John E. Schiel

1.8k total citations
46 papers, 1.2k citations indexed

About

John E. Schiel is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Spectroscopy. According to data from OpenAlex, John E. Schiel has authored 46 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 21 papers in Radiology, Nuclear Medicine and Imaging and 11 papers in Spectroscopy. Recurrent topics in John E. Schiel's work include Protein purification and stability (26 papers), Monoclonal and Polyclonal Antibodies Research (21 papers) and Viral Infectious Diseases and Gene Expression in Insects (10 papers). John E. Schiel is often cited by papers focused on Protein purification and stability (26 papers), Monoclonal and Polyclonal Antibodies Research (21 papers) and Viral Infectious Diseases and Gene Expression in Insects (10 papers). John E. Schiel collaborates with scholars based in United States, United Kingdom and Japan. John E. Schiel's co-authors include David S. Hage, K.S. Joseph, Michelle Ji Yeon Yoo, Annette C. Moser, John P. Marino, Frank Delaglio, Luke W. Arbogast, Sony Soman, Rangan Mallik and Karen W. Phinney and has published in prestigious journals such as Analytical Chemistry, Journal of Virology and Journal of Chromatography A.

In The Last Decade

John E. Schiel

46 papers receiving 1.2k 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 E. Schiel United States 23 977 456 362 204 135 46 1.2k
Matthew Lauber United States 24 1.2k 1.2× 429 0.9× 783 2.2× 288 1.4× 57 0.4× 75 1.5k
Valentina D’Atri Switzerland 29 1.5k 1.5× 652 1.4× 869 2.4× 399 2.0× 190 1.4× 65 2.1k
Simone Nicolardi Netherlands 22 940 1.0× 221 0.5× 574 1.6× 118 0.6× 70 0.5× 70 1.4k
Shawna Hengel United States 16 615 0.6× 161 0.4× 374 1.0× 66 0.3× 205 1.5× 29 987
Guodong Chen United States 25 1.0k 1.0× 501 1.1× 821 2.3× 117 0.6× 131 1.0× 82 1.8k
Rob Haselberg Netherlands 24 929 1.0× 355 0.8× 829 2.3× 917 4.5× 103 0.8× 55 1.9k
Edouard S. P. Bouvier United States 9 671 0.7× 125 0.3× 622 1.7× 215 1.1× 34 0.3× 13 1.2k
Christopher J. Hipolito Japan 16 1.2k 1.2× 111 0.2× 143 0.4× 115 0.6× 273 2.0× 29 1.5k
Jason M. Hogan United States 17 733 0.8× 93 0.2× 903 2.5× 76 0.4× 94 0.7× 30 1.3k
Charles R. Wescott United States 13 839 0.9× 137 0.3× 287 0.8× 111 0.5× 42 0.3× 14 1.1k

Countries citing papers authored by John E. Schiel

Since Specialization
Citations

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

Fields of papers citing papers by John E. Schiel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John E. Schiel

