Jerry M. Troutman

826 total citations
31 papers, 647 citations indexed

About

Jerry M. Troutman is a scholar working on Molecular Biology, Organic Chemistry and Ecology. According to data from OpenAlex, Jerry M. Troutman has authored 31 papers receiving a total of 647 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 12 papers in Organic Chemistry and 5 papers in Ecology. Recurrent topics in Jerry M. Troutman's work include Glycosylation and Glycoproteins Research (10 papers), Carbohydrate Chemistry and Synthesis (9 papers) and Bacteriophages and microbial interactions (5 papers). Jerry M. Troutman is often cited by papers focused on Glycosylation and Glycoproteins Research (10 papers), Carbohydrate Chemistry and Synthesis (9 papers) and Bacteriophages and microbial interactions (5 papers). Jerry M. Troutman collaborates with scholars based in United States, China and Canada. Jerry M. Troutman's co-authors include H. Peter Spielmann, Douglas Andres, Barbara Imperiali, Melissa Kelly, Michael G. Fried, Trevor P. Creamer, Anne‐Frances Miller, Thangaiah Subramanian, Sunita Sharma and Phillip M. Scott and has published in prestigious journals such as Biochemistry, Journal of Bacteriology and International Journal of Molecular Sciences.

In The Last Decade

Jerry M. Troutman

30 papers receiving 646 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jerry M. Troutman United States 14 482 146 82 79 68 31 647
Christopher D. Fage Germany 15 572 1.2× 81 0.6× 50 0.6× 59 0.7× 65 1.0× 23 760
David C. Watson Canada 13 405 0.8× 78 0.5× 71 0.9× 58 0.7× 33 0.5× 16 550
Stefan Schmelz Germany 15 541 1.1× 119 0.8× 51 0.6× 51 0.6× 130 1.9× 30 791
Jiahn‐Haur Liao Taiwan 19 427 0.9× 80 0.5× 91 1.1× 70 0.9× 92 1.4× 34 643
Nina C. Bach Germany 11 329 0.7× 91 0.6× 29 0.4× 42 0.5× 38 0.6× 19 522
Michael S. Van Nieuwenhze United States 9 457 0.9× 148 1.0× 131 1.6× 39 0.5× 179 2.6× 12 791
Kyoung‐Jae Choi United States 16 614 1.3× 68 0.5× 61 0.7× 77 1.0× 64 0.9× 27 810
Stefan Reinelt Switzerland 14 581 1.2× 226 1.5× 55 0.7× 92 1.2× 249 3.7× 19 866
Serge Pérez France 8 525 1.1× 277 1.9× 107 1.3× 59 0.7× 49 0.7× 10 716
Kaitlin Schaefer United States 14 499 1.0× 100 0.7× 166 2.0× 57 0.7× 270 4.0× 18 793

Countries citing papers authored by Jerry M. Troutman

Since Specialization
Citations

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

Fields of papers citing papers by Jerry M. Troutman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jerry M. Troutman. 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 Jerry M. Troutman. The network helps show where Jerry M. Troutman may publish in the future.

Co-authorship network of co-authors of Jerry M. Troutman

This figure shows the co-authorship network connecting the top 25 collaborators of Jerry M. Troutman. A scholar is included among the top collaborators of Jerry M. Troutman 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 Jerry M. Troutman. Jerry M. Troutman 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.
Kay, Emily J., et al.. (2024). Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology. Microbial Cell Factories. 23(1). 72–72. 4 indexed citations
2.
3.
Howell, P. Lynne, et al.. (2023). Metabolic Usage and Glycan Destinations of GlcNAz in E. coli. ACS Chemical Biology. 19(1). 69–80. 2 indexed citations
4.
Eade, Colleen R., et al.. (2021). Tracking Colanic Acid Repeat Unit Formation from Stepwise Biosynthesis Inactivation in Escherichia coli. Biochemistry. 60(27). 2221–2230. 16 indexed citations
5.
Eade, Colleen R., et al.. (2021). Making the Enterobacterial Common Antigen Glycan and Measuring Its Substrate Sequestration. ACS Chemical Biology. 16(4). 691–700. 14 indexed citations
6.
Eade, Colleen R., et al.. (2021). Lipopolysaccharide Is a 4-Aminoarabinose Donor to Exogenous Polyisoprenyl Phosphates through the Reverse Reaction of the Enzyme ArnT. ACS Omega. 6(39). 25729–25741. 4 indexed citations
7.
Eade, Colleen R., et al.. (2020). Diffusible Signal Factors Act through AraC-Type Transcriptional Regulators as Chemical Cues To Repress Virulence of Enteric Pathogens. Infection and Immunity. 88(10). 28 indexed citations
8.
Scott, Phillip M., et al.. (2019). Identification of the Functional Roles of Six Key Proteins in the Biosynthesis of Enterobacteriaceae Colanic Acid. Biochemistry. 58(13). 1818–1830. 34 indexed citations
9.
Williams, Tiffany C., et al.. (2019). General Utilization of Fluorescent Polyisoprenoids with Sugar Selective Phosphoglycosyltransferases. Biochemistry. 59(4). 615–626. 11 indexed citations
10.
11.
Sharma, Sunita, et al.. (2016). Complete Tetrasaccharide Repeat Unit Biosynthesis of the Immunomodulatory Bacteroides fragilis Capsular Polysaccharide A. ACS Chemical Biology. 12(1). 92–101. 33 indexed citations
12.
Troutman, Jerry M., et al.. (2014). Functional identification of a galactosyltransferase critical to Bacteroides fragilis Capsular Polysaccharide A biosynthesis. Carbohydrate Research. 395. 19–28. 6 indexed citations
13.
14.
Subramanian, Thangaiah, June E. Pais, Suxia Liu, et al.. (2012). Farnesyl Diphosphate Analogues with Aryl Moieties Are Efficient Alternate Substrates for Protein Farnesyltransferase. Biochemistry. 51(41). 8307–8319. 13 indexed citations
15.
Sharma, Sunita, et al.. (2012). Chemoenzymatic synthesis of an isoprenoid phosphate tool for the analysis of complex bacterial oligosaccharide biosynthesis. Carbohydrate Research. 359. 44–53. 12 indexed citations
16.
Morrison, James P., Jerry M. Troutman, & Barbara Imperiali. (2010). Development of a multicomponent kinetic assay of the early enzymes in the Campylobacter jejuni N-linked glycosylation pathway. Bioorganic & Medicinal Chemistry. 18(23). 8167–8171. 5 indexed citations
17.
Adams, Val R., David L. DeRemer, Cynthia A. Mattingly, et al.. (2010). Anticancer activity of novel unnatural synthetic isoprenoids.. PubMed. 30(7). 2505–12. 5 indexed citations
18.
Subramanian, Thangaiah, Suxia Liu, Jerry M. Troutman, Douglas Andres, & H. Peter Spielmann. (2008). Protein Farnesyltransferase‐Catalyzed Isoprenoid Transfer to Peptide Depends on Lipid Size and Shape, not Hydrophobicity. ChemBioChem. 9(17). 2872–2882. 20 indexed citations
19.
Troutman, Jerry M., Douglas Andres, & H. Peter Spielmann. (2007). Protein Farnesyl Transferase Target Selectivity Is Dependent upon Peptide Stimulated Product Release. Biochemistry. 46(40). 11299–11309. 10 indexed citations
20.
Troutman, Jerry M., Michael J. Roberts, Douglas Andres, & H. Peter Spielmann. (2005). Tools To Analyze Protein Farnesylation in Cells. Bioconjugate Chemistry. 16(5). 1209–1217. 41 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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