John C. Joly

1.9k total citations
28 papers, 1.5k citations indexed

About

John C. Joly is a scholar working on Molecular Biology, Genetics and Cell Biology. According to data from OpenAlex, John C. Joly has authored 28 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 9 papers in Genetics and 7 papers in Cell Biology. Recurrent topics in John C. Joly's work include Viral Infectious Diseases and Gene Expression in Insects (12 papers), Protein purification and stability (9 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). John C. Joly is often cited by papers focused on Viral Infectious Diseases and Gene Expression in Insects (12 papers), Protein purification and stability (9 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). John C. Joly collaborates with scholars based in United States, Japan and Australia. John C. Joly's co-authors include William Wickner, James R. Swartz, Amy Shen, Gregory C. Flynn, Michael W. Laird, Robert A. Arkowitz, Daniel L. Purich, D L Purich, Julie C. Nishihara and Kathleen M. Champion and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Cell Biology and The EMBO Journal.

In The Last Decade

John C. Joly

28 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John C. Joly United States 23 1.3k 529 289 274 155 28 1.5k
Peter O. Olins United States 17 1.7k 1.3× 488 0.9× 281 1.0× 180 0.7× 191 1.2× 29 2.1k
Mark Vasser United States 12 1.6k 1.2× 554 1.0× 71 0.2× 333 1.2× 269 1.7× 17 1.9k
Oscar Conchillo‐Solé Spain 16 1.2k 0.9× 151 0.3× 98 0.3× 203 0.7× 139 0.9× 35 1.6k
Shaorong Chong United States 22 2.5k 1.9× 376 0.7× 77 0.3× 522 1.9× 208 1.3× 42 2.7k
Gregory D. Davis United States 12 1.5k 1.1× 371 0.7× 182 0.6× 192 0.7× 99 0.6× 20 1.6k
Joe Hedgpeth United States 19 1.1k 0.9× 589 1.1× 130 0.4× 57 0.2× 345 2.2× 26 1.6k
Rebecca Kucera United States 15 1.3k 1.0× 377 0.7× 55 0.2× 155 0.6× 204 1.3× 25 1.5k
S.D. Weeks Belgium 23 1.4k 1.0× 177 0.3× 234 0.8× 106 0.4× 85 0.5× 47 1.7k
Wieslaw Kudlicki United States 25 1.7k 1.3× 291 0.6× 153 0.5× 218 0.8× 165 1.1× 55 1.9k
Elizabeth J. Grayhack United States 28 2.9k 2.2× 330 0.6× 148 0.5× 81 0.3× 187 1.2× 43 3.2k

