John F. Moomaw

1.4k total citations
18 papers, 1.1k citations indexed

About

John F. Moomaw is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, John F. Moomaw has authored 18 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 4 papers in Oncology and 4 papers in Cell Biology. Recurrent topics in John F. Moomaw's work include Protein Kinase Regulation and GTPase Signaling (5 papers), Cellular Mechanics and Interactions (3 papers) and Plant biochemistry and biosynthesis (3 papers). John F. Moomaw is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (5 papers), Cellular Mechanics and Interactions (3 papers) and Plant biochemistry and biosynthesis (3 papers). John F. Moomaw collaborates with scholars based in United States and Germany. John F. Moomaw's co-authors include Patrick J. Casey, Julia Thissen, L.S. Beese, Brad Zerler, H. Earl Ruley, Kazuo Maruyama, Terri Grodzicker, Brian W. Moran, Antonio Landavazo and Eric S. Furfine and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

John F. Moomaw

18 papers receiving 1.1k 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 F. Moomaw United States 14 926 343 223 186 139 18 1.1k
William R. Tschantz United States 18 669 0.7× 249 0.7× 186 0.8× 70 0.4× 99 0.7× 25 868
Zhihao Zhuang United States 30 2.2k 2.3× 567 1.7× 349 1.6× 218 1.2× 301 2.2× 65 2.4k
Ingrid Dreveny United Kingdom 24 1.2k 1.2× 140 0.4× 100 0.4× 424 2.3× 140 1.0× 38 1.5k
Joachim Schnier United States 20 1.3k 1.4× 174 0.5× 228 1.0× 78 0.4× 48 0.3× 40 1.5k
V. Dhanaraj United Kingdom 18 849 0.9× 265 0.8× 57 0.3× 103 0.6× 202 1.5× 36 1.4k
Alice Yam United States 12 990 1.1× 203 0.6× 54 0.2× 165 0.9× 132 0.9× 20 1.2k
Bernd Meyhack Switzerland 21 1.0k 1.1× 104 0.3× 168 0.8× 120 0.6× 59 0.4× 44 1.3k
Samuel Lara‐González Mexico 14 906 1.0× 149 0.4× 109 0.5× 184 1.0× 106 0.8× 25 1.2k
Yoshio Taniyama Japan 20 1.1k 1.1× 139 0.4× 176 0.8× 239 1.3× 265 1.9× 38 1.3k
Kenneth W. Walker United States 16 865 0.9× 428 1.2× 57 0.3× 291 1.6× 65 0.5× 25 1.4k

Countries citing papers authored by John F. Moomaw

Since Specialization
Citations

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

Fields of papers citing papers by John F. Moomaw

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John F. Moomaw

This figure shows the co-authorship network connecting the top 25 collaborators of John F. Moomaw. A scholar is included among the top collaborators of John F. Moomaw 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 F. Moomaw. John F. Moomaw is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

18 of 18 papers shown
1.
Jansen, Patrick J., John F. Moomaw, Keith A. Williams, et al.. (2025). A Novel Hybrid SPPS/LPPS Strategy for the Synthesis of Tirzepatide via Native Chemical Ligation. ChemRxiv. 1 indexed citations
2.
Jansen, Patrick J., John F. Moomaw, Keith A. Williams, et al.. (2025). A Novel Hybrid SPPS/LPPS Strategy for the Synthesis of Tirzepatide via Native Chemical Ligation. ChemRxiv. 1 indexed citations
3.
Rossi, Francesco, Eduardo Ximenes, Yu Zhao, et al.. (2024). Deterministic mathematical modeling, sensitivity analysis, and dynamic optimization of cross-flow ultrafiltration systems for concentration of monoclonal antibody solutions. Computers & Chemical Engineering. 187. 108705–108705. 1 indexed citations
4.
5.
Tao, Yinying, et al.. (2020). pH and excipient profiles during formulation of highly concentrated biotherapeutics using bufferless media. Biotechnology and Bioengineering. 117(11). 3390–3399. 9 indexed citations
6.
Peng, Sheng-Bin, Li Wang, John F. Moomaw, et al.. (2001). Biochemical Characterization of Signal Peptidase I from Gram-Positive Streptococcus pneumoniae. Journal of Bacteriology. 183(2). 621–627. 20 indexed citations
7.
Moomaw, John F., et al.. (1997). Crystal Structure of Protein Farnesyltransferase at 2.25 Angstrom Resolution. Science. 275(5307). 1800–1805. 258 indexed citations
8.
Dietrich, Alexander, Derek P. Brazil, Ole N. Jensen, et al.. (1996). Isoprenylation of the G Protein γ Subunit Is both Necessary and Sufficient for βγ Dimer-Mediated Stimulation of Phospholipase C. Biochemistry. 35(48). 15174–15182. 24 indexed citations
9.
Fu, Hua‐Wen, John F. Moomaw, Carolyn R. Moomaw, & Patrick J. Casey. (1996). Identification of a Cysteine Residue Essential for Activity of Protein Farnesyltransferase. Journal of Biological Chemistry. 271(45). 28541–28548. 43 indexed citations
10.
Furfine, Eric S., Johann Leban, Antonio Landavazo, John F. Moomaw, & Patrick J. Casey. (1995). Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry. 34(20). 6857–6862. 110 indexed citations
11.
Moomaw, John F., et al.. (1995). [2] Isolation of protein prenyltransferases from bovine brain and baculovirus expression system. Methods in enzymology on CD-ROM/Methods in enzymology. 250. 12–21. 23 indexed citations
12.
Casey, Patrick J., et al.. (1994). Prenylation and G Protein Signaling. Elsevier eBooks. 49. 215–238. 19 indexed citations
13.
Moomaw, John F., et al.. (1994). Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I.. Journal of Biological Chemistry. 269(38). 23465–23470. 49 indexed citations
14.
Chen, Wei J., John F. Moomaw, Laurie K. Overton, Thomas A. Kost, & Patrick J. Casey. (1993). High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc. Journal of Biological Chemistry. 268(13). 9675–9680. 77 indexed citations
15.
Moomaw, John F. & Patrick J. Casey. (1992). Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements.. Journal of Biological Chemistry. 267(24). 17438–17443. 129 indexed citations
16.
Casey, Patrick J., Julia Thissen, & John F. Moomaw. (1991). Enzymatic modification of proteins with a geranylgeranyl isoprenoid.. Proceedings of the National Academy of Sciences. 88(19). 8631–8635. 147 indexed citations
17.
Zerler, Brad, Brian W. Moran, Kazuo Maruyama, et al.. (1986). Adenovirus E1A coding sequences that enable ras and pmt oncogenes to transform cultured primary cells.. Molecular and Cellular Biology. 6(3). 887–899. 145 indexed citations
18.
Zerler, Brad, et al.. (1986). Adenovirus E1A Coding Sequences That Enable ras and pmt Oncogenes To Transform Cultured Primary Cells. Molecular and Cellular Biology. 6(3). 887–899. 71 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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