Paul L. Boyer

6.2k total citations
77 papers, 4.8k citations indexed

About

Paul L. Boyer is a scholar working on Infectious Diseases, Virology and Molecular Biology. According to data from OpenAlex, Paul L. Boyer has authored 77 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 73 papers in Infectious Diseases, 68 papers in Virology and 26 papers in Molecular Biology. Recurrent topics in Paul L. Boyer's work include HIV/AIDS drug development and treatment (73 papers), HIV Research and Treatment (68 papers) and HIV/AIDS Research and Interventions (33 papers). Paul L. Boyer is often cited by papers focused on HIV/AIDS drug development and treatment (73 papers), HIV Research and Treatment (68 papers) and HIV/AIDS Research and Interventions (33 papers). Paul L. Boyer collaborates with scholars based in United States, Belgium and France. Paul L. Boyer's co-authors include Stephen H. Hughes, Eddy Arnold, Stefan G. Sarafianos, Kalyan Das, Arthur D. Clark, Jianping Ding, Chris Tantillo, Andrea L. Ferris, Christopher J. Michejda and Raymond G. Nanni 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

Paul L. Boyer

76 papers receiving 4.7k citations

Peers

Paul L. Boyer
Arthur D. Clark United States
Jay A. Grobler United States
Margaret Tisdale United Kingdom
Lee T. Bacheler United States
Stuart F.J. Le Grice United States
Chris Tantillo United States
S H Hughes United States
Paul L. Darke United States
Arthur D. Clark United States
Paul L. Boyer
Citations per year, relative to Paul L. Boyer Paul L. Boyer (= 1×) peers Arthur D. Clark

Countries citing papers authored by Paul L. Boyer

Since Specialization
Citations

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

Fields of papers citing papers by Paul L. Boyer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Paul L. Boyer

This figure shows the co-authorship network connecting the top 25 collaborators of Paul L. Boyer. A scholar is included among the top collaborators of Paul L. 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 Paul L. Boyer. Paul L. Boyer 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.
Zhao, Xue Zhi, Steven J. Smith, Mathieu Métifiot, et al.. (2014). 4-Amino-1-hydroxy-2-oxo-1,8-naphthyridine-Containing Compounds Having High Potency against Raltegravir-Resistant Integrase Mutants of HIV-1. Journal of Medicinal Chemistry. 57(12). 5190–5202. 38 indexed citations
2.
Boyer, Paul L., et al.. (2013). Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease. Virology. 444(1-2). 241–249. 6 indexed citations
3.
Das, Kalyan, Joseph D. Bauman, Arthur D. Clark, et al.. (2010). Structural basis of HIV-1 resistance to AZT by excision. Nature Structural & Molecular Biology. 17(10). 1202–1209. 95 indexed citations
4.
Das, Kalyan, Rajiv P. Bandwar, Kirsten White, et al.. (2009). Structural Basis for the Role of the K65R Mutation in HIV-1 Reverse Transcriptase Polymerization, Excision Antagonism, and Tenofovir Resistance. Journal of Biological Chemistry. 284(50). 35092–35100. 71 indexed citations
5.
Gao, Lu, M. Balakrishnan, Paul L. Boyer, et al.. (2008). Apparent Defects in Processive DNA Synthesis, Strand Transfer, and Primer Elongation of Met-184 Mutants of HIV-1 Reverse Transcriptase Derive Solely from a dNTP Utilization Defect. Journal of Biological Chemistry. 283(14). 9196–9205. 25 indexed citations
6.
Hughes, Stephen H., et al.. (2008). Synthesis of conformationally locked carbocyclic nucleoside phosphonates to probe the active site of HIV-1 RT. Nucleic Acids Symposium Series. 52(1). 623–624. 2 indexed citations
7.
Das, Kalyan, Stefan G. Sarafianos, Arthur D. Clark, et al.. (2006). Crystal Structures of Clinically Relevant Lys103Asn/Tyr181Cys Double Mutant HIV-1 Reverse Transcriptase in Complexes with ATP and Non-nucleoside Inhibitor HBY 097. Journal of Molecular Biology. 365(1). 77–89. 72 indexed citations
8.
Boyer, Paul L., John G. Julias, Víctor E. Márquez, & Stephen H. Hughes. (2004). Fixed Conformation Nucleoside Analogs Effectively Inhibit Excision-proficient HIV-1 Reverse Transcriptases. Journal of Molecular Biology. 345(3). 441–450. 48 indexed citations
9.
Skillman, A. Geoffrey, Karl Maurer, Diana C. Roe, et al.. (2002). A novel mechanism for inhibition of HIV-1 reverse transcriptase. Bioorganic Chemistry. 30(6). 443–458. 27 indexed citations
10.
Sarafianos, Stefan G., Kalyan Das, Chris Tantillo, et al.. (2001). Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA. The EMBO Journal. 20(6). 1449–1461. 341 indexed citations
11.
Boyer, Paul L., Hongqiang Gao, Peter Frank, Patrick K. Clark, & Stephen H. Hughes. (2001). The Basic Loop of the RNase H Domain of MLV RT Is Important Both for RNase H and for Polymerase Activity. Virology. 282(1). 206–213. 13 indexed citations
12.
Hsiou, Y., Kalyan Das, Arthur D. Clark, et al.. (2001). The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance. Journal of Molecular Biology. 309(2). 437–445. 147 indexed citations
13.
Boyer, Paul L., Julianna Lisziewicz, Franco Lori, & Stephen H. Hughes. (1999). Analysis of amino insertion mutations in the fingers subdomain of HIV-1 reverse transcriptase 1 1Edited by J. Karn. Journal of Molecular Biology. 286(4). 995–1008. 24 indexed citations
14.
Sarafianos, Stefan G., et al.. (1999). Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site. Chemistry & Biology. 6(5). R137–R146. 94 indexed citations
15.
Das, Kalyan, Jianping Ding, Y. Hsiou, et al.. (1996). Crystal Structures of 8-Cl and 9-Cl TIBO Complexed with Wild-type HIV-1 RT and 8-Cl TIBO Complexed with the Tyr181Cys HIV-1 RT Drug-resistant Mutant. Journal of Molecular Biology. 264(5). 1085–1100. 159 indexed citations
16.
Boyer, Paul L. & Stephen H. Hughes. (1996). Nucleoside-analogue resistance involves the p66 subunit of HIV-1 RT. Nature Structural Biology. 3(7). 579–580. 5 indexed citations
17.
Smith, Marilyn B. Kroeger, Stephen H. Hughes, Paul L. Boyer, et al.. (1995). Molecular modeling studies of HIV‐1 reverse transcriptase nonnucleoside inhibitors: Total energy of complexation as a predictor of drug placement and activity. Protein Science. 4(10). 2203–2222. 55 indexed citations
18.
Givol, I, Paul L. Boyer, & Stephen H. Hughes. (1995). Isolation and characterization of the chicken c-sno gene. Gene. 156(2). 271–276. 7 indexed citations
20.
Boyer, Paul L., Andrea L. Ferris, Peter Frank, et al.. (1994). Mutational Analysis of the Fingers and Palm Subdomains of Human Immunodeficiency Virus Type-1 (HIV-1) Reverse Transcriptase. Journal of Molecular Biology. 243(3). 472–483. 76 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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