Countries citing papers authored by John C. Joly

Since Specialization
Citations

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

Fields of papers citing papers by John C. Joly

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John C. Joly

This figure shows the co-authorship network connecting the top 25 collaborators of John C. Joly. A scholar is included among the top collaborators of John C. Joly 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 C. Joly. John C. Joly 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.
2.
Shaw, David, John C. Joly, Andy Lin, et al.. (2017). Development and characterization of an automated imaging workflow to generate clonally‐derived cell lines for therapeutic proteins. Biotechnology Progress. 34(3). 584–592. 15 indexed citations
3.
Frye, Christopher C., Rohini Deshpande, Scott Estes, et al.. (2016). Industry view on the relative importance of “clonality” of biopharmaceutical-producing cell lines. Biologicals. 44(2). 117–122. 75 indexed citations
4.
Zhou, Meixia, et al.. (2014). Complete Knockout of the Lactate Dehydrogenase A Gene is Lethal in Pyruvate Dehydrogenase Kinase 1, 2, 3 Down-Regulated CHO Cells. Molecular Biotechnology. 56(9). 833–838. 15 indexed citations
5.
Yuk, Inn H., Stephen W. Russell, Yun Tang, et al.. (2014). Effects of copper on CHO cells: Cellular requirements and product quality considerations. Biotechnology Progress. 31(1). 226–238. 62 indexed citations
6.
Crawford, Yongping, Michelle Zhou, Zhilan Hu, et al.. (2013). Fast identification of reliable hosts for targeted cell line development from a limited‐genome screening using combined φC31 integrase and CRE‐Lox technologies. Biotechnology Progress. 29(5). 1307–1315. 41 indexed citations
7.
8.
Zhou, Meixia, Yongping Crawford, Jack K. Tung, et al.. (2011). Decreasing lactate level and increasing antibody production in Chinese Hamster Ovary cells (CHO) by reducing the expression of lactate dehydrogenase and pyruvate dehydrogenase kinases. Journal of Biotechnology. 153(1-2). 27–34. 117 indexed citations
9.
Yuk, Inn H., Boyan Zhang, George Dutina, et al.. (2011). Controlling glycation of recombinant antibody in fed‐batch cell cultures. Biotechnology and Bioengineering. 108(11). 2600–2610. 64 indexed citations
10.
Guo, Donglin, Albert Gao, David A. Michels, et al.. (2010). Mechanisms of unintended amino acid sequence changes in recombinant monoclonal antibodies expressed in Chinese Hamster Ovary (CHO) cells. Biotechnology and Bioengineering. 107(1). 163–171. 57 indexed citations
11.
Krawitz, Denise C., William F. Forrest, Christina Chen, et al.. (2005). Proteomic Profiling of RecombinantEscherichia coliin High-Cell-Density Fermentations for Improved Production of an Antibody Fragment Biopharmaceutical. Applied and Environmental Microbiology. 71(4). 1717–1728. 50 indexed citations
12.
Chen, Christina, Brad Snedecor, Julie C. Nishihara, et al.. (2004). High‐level accumulation of a recombinant antibody fragment in the periplasm of Escherichia coli requires a triple‐mutant (degP prc spr) host strain. Biotechnology and Bioengineering. 85(5). 463–474. 63 indexed citations
13.
Champion, Kathleen M., et al.. (2001). Similarity of theEscherichia coli proteome upon completion of different biopharmaceutical fermentation processes. PROTEOMICS. 1(8). 1133–1148. 49 indexed citations
14.
Champion, Kathleen M., et al.. (2001). Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. PROTEOMICS. 1(9). 1133–1148. 5 indexed citations
15.
Joly, John C. & James R. Swartz. (1997). In Vitro and in Vivo Redox States of the Escherichia coli Periplasmic Oxidoreductases DsbA and DsbC. Biochemistry. 36(33). 10067–10072. 116 indexed citations
16.
17.
Joly, John C. & James R. Swartz. (1994). Protein Folding Activities of Escherichia coli Protein Disulfide Isomerase. Biochemistry. 33(14). 4231–4236. 32 indexed citations
18.
Joly, John C. & Daniel L. Purich. (1990). Peptides corresponding to the second repeated sequence in MAP-2 inhibit binding of microtubule-associated proteins to microtubules. Biochemistry. 29(38). 8916–8920. 39 indexed citations
19.
Joly, John C., Gregory C. Flynn, & D L Purich. (1989). The microtubule-binding fragment of microtubule-associated protein-2: location of the protease-accessible site and identification of an assembly-promoting peptide.. The Journal of Cell Biology. 109(5). 2289–2294. 91 indexed citations
20.
Flynn, Gregory C., John C. Joly, & Daniel L. Purich. (1987). The 28,000 Mr microtubule-binding domain of microtubule-associated protein-2 also contains a neurofilament-binding site. Biochemical and Biophysical Research Communications. 148(3). 1453–1459. 23 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Peter O. Olins Breakdown of academic impact, for papers by Mark Vasser Breakdown of academic impact, for papers by Oscar Conchillo‐Solé Breakdown of academic impact, for papers by Shaorong Chong Breakdown of academic impact, for papers by Gregory D. Davis Breakdown of academic impact, for papers by Joe Hedgpeth Breakdown of academic impact, for papers by Rebecca Kucera Breakdown of academic impact, for papers by S.D. Weeks Breakdown of academic impact, for papers by Wieslaw Kudlicki Breakdown of academic impact, for papers by Elizabeth J. Grayhack
Rankless by CCL
2026