This figure shows the co-authorship network connecting the top 25 collaborators of John E. Schiel. A scholar is included among the top collaborators of John E. Schiel 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 E. Schiel. John E. Schiel 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.
Kim, Eunkyoung, Jinyang Li, Zhiling Zhao, et al.. (2024). Detecting features of antibody structure through their mediator-accessible redox activities. Nature Chemical Biology. 21(2). 291–299. 4 indexed citations
2.
Lombard‐Banek, Camille, et al.. (2022). A Sensitive and Controlled Data-Independent Acquisition Method for Proteomic Analysis of Cell Therapies. Journal of Proteome Research. 21(5). 1229–1239. 4 indexed citations
3.
Duewer, David L., Jeffrey W. Hudgens, Kyle W. Anderson, et al.. (2022). Interlaboratory Studies Using the NISTmAb to Advance Biopharmaceutical Structural Analytics. Frontiers in Molecular Biosciences. 9. 876780–876780. 9 indexed citations
4.
Lombard‐Banek, Camille & John E. Schiel. (2020). Mass Spectrometry Advances and Perspectives for the Characterization of Emerging Adoptive Cell Therapies. Molecules. 25(6). 1396–1396. 12 indexed citations
5.
Rammohan, Jayan, Joel Welch, J. Michael McCarthy, et al.. (2019). Cyberbiosecurity for Biopharmaceutical Products. Frontiers in Bioengineering and Biotechnology. 7. 116–116. 11 indexed citations
6.
Arbogast, Luke W., et al.. (2018). Heterologous recombinant expression of non-originator NISTmAb. mAbs. 10(6). 922–933. 3 indexed citations
7.
Schiel, John E., et al.. (2018). The NISTmAb Reference Material 8671 lifecycle management and quality plan. Analytical and Bioanalytical Chemistry. 410(8). 2067–2078. 31 indexed citations
8.
Cole, Kenneth D., Paul C. DeRose, Hua‐Jun He, et al.. (2018). NIST Spectroscopic Measurement Standards.. PubMed. 31(4). 22–34. 4 indexed citations
9.
Telikepalli, Srivalli, Jason King, N. Alan Heckert, et al.. (2018). Development of orthogonal NISTmAb size heterogeneity control methods. Analytical and Bioanalytical Chemistry. 410(8). 2095–2110. 27 indexed citations
10.
Faustino, Anneliese M., et al.. (2018). The role of mass spectrometry in the characterization of biologic protein products. Expert Review of Proteomics. 15(5). 431–449. 53 indexed citations
11.
Schiel, John E., et al.. (2018). Development of an LC-MS/MS peptide mapping protocol for the NISTmAb. Analytical and Bioanalytical Chemistry. 410(8). 2111–2126. 104 indexed citations
12.
Arbogast, Luke W., Frank Delaglio, John E. Schiel, & John P. Marino. (2017). Multivariate Analysis of Two-Dimensional 1H, 13C Methyl NMR Spectra of Monoclonal Antibody Therapeutics To Facilitate Assessment of Higher Order Structure. Analytical Chemistry. 89(21). 11839–11845. 68 indexed citations
13.
Schiel, John E., Sarah Rogstad, & Michael T. Boyne. (2015). Comparison of Traditional 2-AB Fluorescence LC–MS/MS and Automated LC–MS for the Comparative Glycan Analysis of Monoclonal Antibodies. Journal of Pharmaceutical Sciences. 104(8). 2464–2472. 9 indexed citations
14.
Schiel, John E., et al.. (2012). LC-MS/MS biopharmaceutical glycoanalysis: identification of desirable reference material characteristics. Analytical and Bioanalytical Chemistry. 403(8). 2279–2289. 17 indexed citations
15.
Lowenthal, Mark S., et al.. (2011). A quantitative LC–MS/MS method for comparative analysis of capture-antibody affinity toward protein antigens. Journal of Chromatography B. 879(26). 2726–2732. 13 indexed citations
16.
Yoo, Michelle Ji Yeon, John E. Schiel, & David S. Hage. (2010). Evaluation of affinity microcolumns containing human serum albumin for rapid analysis of drug–protein binding. Journal of Chromatography B. 878(20). 1707–1713. 33 indexed citations
18.
Chen, Jianzhong, John E. Schiel, & David S. Hage. (2009). Non-Competitive Peak Decay Analysis Of Drugprotein\nDissociation By High-Performance Affinity\nChromatography. Insecta mundi. 42 indexed citations
19.
Schiel, John E. & David S. Hage. (2009). Kinetic studies of biological interactions by affinity chromatography. Journal of Separation Science. 32(10). 1507–1522. 54 indexed citations
20.
Joseph, K.S., et al.. (2008). Evaluation of alternatives to warfarin as probes for Sudlow site I of human serum albumin. Journal of Chromatography A. 1216(16). 3492–3500. 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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