John S. Philo

5.8k total citations
80 papers, 4.4k citations indexed

About

John S. Philo is a scholar working on Molecular Biology, Cell Biology and Spectroscopy. According to data from OpenAlex, John S. Philo has authored 80 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Molecular Biology, 17 papers in Cell Biology and 12 papers in Spectroscopy. Recurrent topics in John S. Philo's work include Protein purification and stability (15 papers), Hemoglobin structure and function (10 papers) and Glycosylation and Glycoproteins Research (6 papers). John S. Philo is often cited by papers focused on Protein purification and stability (15 papers), Hemoglobin structure and function (10 papers) and Glycosylation and Glycoproteins Research (6 papers). John S. Philo collaborates with scholars based in United States, Japan and United Kingdom. John S. Philo's co-authors include Tsutomu Arakawa, Jie Wen, Daisuke Ejima, Linda O. Narhi, Tiansheng Li, Izumi Kumagai, Mitsuo Umetsu, K. Tsumoto, Ryosuke Yumioka and Kouhei Tsumoto and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

John S. Philo

80 papers receiving 4.3k 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. Philo United States 33 3.2k 986 475 451 407 80 4.4k
Irwin Chaiken United States 42 3.9k 1.2× 1.2k 1.3× 455 1.0× 869 1.9× 314 0.8× 221 6.6k
Jim Warwicker United Kingdom 37 4.1k 1.3× 587 0.6× 797 1.7× 340 0.8× 385 0.9× 125 5.2k
Yoji Arata Japan 36 3.0k 1.0× 958 1.0× 753 1.6× 564 1.3× 297 0.7× 151 5.1k
Walter F. Stafford United States 40 3.9k 1.2× 703 0.7× 584 1.2× 374 0.8× 1.2k 3.0× 114 5.7k
Neil A. Farrow United States 30 3.8k 1.2× 501 0.5× 1.1k 2.3× 317 0.7× 463 1.1× 51 5.6k
G. Ya. Wiederschain United States 18 3.5k 1.1× 455 0.5× 329 0.7× 865 1.9× 602 1.5× 46 5.6k
Yoshinori Satow Japan 31 2.6k 0.8× 595 0.6× 1.0k 2.2× 588 1.3× 412 1.0× 89 4.5k
Jacek Otlewski Poland 40 4.1k 1.3× 465 0.5× 464 1.0× 518 1.1× 825 2.0× 167 5.4k
F.F. Vajdos United States 16 4.0k 1.3× 965 1.0× 675 1.4× 634 1.4× 320 0.8× 20 6.1k
Hans Rudolf Bosshard Switzerland 39 4.1k 1.3× 1.2k 1.2× 667 1.4× 270 0.6× 554 1.4× 105 6.2k

Countries citing papers authored by John S. Philo

Since Specialization
Citations

This map shows the geographic impact of John S. Philo'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. Philo 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. Philo more than expected).

