John J. Barker

2.2k total citations
24 papers, 1.2k citations indexed

About

John J. Barker is a scholar working on Molecular Biology, Organic Chemistry and Computational Theory and Mathematics. According to data from OpenAlex, John J. Barker has authored 24 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 7 papers in Organic Chemistry and 5 papers in Computational Theory and Mathematics. Recurrent topics in John J. Barker's work include Computational Drug Discovery Methods (5 papers), Organometallic Complex Synthesis and Catalysis (4 papers) and Cancer therapeutics and mechanisms (3 papers). John J. Barker is often cited by papers focused on Computational Drug Discovery Methods (5 papers), Organometallic Complex Synthesis and Catalysis (4 papers) and Cancer therapeutics and mechanisms (3 papers). John J. Barker collaborates with scholars based in United Kingdom, United States and Germany. John J. Barker's co-authors include R.L. Brady, A. V. Konarev, Anthony R. Clarke, P. R. Shewry, Anthony C.F. Perry, Mark J. Banfield, Mark Whittaker, Richard Law, Thomas Hesterkamp and Osamu Ichihara and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

John J. Barker

23 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John J. Barker United Kingdom 17 890 224 180 132 109 24 1.2k
Kenneth Borrelli United States 17 898 1.0× 247 1.1× 373 2.1× 147 1.1× 84 0.8× 17 1.3k
Timothy E. Benson United States 20 778 0.9× 237 1.1× 254 1.4× 146 1.1× 226 2.1× 27 1.5k
Christopher R. Otey United States 12 1.5k 1.6× 125 0.6× 112 0.6× 241 1.8× 66 0.6× 15 1.9k
Molly M. He United States 15 575 0.6× 108 0.5× 83 0.5× 150 1.1× 60 0.6× 19 1.0k
Jonathan J. Burbaum United States 23 1.4k 1.6× 308 1.4× 106 0.6× 119 0.9× 117 1.1× 34 1.9k
Jonathan P. Lee United States 18 1.3k 1.5× 404 1.8× 168 0.9× 163 1.2× 233 2.1× 25 1.9k
Reetta Raag United States 15 965 1.1× 83 0.4× 193 1.1× 218 1.7× 55 0.5× 19 1.8k
Iris Antes Germany 25 1.1k 1.3× 327 1.5× 201 1.1× 110 0.8× 143 1.3× 67 1.8k
Gregory B. Quinn United States 9 746 0.8× 70 0.3× 174 1.0× 144 1.1× 54 0.5× 18 1.0k
R. P. Bywater United Kingdom 10 762 0.9× 148 0.7× 173 1.0× 150 1.1× 59 0.5× 16 1.1k

Countries citing papers authored by John J. Barker

Since Specialization
Citations

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

Fields of papers citing papers by John J. Barker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John J. Barker

This figure shows the co-authorship network connecting the top 25 collaborators of John J. Barker. A scholar is included among the top collaborators of John J. Barker 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 John J. Barker. John J. Barker 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.
Mak, Victor, Aileen Soriano, M. Zebisch, et al.. (2023). Structural insights into selective small molecule activation of PKG1α. Communications Biology. 6(1). 798–798.
2.
Byrne, Noel, John C. Reid, Sung‐Sau So, et al.. (2020). Development of a robust crystallization platform for immune receptor TREM2 using a crystallization chaperone strategy. Protein Expression and Purification. 179. 105796–105796. 6 indexed citations
3.
Barker, John J., et al.. (2017). High-Throughput Production of Proteins in E. coli for Structural Studies. Methods in molecular biology. 1586. 359–371. 1 indexed citations
4.
Mesleh, Michael F., Jason B. Cross, Jing Zhang, et al.. (2016). Fragment-based discovery of DNA gyrase inhibitors targeting the ATPase subunit of GyrB. Bioorganic & Medicinal Chemistry Letters. 26(4). 1314–1318. 52 indexed citations
5.
Ichihara, Osamu, John J. Barker, Richard Law, & Mark Whittaker. (2011). Compound Design by Fragment‐Linking. Molecular Informatics. 30(4). 298–306. 68 indexed citations
6.
Madden, J. Patrick, Robert Godemann, M. A. Smith, et al.. (2010). Fragment-based discovery and optimization of BACE1 inhibitors. Bioorganic & Medicinal Chemistry Letters. 20(17). 5329–5333. 37 indexed citations
7.
Barker, John J., Oliver Barker, Stephen M. Courtney, et al.. (2010). Discovery of a Novel Hsp90 Inhibitor by Fragment Linking. ChemMedChem. 5(10). 1697–1700. 42 indexed citations
8.
Smith, M. A., Volker Mack, Andreas Ebneth, et al.. (2010). The Structure of Mammalian Serine Racemase. Journal of Biological Chemistry. 285(17). 12873–12881. 71 indexed citations
9.
Law, Richard, Oliver Barker, John J. Barker, et al.. (2009). The multiple roles of computational chemistry in fragment-based drug design. Journal of Computer-Aided Molecular Design. 23(8). 459–473. 45 indexed citations
10.
Cheng, R.K., Brunella Felicetti, Shilpa Palan, et al.. (2009). High‐resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand. Protein Science. 19(1). 168–173. 16 indexed citations
11.
Andersen, Ole A., D.L. Schönfeld, Brunella Felicetti, et al.. (2009). Cross-linking of protein crystals as an aid in the generation of binary protein–ligand crystal complexes, exemplified by the human PDE10a–papaverine structure. Acta Crystallographica Section D Biological Crystallography. 65(8). 872–874. 22 indexed citations
12.
Barker, John J., et al.. (2006). Fragment screening by biochemical assay. Expert Opinion on Drug Discovery. 1(3). 225–236. 39 indexed citations
13.
Barker, John J.. (2006). Antibacterial drug discovery and structure-based design. Drug Discovery Today. 11(9-10). 391–404. 71 indexed citations
14.
Sun, Shaoxian, Jonathan Almaden, Thomas J. Carlson, John J. Barker, & Michael R. Gehring. (2005). Assay development and data analysis of receptor–ligand binding based on scintillation proximity assay. Metabolic Engineering. 7(1). 38–44. 16 indexed citations
15.
Zhao, Lihua, Nigel M. Allanson, John Maclean, et al.. (2003). Inhibitors of phosphopantetheine adenylyltransferase. European Journal of Medicinal Chemistry. 38(4). 345–349. 36 indexed citations
16.
Izard, Tina, Arie Geerlof, Ann Lewendon, & John J. Barker. (1999). Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallographica Section D Biological Crystallography. 55(6). 1226–1228. 9 indexed citations
17.
Barker, John J., et al.. (1999). High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. Journal of Molecular Biology. 290(2). 525–533. 341 indexed citations
18.
Banfield, Mark J., John J. Barker, Anthony C.F. Perry, & R.L. Brady. (1998). Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 6(10). 1245–1254. 165 indexed citations
19.
Head, Jared, et al.. (1998). Engineering an intertwined form of CD2 for stability and assembly. Nature Structural Biology. 5(9). 778–782. 48 indexed citations
20.

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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