Emily Jackson-Machelski

1.4k total citations
19 papers, 1.2k citations indexed

About

Emily Jackson-Machelski is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Emily Jackson-Machelski has authored 19 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 9 papers in Materials Chemistry and 5 papers in Cell Biology. Recurrent topics in Emily Jackson-Machelski's work include Enzyme Structure and Function (9 papers), Protein Kinase Regulation and GTPase Signaling (5 papers) and Protein Structure and Dynamics (4 papers). Emily Jackson-Machelski is often cited by papers focused on Enzyme Structure and Function (9 papers), Protein Kinase Regulation and GTPase Signaling (5 papers) and Protein Structure and Dynamics (4 papers). Emily Jackson-Machelski collaborates with scholars based in United States, Germany and Italy. Emily Jackson-Machelski's co-authors include Jeffrey I. Gordon, S P Adams, Dwight A. Towler, Shad R. Eubanks, L Glaser, Jennifer K. Lodge, Charles A. McWherter, Dena L. Toffaletti, Rajiv S. Bhatnagar and John R. Perfect and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Emily Jackson-Machelski

19 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Emily Jackson-Machelski United States 15 928 373 323 181 177 19 1.2k
Gabriela C. Pérez-Alvarado United States 16 1.4k 1.5× 156 0.4× 277 0.9× 189 1.0× 50 0.3× 17 1.8k
P.J. Finerty Canada 15 1.1k 1.2× 164 0.4× 145 0.4× 52 0.3× 105 0.6× 16 1.5k
Kvido Střı́šovský Czechia 24 1.1k 1.2× 344 0.9× 116 0.4× 111 0.6× 122 0.7× 46 1.7k
Balekudru Devadas United States 18 609 0.7× 133 0.4× 196 0.6× 181 1.0× 130 0.7× 31 938
Hiroto Yamaguchi Japan 15 1.1k 1.2× 129 0.3× 183 0.6× 115 0.6× 325 1.8× 28 1.9k
Rajiv S. Bhatnagar United States 7 572 0.6× 184 0.5× 129 0.4× 54 0.3× 71 0.4× 8 747
Seema Dalal United States 20 900 1.0× 286 0.8× 125 0.4× 58 0.3× 233 1.3× 41 1.5k
Feiran Lu United States 10 776 0.8× 179 0.5× 88 0.3× 73 0.4× 108 0.6× 13 1.3k
Robyn M. Kaake United States 20 904 1.0× 263 0.7× 84 0.3× 70 0.4× 182 1.0× 28 1.3k
Yugong Cheng United States 8 1.4k 1.6× 182 0.5× 472 1.5× 49 0.3× 88 0.5× 9 1.7k

Countries citing papers authored by Emily Jackson-Machelski

Since Specialization
Citations

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

Fields of papers citing papers by Emily Jackson-Machelski

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Emily Jackson-Machelski. 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 Emily Jackson-Machelski. The network helps show where Emily Jackson-Machelski may publish in the future.

