Reb J. Russell

1.0k total citations
20 papers, 807 citations indexed

About

Reb J. Russell is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Spectroscopy. According to data from OpenAlex, Reb J. Russell has authored 20 papers receiving a total of 807 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 6 papers in Radiology, Nuclear Medicine and Imaging and 5 papers in Spectroscopy. Recurrent topics in Reb J. Russell's work include Protein purification and stability (10 papers), Viral Infectious Diseases and Gene Expression in Insects (8 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). Reb J. Russell is often cited by papers focused on Protein purification and stability (10 papers), Viral Infectious Diseases and Gene Expression in Insects (8 papers) and Monoclonal and Polyclonal Antibodies Research (6 papers). Reb J. Russell collaborates with scholars based in United States, Germany and Sweden. Reb J. Russell's co-authors include Adrienne A. Tymiak, Liyuan Tao, John C. Gebler, Kenneth J. Fountain, Martin Gilár, Paul Rainville, Uwe D. Neue, Guodong Chen, John R. Engen and Hui Wei and has published in prestigious journals such as Journal of Chromatography A, Biotechnology and Bioengineering and Protein Science.

In The Last Decade

Reb J. Russell

20 papers receiving 783 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Reb J. Russell United States 13 646 235 179 148 63 20 807
Rohin Mhatre United States 13 462 0.7× 176 0.7× 230 1.3× 136 0.9× 17 0.3× 15 613
Da Ren United States 15 765 1.2× 235 1.0× 417 2.3× 62 0.4× 41 0.7× 27 948
Yuwei Tian China 20 608 0.9× 312 1.3× 163 0.9× 58 0.4× 82 1.3× 37 931
John P. Gabrielson United States 17 701 1.1× 124 0.5× 312 1.7× 128 0.9× 28 0.4× 25 881
Grigoriy Cħaga Sweden 11 456 0.7× 97 0.4× 195 1.1× 88 0.6× 34 0.5× 15 595
Yasuhiro Takegawa Japan 22 1.0k 1.6× 465 2.0× 172 1.0× 87 0.6× 24 0.4× 32 1.2k
John A. Chakel United States 12 868 1.3× 593 2.5× 46 0.3× 184 1.2× 53 0.8× 20 1.2k
Zoran Sosic United States 18 560 0.9× 160 0.7× 263 1.5× 407 2.8× 34 0.5× 34 950
Somak Ray United States 15 372 0.6× 205 0.9× 57 0.3× 164 1.1× 43 0.7× 21 570
Johanna Hofmann Germany 19 824 1.3× 566 2.4× 399 2.2× 88 0.6× 16 0.3× 45 1.5k

Countries citing papers authored by Reb J. Russell

Since Specialization
Citations

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

Fields of papers citing papers by Reb J. Russell

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Reb J. Russell. 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 Reb J. Russell. The network helps show where Reb J. Russell may publish in the future.

Co-authorship network of co-authors of Reb J. Russell

This figure shows the co-authorship network connecting the top 25 collaborators of Reb J. Russell. A scholar is included among the top collaborators of Reb J. Russell 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 Reb J. Russell. Reb J. Russell 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.
Huang, Yunping, Jinmei Fu, Richard Ludwig, et al.. (2017). Identification and quantification of signal peptide variants in an IgG1 monoclonal antibody produced in mammalian cell lines. Journal of Chromatography B. 1068-1069. 193–200. 8 indexed citations
2.
Fan, Lianchun, Giovanni Rizzi, Jun Tian, et al.. (2017). Comparative study of therapeutic antibody candidates derived from mini‐pool and clonal cell lines. Biotechnology Progress. 33(6). 1456–1462. 29 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.
Xu, Ping, et al.. (2016). Characterization of TAP Ambr 250 disposable bioreactors, as a reliable scale‐down model for biologics process development. Biotechnology Progress. 33(2). 478–489. 55 indexed citations
5.
Rizzi, Giovanni, et al.. (2016). CHO cells knocked out for TSC2 display an improved productivity of antibodies under fed batch conditions. Biotechnology and Bioengineering. 113(9). 1942–1952. 20 indexed citations
6.
7.
Xu, Ping, et al.. (2014). Effects of glutamine and asparagine on recombinant antibody production using CHO‐GS cell lines. Biotechnology Progress. 30(6). 1457–1468. 23 indexed citations
8.
Wang, Lu, et al.. (2013). A safe, effective, and facility compatible cleaning in place procedure for affinity resin in large-scale monoclonal antibody purification. Journal of Chromatography A. 1308. 86–95. 18 indexed citations
9.
Wei, Hui, Jingjie Mo, Liyuan Tao, et al.. (2013). Hydrogen/deuterium exchange mass spectrometry for probing higher order structure of protein therapeutics: methodology and applications. Drug Discovery Today. 19(1). 95–102. 153 indexed citations
10.
Huang, Yunping, Richard Ludwig, Jinmei Fu, et al.. (2012). Glycine to glutamic acid misincorporation observed in a recombinant protein expressed by Escherichia coli cells. Protein Science. 21(5). 625–632. 11 indexed citations
11.
Fu, Jinmei, Jacob Bongers, Li Tao, et al.. (2012). Characterization and identification of alanine to serine sequence variants in an IgG4 monoclonal antibody produced in mammalian cell lines. Journal of Chromatography B. 908. 1–8. 20 indexed citations
12.
Nayak, Vikram S., et al.. (2011). Evaporative Light Scattering Detection Based HPLC Method for the Determination of Polysorbate 80 in Therapeutic Protein Formulations. Journal of Chromatographic Science. 50(1). 21–25. 29 indexed citations
13.
Bongers, Jacob, Jinmei Fu, Peiqing Huang, et al.. (2011). Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a CTLA4-Ig fusion protein by liquid chromatography–mass spectrometry peptide mapping. Journal of Chromatography A. 1218(45). 8140–8149. 44 indexed citations
14.
Aranı́bar, Nelly, Michael Borys, Nancy A. Mackin, et al.. (2011). NMR-based metabolomics of mammalian cell and tissue cultures. Journal of Biomolecular NMR. 49(3-4). 195–206. 57 indexed citations
15.
Tan, Zhijun, et al.. (2011). Quantitative analysis of tris(2-carboxyethyl)phosphine by anion-exchange chromatography and evaporative light-scattering detection. Journal of Pharmaceutical and Biomedical Analysis. 59. 167–172. 11 indexed citations
16.
Liu, Peiran, Bethanne M. Warrack, Wei Wu, et al.. (2010). A tris (2-carboxyethyl) phosphine (TCEP) related cleavage on cysteine-containing proteins. Journal of the American Society for Mass Spectrometry. 21(5). 837–844. 59 indexed citations
17.
Liu, Peiran, Wei Wu, Haiying Zhang, et al.. (2009). Characterization of S‐thiolation on secreted proteins from E. coli by mass spectrometry. Rapid Communications in Mass Spectrometry. 23(20). 3343–3349. 1 indexed citations
18.
Gadgil, Himanshu S., Da Ren, Paul Rainville, et al.. (2003). SEC-MS analysis of aggregates in protein mixtures. LCGC North America. 23–24. 2 indexed citations
19.
Gilár, Martin, Kenneth J. Fountain, Uwe D. Neue, et al.. (2002). Ion-pair reversed-phase high-performance liquid chromatography analysis of oligonucleotides:. Journal of Chromatography A. 958(1-2). 167–182. 182 indexed citations
20.
Russell, Reb J.. (1997). Liposome-Mediated DNA Transfer. 1 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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