M. Ashley Spies

641 total citations
26 papers, 516 citations indexed

About

M. Ashley Spies is a scholar working on Molecular Biology, Materials Chemistry and Computational Theory and Mathematics. According to data from OpenAlex, M. Ashley Spies has authored 26 papers receiving a total of 516 indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 8 papers in Materials Chemistry and 7 papers in Computational Theory and Mathematics. Recurrent topics in M. Ashley Spies's work include Enzyme Structure and Function (8 papers), Computational Drug Discovery Methods (7 papers) and Protein Structure and Dynamics (6 papers). M. Ashley Spies is often cited by papers focused on Enzyme Structure and Function (8 papers), Computational Drug Discovery Methods (7 papers) and Protein Structure and Dynamics (6 papers). M. Ashley Spies collaborates with scholars based in United States, Italy and Russia. M. Ashley Spies's co-authors include Michael D. Toney, K.L. Whalen, Richard L. Schowen, Steven R. Blanke, Joshua J. Woodward, Mitchell Watnik, Weiming Wu, Steven D. Christenson, Ben Shen and Dylan Dodd and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

M. Ashley Spies

26 papers receiving 514 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M. Ashley Spies United States 14 376 153 119 80 56 26 516
Dengguo Wei China 16 642 1.7× 100 0.7× 54 0.5× 115 1.4× 26 0.5× 38 934
C. Paris Switzerland 13 475 1.3× 67 0.4× 52 0.4× 60 0.8× 69 1.2× 18 645
John A. Gerlt United States 13 581 1.5× 286 1.9× 140 1.2× 71 0.9× 56 1.0× 15 732
William E. Karsten United States 17 547 1.5× 347 2.3× 243 2.0× 38 0.5× 39 0.7× 36 745
M M Yamashita United States 6 405 1.1× 200 1.3× 99 0.8× 53 0.7× 32 0.6× 6 590
Anthony A. Morollo United States 8 394 1.0× 222 1.5× 138 1.2× 43 0.5× 40 0.7× 8 512
Todd M. Larsen United States 11 639 1.7× 300 2.0× 114 1.0× 47 0.6× 44 0.8× 13 830
Sebastian Radestock Germany 10 534 1.4× 165 1.1× 60 0.5× 29 0.4× 59 1.1× 12 699
Susanne Brakmann Germany 16 618 1.6× 63 0.4× 19 0.2× 160 2.0× 52 0.9× 38 840

Countries citing papers authored by M. Ashley Spies

Since Specialization
Citations

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

Fields of papers citing papers by M. Ashley Spies

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Ashley Spies

This figure shows the co-authorship network connecting the top 25 collaborators of M. Ashley Spies. A scholar is included among the top collaborators of M. Ashley Spies 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 M. Ashley Spies. M. Ashley Spies 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.
Honda, Masayoshi, Eva Malacaria, Lokesh Gakhar, et al.. (2025). The RAD52 double-ring remodels replication forks restricting fork reversal. Nature. 641(8062). 512–519. 3 indexed citations
2.
Zhang, Yuzhou, et al.. (2023). Renin and renin blockade have no role in complement activity. Kidney International. 105(2). 328–337. 4 indexed citations
3.
Skoko, John, Juxiang Cao, David C. A. Gaboriau, et al.. (2022). Redox regulation of RAD51 Cys319 and homologous recombination by peroxiredoxin 1. Redox Biology. 56. 102443–102443. 14 indexed citations
4.
Chernykh, Anton V., Dmytro S. Radchenko, Эдуард Б. Русанов, et al.. (2022). A stereochemical journey around spirocyclic glutamic acid analogs. Organic & Biomolecular Chemistry. 20(15). 3183–3200. 6 indexed citations
5.
Hobbs, Kathryn, et al.. (2021). Decrypting a cryptic allosteric pocket in H. pylori glutamate racemase. Communications Chemistry. 4(1). 172–172. 4 indexed citations
6.
Spies, M. Ashley, et al.. (2018). Integrating Experimental and In Silico HTS in the Discovery of Inhibitors of Protein–Nucleic Acid Interactions. Methods in enzymology on CD-ROM/Methods in enzymology. 601. 243–273. 3 indexed citations
7.
Li, Yalan, et al.. (2018). Elucidating the Catalytic Power of Glutamate Racemase by Investigating a Series of Covalent Inhibitors. ChemMedChem. 13(23). 2514–2521. 3 indexed citations
8.
9.
King, Jessica, et al.. (2015). Inhibition of Pseudomonas aeruginosa ExsA DNA-Binding Activity by N -Hydroxybenzimidazoles. Antimicrobial Agents and Chemotherapy. 60(2). 766–776. 21 indexed citations
10.
Whalen, K.L., Anthony Chau, & M. Ashley Spies. (2013). In silico Optimization of a Fragment‐Based Hit Yields Biologically Active, High‐Efficiency Inhibitors for Glutamate Racemase. ChemMedChem. 8(10). 1681–1689. 12 indexed citations
11.
Spies, M. Ashley. (2013). Nexus Between Protein–Ligand Affinity Rank-Ordering, Biophysical Approaches, and Drug Discovery. ACS Medicinal Chemistry Letters. 4(10). 895–897. 2 indexed citations
12.
Whalen, K.L. & M. Ashley Spies. (2013). Flooding Enzymes: Quantifying the Contributions of Interstitial Water and Cavity Shape to Ligand Binding Using Extended Linear Response Free Energy Calculations. Journal of Chemical Information and Modeling. 53(9). 2349–2359. 12 indexed citations
13.
14.
Whalen, K.L., et al.. (2011). Nature of Allosteric Inhibition in Glutamate Racemase: Discovery and Characterization of a Cryptic Inhibitory Pocket Using Atomistic MD Simulations and pKaCalculations. The Journal of Physical Chemistry B. 115(13). 3416–3424. 20 indexed citations
15.
Whalen, K.L., et al.. (2009). Exploiting Enzyme Plasticity in Virtual Screening: High Efficiency Inhibitors of Glutamate Racemase. ACS Medicinal Chemistry Letters. 1(1). 9–13. 22 indexed citations
16.
Spies, M. Ashley, et al.. (2009). Determinants of Catalytic Power and Ligand Binding in Glutamate Racemase. Journal of the American Chemical Society. 131(14). 5274–5284. 25 indexed citations
17.
Spies, M. Ashley & Michael D. Toney. (2007). Intrinsic Primary and Secondary Hydrogen Kinetic Isotope Effects for Alanine Racemase from Global Analysis of Progress Curves. Journal of the American Chemical Society. 129(35). 10678–10685. 22 indexed citations
18.
Dodd, Dylan, et al.. (2007). Functional Comparison of the Two Bacillus anthracis Glutamate Racemases. Journal of Bacteriology. 189(14). 5265–5275. 27 indexed citations
19.
Christenson, Steven D., Weiming Wu, M. Ashley Spies, Ben Shen, & Michael D. Toney. (2003). Kinetic Analysis of the 4-Methylideneimidazole-5-one-Containing Tyrosine Aminomutase in Enediyne Antitumor Antibiotic C-1027 Biosynthesis. Biochemistry. 42(43). 12708–12718. 64 indexed citations
20.
Spies, M. Ashley & Richard L. Schowen. (2002). The Trapping of a Spontaneously “Flipped-Out” Base from Double Helical Nucleic Acids by Host−Guest Complexation with β-Cyclodextrin:  The Intrinsic Base-Flipping Rate Constant for DNA and RNA. Journal of the American Chemical Society. 124(47). 14049–14053. 55 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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