Co-authorship network of co-authors of Emily Jackson-Machelski

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

All Works

19 of 19 papers shown
1.
Hawes, John W., Kevin L. Knudtson, George S. Grills, et al.. (2006). Evaluation of methods for sequence analysis of highly repetitive DNA templates.. PubMed. 17(2). 138–44. 4 indexed citations
2.
Hawes, John W., et al.. (2003). DNA SEQUENCING RESEARCH GROUP (DSRG) 2003—A GENERAL SURVEY OF CORE DNA SEQUENCING FACILITIES.. PubMed Central. 14(3). 231–235. 3 indexed citations
3.
Hawes, John W., et al.. (2003). RESEARCH GROUP COMMITTEE REPORTS. 1 indexed citations
4.
Lodge, Jennifer K., Emily Jackson-Machelski, Charles A. McWherter, et al.. (1998). Genetic and Biochemical Studies Establish That the Fungicidal Effect of a Fully Depeptidized Inhibitor of Cryptococcus neoformans Myristoyl-CoA:ProteinN-Myristoyltransferase (Nmt) Is Nmt-dependent. Journal of Biological Chemistry. 273(20). 12482–12491. 37 indexed citations
5.
Bhatnagar, Rajiv S., Klaus Fütterer, Thalia A. Farazi, et al.. (1998). Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs. Nature Structural Biology. 5(12). 1091–1097. 109 indexed citations
6.
Devadas, Balekudru, Sandra K. Freeman, Charles A. McWherter, et al.. (1998). Novel Biologically Active Nonpeptidic Inhibitors of MyristoylCoA:Protein N-Myristoyltransferase. Journal of Medicinal Chemistry. 41(6). 996–1000. 40 indexed citations
7.
Bhatnagar, Rajiv S., Otto F. Schall, Emily Jackson-Machelski, et al.. (1997). Titration Calorimetric Analysis of AcylCoA Recognition by MyristoylCoA:Protein N-Myristoyltransferase. Biochemistry. 36(22). 6700–6708. 38 indexed citations
8.
Lodge, Jennifer K., Emily Jackson-Machelski, Balekudru Devadas, et al.. (1997). N-Myristoylation of Arf proteins in Candida albicans: an in vivo assay for evaluating antifungal inhibitors of myristoyl-CoA:protein N-myristoyltransferase. Microbiology. 143(2). 357–366. 37 indexed citations
9.
Zhang, Litao, Emily Jackson-Machelski, & Jeffrey I. Gordon. (1996). Biochemical Studies of Saccharomyces cerevisiae Myristoyl-coenzyme A:Protein N-Myristoyltransferase Mutants. Journal of Biological Chemistry. 271(51). 33131–33140. 19 indexed citations
10.
Bhatnagar, Rajiv S., Emily Jackson-Machelski, Charles A. McWherter, & Jeffrey I. Gordon. (1994). Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands. Journal of Biological Chemistry. 269(15). 11045–11053. 48 indexed citations
11.
Lodge, Jennifer K., Emily Jackson-Machelski, Dena L. Toffaletti, John R. Perfect, & Jeffrey I. Gordon. (1994). Targeted gene replacement demonstrates that myristoyl-CoA: protein N-myristoyltransferase is essential for viability of Cryptococcus neoformans.. Proceedings of the National Academy of Sciences. 91(25). 12008–12012. 148 indexed citations
12.
Lu, Taotao, Qing Li, Akira Katoh, et al.. (1994). The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Polar probes of the enzyme's myristoyl-CoA recognition site.. Journal of Biological Chemistry. 269(7). 5346–5357. 23 indexed citations
13.
Rudnick, David A., Warren J. Rocque, Charles A. McWherter, et al.. (1993). Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism.. Proceedings of the National Academy of Sciences. 90(3). 1087–1091. 28 indexed citations
14.
Rudnick, David A., et al.. (1992). Analogs of palmitoyl-CoA that are substrates for myristoyl-CoA:protein N-myristoyltransferase.. Proceedings of the National Academy of Sciences. 89(21). 10507–10511. 38 indexed citations
15.
Gokel, George W., Tianbao Lu, David A. Rudnick, Emily Jackson-Machelski, & Jeffrey I. Gordon. (1992). MyristoylCoA:protein N‐Myristoyltransferase: Probing Host‐Guest Interactions Using Synthetic Substrates. Israel Journal of Chemistry. 32(1). 127–133. 4 indexed citations
16.
Heuckeroth, Robert O., et al.. (1990). Novel fatty acyl substrates for myristoyl-CoA:protein N-myristoyl-transferase.. Journal of Lipid Research. 31(6). 1121–1129. 31 indexed citations
17.
Duronio, Robert J., Emily Jackson-Machelski, Robert O. Heuckeroth, et al.. (1990). Protein N-myristoylation in Escherichia coli: reconstitution of a eukaryotic protein modification in bacteria.. Proceedings of the National Academy of Sciences. 87(4). 1506–1510. 224 indexed citations
18.
Towler, Dwight A., S P Adams, Shad R. Eubanks, et al.. (1988). Myristoyl CoA:protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities.. Journal of Biological Chemistry. 263(4). 1784–1790. 175 indexed citations
19.
Towler, Dwight A., S P Adams, Shad R. Eubanks, et al.. (1987). Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase.. Proceedings of the National Academy of Sciences. 84(9). 2708–2712. 215 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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