Joshua A. Boyer

835 total citations
16 papers, 514 citations indexed

About

Joshua A. Boyer is a scholar working on Molecular Biology, Immunology and Spectroscopy. According to data from OpenAlex, Joshua A. Boyer has authored 16 papers receiving a total of 514 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 4 papers in Immunology and 3 papers in Spectroscopy. Recurrent topics in Joshua A. Boyer's work include Protein Structure and Dynamics (6 papers), RNA and protein synthesis mechanisms (5 papers) and interferon and immune responses (4 papers). Joshua A. Boyer is often cited by papers focused on Protein Structure and Dynamics (6 papers), RNA and protein synthesis mechanisms (5 papers) and interferon and immune responses (4 papers). Joshua A. Boyer collaborates with scholars based in United States and China. Joshua A. Boyer's co-authors include Andrew L. Lee, Qi Zhang, Pengda Liu, Philip C. Bevilacqua, Robert K. McGinty, Andrew P. Cesmat, Joshua D. Strauss, Cathy J. Spangler, Christopher A. Strulson and Subba Rao Nallagatla and has published in prestigious journals such as Science, Journal of the American Chemical Society and The EMBO Journal.

In The Last Decade

Joshua A. Boyer

16 papers receiving 511 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Joshua A. Boyer United States	11	387	185	75	53	35	16	514
Yuichiro Hourai Japan	5	439 1.1×	59 0.3×	36 0.5×	82 1.5×	30 0.9×	6	570
Y. Yang China	7	358 0.9×	318 1.7×	61 0.8×	68 1.3×	49 1.4×	15	736
Shane Ó Conchúir United States	5	419 1.1×	50 0.3×	54 0.7×	65 1.2×	57 1.6×	6	558
Erandi Lira‐Navarrete Spain	14	505 1.3×	166 0.9×	52 0.7×	39 0.7×	29 0.8×	20	642
Akash Bhattacharya United States	13	521 1.3×	130 0.7×	216 2.9×	80 1.5×	53 1.5×	35	809
Huiyi Li China	7	244 0.6×	134 0.7×	46 0.6×	28 0.5×	11 0.3×	21	383
Ignacia Echeverria United States	16	570 1.5×	47 0.3×	57 0.8×	74 1.4×	32 0.9×	29	743
Helena Coelho Portugal	14	435 1.1×	211 1.1×	51 0.7×	15 0.3×	23 0.7×	23	555
Halina Mikolajek United Kingdom	15	336 0.9×	52 0.3×	53 0.7×	86 1.6×	68 1.9×	29	532
Thorsten Biet Germany	8	257 0.7×	56 0.3×	71 0.9×	35 0.7×	17 0.5×	10	418

Countries citing papers authored by Joshua A. Boyer

Since Specialization

Citations

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

Fields of papers citing papers by Joshua A. Boyer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joshua A. Boyer. 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 Joshua A. Boyer. The network helps show where Joshua A. Boyer may publish in the future.

Co-authorship network of co-authors of Joshua A. Boyer

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

All Works

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16 of 16 papers shown

Boyer, Joshua A., Stephanie Cambier, Jordyn J. VanPortfliet, et al.. (2025). Structures of ATP-binding cassette transporter ABCC1 reveal the molecular basis of cyclic dinucleotide cGAMP export. Immunity. 58(1). 59–73.e5. 8 indexed citations

Boyer, Joshua A., Hui Yang, Mengxi Liu, et al.. (2024). Using NMR to Monitor TET-Dependent Methylcytosine Dioxygenase Activity and Regulation. ACS Chemical Biology. 19(1). 15–21. 6 indexed citations

Boyer, Joshua A., Brenda Temple, Thomas Bonacci, et al.. (2021). Functional conservation and divergence of the helix‐turn‐helix motif of E2 ubiquitin‐conjugating enzymes. The EMBO Journal. 41(3). e108823–e108823. 9 indexed citations

Spangler, Cathy J., Joshua A. Boyer, Joshua D. Strauss, et al.. (2021). Cryo-EM Structure of cGAS-Nucleosome Complex Reveals Mechanism of Nucleosome-Dependent cGAS Inhibition. Biophysical Journal. 120(3). 7a–7a. 2 indexed citations

Boyer, Joshua A., Cathy J. Spangler, Joshua D. Strauss, et al.. (2020). Structural basis of nucleosome-dependent cGAS inhibition. Science. 370(6515). 450–454. 164 indexed citations

Ma, Zhe, Joshua A. Boyer, Guoxin Ni, et al.. (2020). Streptavidin Promotes DNA Binding and Activation of cGAS to Enhance Innate Immunity. iScience. 23(9). 101463–101463. 27 indexed citations

Boyer, Joshua A., et al.. (2020). Visualizing a protonated RNA state that modulates microRNA-21 maturation. Nature Chemical Biology. 17(1). 80–88. 38 indexed citations

Strulson, Christopher A., et al.. (2014). Molecular crowders and cosolutes promote folding cooperativity of RNA under physiological ionic conditions. RNA. 20(3). 331–347. 59 indexed citations

Whitley, Matthew J., et al.. (2013). Colocalization of Fast and Slow Timescale Dynamics in the Allosteric Signaling Protein CheY. Journal of Molecular Biology. 425(13). 2372–2381. 28 indexed citations

10.

Boyer, Joshua A., et al.. (2012). Segmental Motions, Not a Two-State Concerted Switch, Underlie Allostery in CheY. Structure. 20(8). 1363–1373. 42 indexed citations

11.

Toroney, Rebecca, Subba Rao Nallagatla, Joshua A. Boyer, Craig E. Cameron, & Philip C. Bevilacqua. (2010). Regulation of PKR by HCV IRES RNA: Importance of Domain II and NS5A. Journal of Molecular Biology. 400(3). 393–412. 50 indexed citations

12.

Boyer, Joshua A., et al.. (2010). Detection of Native-State Nonadditivity in Double Mutant Cycles via Hydrogen Exchange. Journal of the American Chemical Society. 132(23). 8010–8019. 12 indexed citations

13.

Boyer, Joshua A. & Andrew L. Lee. (2008). Monitoring Aromatic Picosecond to Nanosecond Dynamics in Proteins via ¹³C Relaxation: Expanding Perturbation Mapping of the Rigidifying Core Mutation, V54A, in Eglin c. Biochemistry. 47(17). 4876–4886. 33 indexed citations

14.

Ropson, Ira J., et al.. (2008). Comparison of the folding mechanism of highly homologous proteins in the lipid‐binding protein family. Proteins Structure Function and Bioinformatics. 75(4). 799–806. 5 indexed citations

15.

Ropson, Ira J., Joshua A. Boyer, & Paula M. Dalessio. (2006). A Residual Structure in Unfolded Intestinal Fatty Acid Binding Protein Consists of Amino Acids That Are Neighbors in the Native State. Biochemistry. 45(8). 2608–2617. 15 indexed citations

16.

Dalessio, Paula M., et al.. (2005). Swapping Core Residues in Homologous Proteins Swaps Folding Mechanism. Biochemistry. 44(8). 3082–3090. 16 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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