobulins Identifies an Innate Foundation to an Adaptive Immune Response. The Journal of Immunology. 174(8). 4768–4778. 36 indexed citations
14.
Rathanaswami, Palaniswami, Shelly Roalstad, Lorin Roskos, et al.. (2005). Demonstration of an in vivo generated sub-picomolar affinity fully human monoclonal antibody to interleukin-8. Biochemical and Biophysical Research Communications. 334(4). 1004–1013. 36 indexed citations
15.
Fanger, Gary R., Raymond L. Houghton, Marc W. Retter, et al.. (2002). Detection of Mammaglobin in the Sera of Patients with Breast Cancer. Tumor Biology. 23(4). 212–221. 27 indexed citations
16.
Jiang, Zhong, Bruce A. Woda, Kenneth L. Rock, et al.. (2001). P504S. The American Journal of Surgical Pathology. 25(11). 1397–1404. 295 indexed citations
17.
Babcook, John S., Kevin B. Leslie, Odd‐Arne Olsen, Ruth A. Salmon, & John W. Schrader. (1996). A novel strategy for generating monoclonal antibodies from single, isolated lymphocytes producing antibodies of defined specificities.. Proceedings of the National Academy of Sciences. 93(15). 7843–7848. 107 indexed citations
18.
Babcook, John S., Julian D. Watts, Ruedi Aebersold, & Hermann J. Ziltener. (1991). Automated nonisotopic assay for protein-tyrosine kinase and protein-tyrosine phosphatase activities. Analytical Biochemistry. 196(2). 245–251. 13 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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