Grant S. Murphy

1.3k total citations
9 papers, 174 citations indexed

About

Grant S. Murphy is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Grant S. Murphy has authored 9 papers receiving a total of 174 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 5 papers in Materials Chemistry and 1 paper in Organic Chemistry. Recurrent topics in Grant S. Murphy's work include Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and RNA and protein synthesis mechanisms (3 papers). Grant S. Murphy is often cited by papers focused on Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and RNA and protein synthesis mechanisms (3 papers). Grant S. Murphy collaborates with scholars based in United States. Grant S. Murphy's co-authors include Michael H. Hecht, Katherine M. Digianantonio, Mischa Machius, Thomas Szyperski, Brian Kuhlman, Michael J. Miley, Jeffrey Mills, S. Pulavarti, Bharathwaj Sathyamoorthy and Bryan S. Der and has published in prestigious journals such as PLoS ONE, Journal of Molecular Biology and ACS Catalysis.

In The Last Decade

Grant S. Murphy

8 papers receiving 173 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Grant S. Murphy United States 6 141 49 18 13 12 9 174
Benjamin Basanta United States 6 219 1.6× 70 1.4× 18 1.0× 19 1.5× 11 0.9× 12 249
Fabian Sesterhenn Switzerland 9 193 1.4× 36 0.7× 19 1.1× 47 3.6× 15 1.3× 12 267
Andrew P. Latham United States 12 367 2.6× 74 1.5× 11 0.6× 9 0.7× 15 1.3× 20 416
Jason M. Gilmore United States 5 264 1.9× 70 1.4× 14 0.8× 31 2.4× 12 1.0× 7 308
Samuel J. Hendel United States 7 154 1.1× 27 0.6× 8 0.4× 21 1.6× 21 1.8× 7 237
Reyes Núñez‐Franco Spain 8 185 1.3× 16 0.3× 9 0.5× 17 1.3× 16 1.3× 17 242
Hector Garcia‐Seisdedos Israel 6 209 1.5× 78 1.6× 40 2.2× 11 0.8× 10 0.8× 11 267
Ameeq Ul Mushtaq Sweden 8 157 1.1× 30 0.6× 53 2.9× 5 0.4× 6 0.5× 23 216
Pedro M. F. Sousa Portugal 8 152 1.1× 16 0.3× 13 0.7× 6 0.5× 8 0.7× 15 193

Countries citing papers authored by Grant S. Murphy

Since Specialization
Citations

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

Fields of papers citing papers by Grant S. Murphy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Grant S. Murphy

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

All Works

9 of 9 papers shown
1.
Kosjek, Birgit, Jackson K. B. Cahn, Wai Ling Cheung‐Lee, et al.. (2025). Ketoreductase Engineering for a Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade. ACS Catalysis. 15(15). 13059–13068.
2.
Li, Xinyi, et al.. (2024). Enzyme purification and sustained enzyme activity for pharmaceutical biocatalysis by fusion with phase‐separating intrinsically disordered protein. Biotechnology and Bioengineering. 121(10). 3155–3168. 5 indexed citations
3.
Murphy, Grant S., et al.. (2018). A de novo enzyme catalyzes a life-sustaining reaction in Escherichia coli. Nature Chemical Biology. 14(3). 253–255. 42 indexed citations
4.
Pan, Weilan, et al.. (2018). Role of simple descriptors and applicability domain in predicting change in protein thermostability. PLoS ONE. 13(9). e0203819–e0203819. 11 indexed citations
5.
Murphy, Grant S., et al.. (2015). De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic. Journal of Molecular Biology. 428(2). 399–411. 22 indexed citations
6.
Murphy, Grant S., et al.. (2015). Mitigation of aging in low voltage power cables in nuclear power plants. 3 indexed citations
7.
Murphy, Grant S., Bharathwaj Sathyamoorthy, Bryan S. Der, et al.. (2014). Computational de novo design of a four‐helix bundle protein—DND_4HB. Protein Science. 24(4). 434–445. 22 indexed citations
8.
Beck, Moriah R., Silvia M. Goicoechea, Grant S. Murphy, et al.. (2013). Structure and Function of Palladin's Actin Binding Domain. Journal of Molecular Biology. 425(18). 3325–3337. 22 indexed citations
9.
Murphy, Grant S., Jeffrey Mills, Michael J. Miley, et al.. (2012). Increasing Sequence Diversity with Flexible Backbone Protein Design: The Complete Redesign of a Protein Hydrophobic Core. Structure. 20(6). 1086–1096. 47 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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