Jon A. Friesen

945 total citations
30 papers, 732 citations indexed

About

Jon A. Friesen is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Jon A. Friesen has authored 30 papers receiving a total of 732 indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 6 papers in Materials Chemistry and 5 papers in Cell Biology. Recurrent topics in Jon A. Friesen's work include Plant biochemistry and biosynthesis (8 papers), Glycosylation and Glycoproteins Research (6 papers) and Enzyme Structure and Function (6 papers). Jon A. Friesen is often cited by papers focused on Plant biochemistry and biosynthesis (8 papers), Glycosylation and Glycoproteins Research (6 papers) and Enzyme Structure and Function (6 papers). Jon A. Friesen collaborates with scholars based in United States, Colombia and United Kingdom. Jon A. Friesen's co-authors include Victor W. Rodwell, Claudia Kent, David W. Borst, Beth A. Helmink, Sheng Li, Jay D. Braker, Marjorie A. Jones, Young‐Seo Park, Mingfang Liu and Subramaniam Sanker and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Langmuir.

In The Last Decade

Jon A. Friesen

29 papers receiving 715 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jon A. Friesen United States 15 481 96 91 74 62 30 732
Gordon W. Robinson United States 17 890 1.9× 57 0.6× 84 0.9× 120 1.6× 132 2.1× 22 1.1k
Britta Spanier Germany 17 537 1.1× 57 0.6× 56 0.6× 22 0.3× 62 1.0× 32 1.0k
Vasudev C. Joshi United States 6 573 1.2× 131 1.4× 64 0.7× 53 0.7× 59 1.0× 9 913
Vernon F. Kalb United States 10 732 1.5× 98 1.0× 30 0.3× 94 1.3× 161 2.6× 11 1.1k
Catherine Corbier France 18 745 1.5× 97 1.0× 40 0.4× 25 0.3× 97 1.6× 38 959
Wei Guang United States 17 565 1.2× 68 0.7× 75 0.8× 70 0.9× 85 1.4× 36 850
Jeffrey L. Garwin United States 16 837 1.7× 90 0.9× 56 0.6× 154 2.1× 58 0.9× 17 1.2k
Sudarslal Sadasivan Nair India 18 498 1.0× 40 0.4× 24 0.3× 77 1.0× 73 1.2× 30 848
Kazuyo Nishihara Japan 11 754 1.6× 83 0.9× 34 0.4× 66 0.9× 63 1.0× 33 1.1k
Parimal C. Sen India 18 413 0.9× 67 0.7× 44 0.5× 27 0.4× 74 1.2× 62 830

Countries citing papers authored by Jon A. Friesen

Since Specialization
Citations

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

Fields of papers citing papers by Jon A. Friesen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jon A. Friesen. 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 Jon A. Friesen. The network helps show where Jon A. Friesen may publish in the future.

Co-authorship network of co-authors of Jon A. Friesen

This figure shows the co-authorship network connecting the top 25 collaborators of Jon A. Friesen. A scholar is included among the top collaborators of Jon A. Friesen 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 Jon A. Friesen. Jon A. Friesen 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.
Peters, Steven J., et al.. (2021). Characterization of an archaeal inorganic pyrophosphatase from Sulfolobus islandicus using a [31P]-NMR-based assay. Biochemical and Biophysical Research Communications. 585. 8–14. 1 indexed citations
3.
Peters, Steven J., et al.. (2019). Development of a new and reliable assay for choline kinase using 31P NMR. Heliyon. 5(10). e02585–e02585. 5 indexed citations
4.
Álzate, Juan F., David L. Cedeño, Monika A. Makurath, et al.. (2017). Insights into the phosphatidylcholine and phosphatidylethanolamine biosynthetic pathways in Leishmania parasites and characterization of a choline kinase from Leishmania infantum. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 213. 45–54. 16 indexed citations
5.
Friesen, Jon A., et al.. (2016). Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography. Analytical Biochemistry. 510. 26–32. 7 indexed citations
6.
Hughes, Stephen R., Bryan R. Moser, Jon A. Friesen, et al.. (2012). Synthetic resin-bound truncated Candida antarctica lipase B for production of fatty acid alkyl esters by transesterification of corn and soybean oils with ethanol or butanol. Journal of Biotechnology. 159(1-2). 69–77. 6 indexed citations
7.
Friesen, Jon A., et al.. (2012). Comparative kinetic analysis of glycerol 3-phosphate cytidylyltransferase from Enterococcus faecalis and Listeria monocytogenes. Medical Science Monitor. 18(11). BR427–BR434. 6 indexed citations
8.
Cedeño, David L., et al.. (2010). Integrating Free Computer Software in Chemistry and Biochemistry Instruction: An International Collaboration. Journal of Science Education and Technology. 19(5). 434–437. 3 indexed citations
9.
Li, Sheng, et al.. (2009). Methyl farnesoate synthesis in the lobster mandibular organ: The roles of HMG-CoA reductase and farnesoic acid O-methyltransferase. Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology. 155(1). 49–55. 29 indexed citations
10.
Braker, Jay D., et al.. (2009). Identification of hydrophobic amino acids required for lipid activation of C. elegans CTP:phosphocholine cytidylyltransferase. Archives of Biochemistry and Biophysics. 492(1-2). 10–16. 8 indexed citations
11.
Tilley, Dana, et al.. (2008). Identification and Characterization of the Nuclear Isoform of Drosophila melanogaster CTP:Phosphocholine Cytidylyltransferase. Biochemistry. 47(45). 11838–11846. 12 indexed citations
12.
Stephenson, Jason R., et al.. (2007). Role of aspartate 400, arginine 262, and arginine 401 in the catalytic mechanism of human coproporphyrinogen oxidase. Protein Science. 16(3). 401–410. 15 indexed citations
13.
Friesen, Jon A. & Victor W. Rodwell. (2004). The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.. Genome Biology. 5(11). 248–248. 304 indexed citations
14.
Helmink, Beth A. & Jon A. Friesen. (2004). Characterization of a lipid activated CTP:phosphocholine cytidylyltransferase from Drosophila melanogaster. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1683(1-3). 78–88. 18 indexed citations
15.
Li, Sheng, et al.. (2003). 3-Hydroxy-3-methylglutaryl-coenzyme A reductase in the lobster mandibular organ: regulation by the eyestalk. General and Comparative Endocrinology. 134(2). 147–155. 30 indexed citations
16.
Jones, Marjorie A., et al.. (2003). Use of Computer Modeling of Site-Directed Mutagenesis of a Selected Enzyme: A Class Activity for an Introductory Biochemistry Course. Journal of Science Education and Technology. 12(4). 413–419. 2 indexed citations
17.
Friesen, Jon A., Young‐Seo Park, & Claudia Kent. (2001). Purification and Kinetic Characterization of CTP:Phosphocholine Cytidylyltransferase from Saccharomyces cerevisiae. Protein Expression and Purification. 21(1). 141–148. 21 indexed citations
19.
Friesen, Jon A., et al.. (1999). Enzymatic and Cellular Characterization of a Catalytic Fragment of CTP:Phosphocholine Cytidylyltransferase α. Journal of Biological Chemistry. 274(19). 13384–13389. 59 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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