Joseph L. Johnson

1.7k total citations · 1 hit paper
47 papers, 1.4k citations indexed

About

Joseph L. Johnson is a scholar working on Organic Chemistry, Pharmacology and Molecular Biology. According to data from OpenAlex, Joseph L. Johnson has authored 47 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Organic Chemistry, 12 papers in Pharmacology and 11 papers in Molecular Biology. Recurrent topics in Joseph L. Johnson's work include Cholinesterase and Neurodegenerative Diseases (11 papers), Computational Drug Discovery Methods (8 papers) and Aerospace and Aviation Technology (8 papers). Joseph L. Johnson is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (11 papers), Computational Drug Discovery Methods (8 papers) and Aerospace and Aviation Technology (8 papers). Joseph L. Johnson collaborates with scholars based in United States and Italy. Joseph L. Johnson's co-authors include George N. Welch, Joseph Loscalzo, John F. Keaney, Gilbert R. Upchurch, Jane E. Freedman, Attila J. Fabian, Terrone L. Rosenberry, Bernadette Cusack, Gerald D. Watt and Mathias Toft and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Nature Biotechnology.

In The Last Decade

Joseph L. Johnson

43 papers receiving 1.3k citations

Hit Papers

Homocyst(e)ine Decreases Bioavailable Nitric Oxide by a M... 1997 2026 2006 2016 1997 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph L. Johnson United States 16 446 270 235 221 178 47 1.4k
Abdel Ali Belaidi Australia 22 166 0.4× 1.4k 5.1× 84 0.4× 152 0.7× 354 2.0× 38 2.8k
Chuang Guo China 24 112 0.3× 736 2.7× 137 0.6× 193 0.9× 652 3.7× 41 2.0k
Nobuo Itoh Japan 20 55 0.1× 504 1.9× 52 0.2× 146 0.7× 358 2.0× 96 1.5k
Mariacristina Siotto Italy 22 54 0.1× 255 0.9× 114 0.5× 94 0.4× 751 4.2× 47 1.5k
Ofer Spiegelstein United States 19 395 0.9× 305 1.1× 56 0.2× 120 0.5× 63 0.4× 60 1.2k
Elena A. Ostrakhovitch Canada 20 138 0.3× 491 1.8× 47 0.2× 24 0.1× 145 0.8× 32 1.4k
Juan-Li Gu United States 25 56 0.1× 1.4k 5.2× 148 0.6× 85 0.4× 428 2.4× 29 3.0k
Swapna V. Shenvi United States 10 76 0.2× 748 2.8× 71 0.3× 180 0.8× 286 1.6× 14 1.5k
Giuliana Leoncini Italy 23 190 0.4× 406 1.5× 263 1.1× 24 0.1× 311 1.7× 91 1.4k
Natalia Mena Chile 20 65 0.1× 522 1.9× 60 0.3× 361 1.6× 275 1.5× 26 1.9k

Countries citing papers authored by Joseph L. Johnson

Since Specialization
Citations

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

Fields of papers citing papers by Joseph L. Johnson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Joseph L. Johnson

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph L. Johnson. A scholar is included among the top collaborators of Joseph L. Johnson 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 Joseph L. Johnson. Joseph L. Johnson 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.
Anderson, Heidi, et al.. (2020). Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase. The Protein Journal. 39(5). 542–553. 6 indexed citations
2.
Jonnalagadda, Sravan K., et al.. (2020). Synthesis, in vitro, and in vivo evaluation of novel N-phenylindazolyl diarylureas as potential anti-cancer agents. Scientific Reports. 10(1). 17969–17969. 16 indexed citations
3.
Venkatasubban, Kunisi S., et al.. (2018). Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size. Archives of Biochemistry and Biophysics. 655. 67–74. 12 indexed citations
4.
Johnson, Joseph L., et al.. (2016). Fluorescence fluctuation analysis of BACE1-GFP fusion protein in cultured HEK293 cells. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 9956. 99560K–99560K. 1 indexed citations
5.
Tekkam, Srinivas, Mohammad A. Alam, Steven M. Berry, et al.. (2013). Stereoselective Synthesis of Pyroglutamate Natural Product Analogs from α- Aminoacids and their Anti-Cancer Evaluation. Anti-Cancer Agents in Medicinal Chemistry. 13(10). 1514–1530. 8 indexed citations
6.
Tekkam, Srinivas, Joseph L. Johnson, Subash C. Jonnalagadda, & Venkatram R. Mereddy. (2013). Concise Synthesis of α-Methylene-β-hydroxy-γ-carboxy-γ-lactams. Journal of Heterocyclic Chemistry. 50(4). 955–958. 3 indexed citations
7.
Johnson, Joseph L., et al.. (2010). Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase. Chemico-Biological Interactions. 187(1-3). 135–141. 16 indexed citations
8.
Rosenberry, Terrone L., et al.. (2008). Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis. Chemico-Biological Interactions. 175(1-3). 235–241. 19 indexed citations
9.
Papapetropoulos, Spiridon, Carlos Singer, Owen A. Ross, et al.. (2006). Clinical Heterogeneity of the LRRK2 G2019S Mutation. Archives of Neurology. 63(9). 1242–1242. 24 indexed citations
10.
Ross, Owen A., Mathias Toft, Andrew J. Whittle, et al.. (2006). Lrrk2 and Lewy body disease. Annals of Neurology. 59(2). 388–393. 205 indexed citations
11.
Nyborg, Andrew C., et al.. (2006). Evidence for a synergistic salt–protein interaction—complex patterns of activation vs. inhibition of nitrogenase by salt. Biophysical Chemistry. 122(3). 184–194. 2 indexed citations
12.
Venkatasubban, Kunisi S., et al.. (2005). (49) Steric effects in the decarbamoylation of carbamoylated acetylcholinesterases. Chemico-Biological Interactions. 157-158. 433–434. 2 indexed citations
14.
Johnson, Joseph L., Bernadette Cusack, Thomas F. Hughes, et al.. (2003). Inhibitors Tethered Near the Acetylcholinesterase Active Site Serve as Molecular Rulers of the Peripheral and Acylation Sites. Journal of Biological Chemistry. 278(40). 38948–38955. 43 indexed citations
15.
Nyborg, Andrew C., et al.. (2000). Evidence for a Two-Electron Transfer Using the All-Ferrous Fe Protein during Nitrogenase Catalysis. Journal of Biological Chemistry. 275(50). 39307–39312. 23 indexed citations
16.
Nyborg, Andrew C., et al.. (2000). Reactions of Azotobacter vinelandii nitrogenase using Ti(III) as reductant. Journal of Inorganic Biochemistry. 78(4). 371–381. 9 indexed citations
17.
Johnson, Joseph L., et al.. (1999). Forming the Phosphate Layer in Reconstituted Horse Spleen Ferritin and the Role of Phosphate in Promoting Core Surface Redox Reactions. Biochemistry. 38(20). 6706–6713. 26 indexed citations
18.
19.
Johnson, Joseph L., et al.. (1986). Preliminary aerodynamic design considerations for advanced laminar flow aircraft configurations. NASA Technical Reports Server (NASA). 6 indexed citations
20.
Johnson, Joseph L., et al.. (1979). Full-Scale Wind-Tunnel Investigation of an Ayres S2R-800 Thrush Agricultural Airplane. SAE technical papers on CD-ROM/SAE technical paper series. 1. 3 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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