Fields of papers citing papers by John S. Philo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of John S. Philo. A scholar is included among the top collaborators of John S. Philo 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. Philo. John S. Philo 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.
Philo, John S.. (2023). SEDNTERP: a calculation and database utility to aid interpretation of analytical ultracentrifugation and light scattering data. European Biophysics Journal. 52(4-5). 233–266. 59 indexed citations
2.
Ejima, Daisuke, Kouhei Tsumoto, Harumi Fukada, et al.. (2006). Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins Structure Function and Bioinformatics. 66(4). 954–962. 173 indexed citations
3.
Philo, John S., Tzung‐Horng Yang, & Michael J. LaBarre. (2004). Re-examining the oligomerization state of macrophage migration inhibitory factor (MIF) in solution. Biophysical Chemistry. 108(1-3). 77–87. 39 indexed citations
4.
Tsumoto, K., Mitsuo Umetsu, Izumi Kumagai, et al.. (2004). Role of Arginine in Protein Refolding, Solubilization, and Purification. Biotechnology Progress. 20(5). 1301–1308. 367 indexed citations
5.
Ishibashi, Matsujiro, et al.. (2002). Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high- and low-salt conditions. FEMS Microbiology Letters. 216(2). 235–241. 24 indexed citations
6.
Tokunaga, Masao, Makoto Mizukami, Hiroko Tokunaga, et al.. (2001). Molecular Cloning of groESL Locus, and Purification and Characterization of Chaperonins, GroEL and GroES, from Bacillus brevis. Bioscience Biotechnology and Biochemistry. 65(6). 1379–1387. 2 indexed citations
7.
Zhang, Mei, Thomas P. Horan, John S. Philo, et al.. (2001). Copper Staining Method for Extracting Biologically Active Proteins from Native Gels. Bioscience Biotechnology and Biochemistry. 65(6). 1315–1320. 2 indexed citations
8.
Narhi, Linda O., Robert Rosenfeld, Grant Shimamoto, et al.. (1997). Comparison of solution properties of human and rat ciliary neurotrophic factor. Journal of Peptide Research. 50(4). 300–309. 1 indexed citations
9.
Kita, Yoshiko, Julia Tseng, Thomas P. Horan, et al.. (1996). ErbB Receptor Activation, Cell Morphology Changes, and Apoptosis Induced by Anti-Her2 Monoclonal Antibodies. Biochemical and Biophysical Research Communications. 226(1). 59–69. 33 indexed citations
10.
Philo, John S., et al.. (1996). Human Stem Cell Factor Dimer Forms a Complex with Two Molecules of the Extracellular Domain of Its Receptor, Kit. Journal of Biological Chemistry. 271(12). 6895–6902. 58 indexed citations
11.
Hill, John S., Richard C. Davis, Dawn Yang, et al.. (1996). Human Hepatic Lipase Subunit Structure Determination. Journal of Biological Chemistry. 271(37). 22931–22936. 32 indexed citations
12.
Philo, John S., et al.. (1996). Quaternary structure dynamics and carbon monoxide binding kinetics of hemoglobin valency hybrids. Biophysical Journal. 70(4). 1949–1965. 7 indexed citations
13.
Horan, Thomas P., Jie Wen, Tsutomu Arakawa, et al.. (1995). Binding of Neu Differentiation Factor with the Extracellular Domain of Her2 and Her3. Journal of Biological Chemistry. 270(41). 24604–24608. 65 indexed citations
14.
Lu, Hsieng S., David Chang, John S. Philo, et al.. (1995). Studies on the Structure and Function of Glycosylated and Nonglycosylated neu Differentiation Factors. Journal of Biological Chemistry. 270(9). 4784–4791. 38 indexed citations
15.
Arakawa, Tsutomu, Jie Wen, & John S. Philo. (1994). Stoichiometry of Heparin Binding to Basic Fibroblast Growth Factor. Archives of Biochemistry and Biophysics. 308(1). 267–273. 50 indexed citations
16.
Arakawa, Tsutomu, Jie Wen, & John S. Philo. (1993). Densimetric determination of equilibrium binding of sucrose octasulfate with basic fibroblast growth factor. Journal of Protein Chemistry. 12(6). 689–693. 10 indexed citations
17.
Narhi, Linda O., Robert Rosenfeld, Jie Wen, et al.. (1993). Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric "A state". Biochemistry. 32(40). 10819–10825. 22 indexed citations
18.
Sivaraja, M., et al.. (1991). Calcium depletion from the photosynthetic water-oxidizing complex reveals photooxidation of a protein residue. Biochemistry. 30(19). 4740–4747. 17 indexed citations
19.
Philo, John S. & J.W. Lary. (1990). Kinetic investigations of the quaternary enhancement effect and alpha/beta differences in binding the last oxygen to hemoglobin tetramers and dimers.. Journal of Biological Chemistry. 265(1). 139–143. 38 indexed citations
20.
Philo, John S., et al.. (1984). Diamagnetism of human apo-, oxy-, and carbon monoxyhemoglobin. Biochemistry. 23(5). 865–872. 20 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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