M.J. Cuneo

2.4k total citations
64 papers, 1.7k citations indexed

About

M.J. Cuneo is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, M.J. Cuneo has authored 64 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 25 papers in Materials Chemistry and 7 papers in Oncology. Recurrent topics in M.J. Cuneo's work include Enzyme Structure and Function (25 papers), Protein Structure and Dynamics (15 papers) and DNA Repair Mechanisms (9 papers). M.J. Cuneo is often cited by papers focused on Enzyme Structure and Function (25 papers), Protein Structure and Dynamics (15 papers) and DNA Repair Mechanisms (9 papers). M.J. Cuneo collaborates with scholars based in United States, Denmark and India. M.J. Cuneo's co-authors include Homme W. Hellinga, Robert E. London, Tanja Mittag, L.S. Beese, Samuel H. Wilson, Dean A. A. Myles, Bret Freudenthal, William A. Beard, Nadezhda S. Dyrkheeva and Anita Changela and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

M.J. Cuneo

63 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M.J. Cuneo United States	25	1.1k	359	219	137	112	64	1.7k
Catherine Vénien‐Bryan France	29	1.8k 1.6×	271 0.8×	127 0.6×	118 0.9×	100 0.9×	79	2.5k
M. Schiltz Switzerland	19	1.0k 0.9×	566 1.6×	88 0.4×	145 1.1×	164 1.5×	46	1.8k
Yuko Yoshikawa Japan	24	1.0k 0.9×	331 0.9×	155 0.7×	132 1.0×	113 1.0×	85	1.8k
Grzegorz Piszczek United States	33	2.1k 1.9×	509 1.4×	266 1.2×	245 1.8×	125 1.1×	92	3.3k
Lilian Jacquamet France	25	680 0.6×	552 1.5×	196 0.9×	219 1.6×	62 0.6×	35	1.7k
Yifan Song China	18	2.3k 2.0×	633 1.8×	157 0.7×	237 1.7×	72 0.6×	46	3.0k
Alejandro Panjkovich Germany	16	1.9k 1.6×	614 1.7×	125 0.6×	204 1.5×	40 0.4×	23	2.6k
Gevorg Grigoryan United States	22	1.7k 1.5×	517 1.4×	98 0.4×	105 0.8×	53 0.5×	54	2.1k
Gautam Basu India	26	1.3k 1.1×	340 0.9×	138 0.6×	76 0.6×	66 0.6×	81	1.9k
Scott E. Boyken United States	20	2.3k 2.0×	445 1.2×	268 1.2×	173 1.3×	110 1.0×	28	3.0k

Countries citing papers authored by M.J. Cuneo

Since Specialization

Citations

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

Fields of papers citing papers by M.J. Cuneo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M.J. Cuneo

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Myles, Dean A. A., et al.. (2022). Mapping periplasmic binding protein oligosaccharide recognition with neutron crystallography. Scientific Reports. 12(1). 17647–17647. 2 indexed citations

Martin, Erik, F. Emil Thomasen, Nicole M. Milkovic, et al.. (2021). Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation. Nucleic Acids Research. 49(5). 2931–2945. 108 indexed citations

Lim, Ailam, et al.. (2021). Meningoencephalitis, Vasculitis, and Abortions Caused by Chlamydia pecorum in a Herd of Cattle. Veterinary Pathology. 58(3). 549–557. 9 indexed citations

Jafta, Charl J., Xiao‐Guang Sun, Hailong Lyu, et al.. (2021). Insight into the Solid Electrolyte Interphase Formation in Bis(fluorosulfonyl)Imide Based Ionic Liquid Electrolytes. Advanced Functional Materials. 31(23). 48 indexed citations

Serpersu, Engin H., et al.. (2020). “Catch and Release”: a Variation of the Archetypal Nucleotidyl Transfer Reaction. ACS Catalysis. 10(6). 3548–3555. 3 indexed citations

Hiromoto, Takeshi, Koji Nishikawa, Seiya Inoue, et al.. (2020). Towards cryogenic neutron crystallography on the reduced form of [NiFe]-hydrogenase. Acta Crystallographica Section D Structural Biology. 76(10). 946–953. 2 indexed citations

Agarwal, Pratul K., et al.. (2019). Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad. Angewandte Chemie. 131(45). 16406–16412. 3 indexed citations

Agarwal, Pratul K., et al.. (2019). Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad. Angewandte Chemie International Edition. 58(45). 16260–16266. 18 indexed citations

McShan, Andrew C., Scott E. Boyken, Kathy Y. Wei, et al.. (2019). De novo design of a homo-trimeric amantadine-binding protein. eLife. 8. 19 indexed citations

10.

Heller, William T., M.J. Cuneo, Lisa DeBeer‐Schmitt, et al.. (2018). The suite of small-angle neutron scattering instruments at Oak Ridge National Laboratory. Journal of Applied Crystallography. 51(2). 242–248. 145 indexed citations

11.

Serpersu, Engin H., et al.. (2018). Encoding of Promiscuity in an Aminoglycoside Acetyltransferase. Journal of Medicinal Chemistry. 61(22). 10218–10227. 10 indexed citations

12.

Duff, Michael R., Jose M. Borreguero, M.J. Cuneo, et al.. (2018). Modulating Enzyme Activity by Altering Protein Dynamics with Solvent. Biochemistry. 57(29). 4263–4275. 30 indexed citations

13.

Serpersu, Engin H., et al.. (2018). A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad. Science Advances. 4(4). eaas8667–eaas8667. 35 indexed citations

14.

Rodriguez, Yesenia, Michael J. Howard, M.J. Cuneo, Rajendra Prasad, & Samuel H. Wilson. (2017). Unencumbered Pol β lyase activity in nucleosome core particles. Nucleic Acids Research. 45(15). 8901–8915. 20 indexed citations

15.

Bacik, J.P., Sophanit Mekasha, Zarah Forsberg, et al.. (2017). Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation. Biochemistry. 56(20). 2529–2532. 47 indexed citations

16.

Bacik, J.P., Sophanit Mekasha, Zarah Forsberg, et al.. (2015). Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase. Acta Crystallographica Section F Structural Biology Communications. 71(11). 1448–1452. 6 indexed citations

17.

Coates, Leighton, M.J. Cuneo, Matthew Frost, et al.. (2015). The Macromolecular Neutron Diffractometer MaNDi at the Spallation Neutron Source. Journal of Applied Crystallography. 48(4). 1302–1306. 57 indexed citations

18.

Antunes, Mauricio S., Kevin J. Morey, James J. Smith, et al.. (2011). Programmable Ligand Detection System in Plants through a Synthetic Signal Transduction Pathway. PLoS ONE. 6(1). e16292–e16292. 91 indexed citations

19.

Mueller, Geoffrey A., Joseph M. Krahn, Lori L. Edwards, et al.. (2010). Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens. Journal of Biological Chemistry. 285(33). 25394–25401. 46 indexed citations

20.

Cuneo, M.J., et al.. (2007). Structure‐based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose‐binding protein. Protein Science. 16(10). 2240–2250. 36 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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