Robert Clubb

4.2k total citations
91 papers, 3.3k citations indexed

About

Robert Clubb is a scholar working on Molecular Biology, Infectious Diseases and Cell Biology. According to data from OpenAlex, Robert Clubb has authored 91 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 19 papers in Infectious Diseases and 17 papers in Cell Biology. Recurrent topics in Robert Clubb's work include Biochemical and Structural Characterization (31 papers), Hemoglobin structure and function (17 papers) and Botanical Research and Chemistry (16 papers). Robert Clubb is often cited by papers focused on Biochemical and Structural Characterization (31 papers), Hemoglobin structure and function (17 papers) and Botanical Research and Chemistry (16 papers). Robert Clubb collaborates with scholars based in United States, Australia and United Kingdom. Robert Clubb's co-authors include Thomas Spirig, Michael E. Jung, Udayar Ilangovan, Valerie A. Villareal, Nuttee Suree, Hung Ton‐That, Rosemarie Pilpa, Scott A. Robson, Junji Iwahara and Olaf Schneewind and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Robert Clubb

88 papers receiving 3.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert Clubb United States 33 2.5k 533 503 421 388 91 3.3k
Yves Jacob France 40 1.4k 0.6× 481 0.9× 932 1.9× 145 0.3× 387 1.0× 103 3.9k
Juan C. Engel United States 39 1.4k 0.6× 2.2k 4.1× 376 0.7× 279 0.7× 302 0.8× 67 4.4k
Alejandro Buschiazzo France 33 2.2k 0.9× 393 0.7× 200 0.4× 77 0.2× 484 1.2× 82 3.3k
Alla Gustchina United States 37 1.7k 0.7× 172 0.3× 684 1.4× 68 0.2× 368 0.9× 94 3.2k
José L. Nieva Spain 36 2.5k 1.0× 241 0.5× 896 1.8× 89 0.2× 235 0.6× 118 4.1k
Kylene Kehn‐Hall United States 37 1.8k 0.7× 819 1.5× 1.7k 3.4× 298 0.7× 275 0.7× 140 4.3k
Raymond C. Sowder United States 37 2.7k 1.1× 195 0.4× 1.5k 3.0× 136 0.3× 425 1.1× 56 5.7k
Gordon Langsley France 42 1.8k 0.7× 2.2k 4.1× 392 0.8× 224 0.5× 155 0.4× 136 4.9k
François Ferrón France 31 1.5k 0.6× 577 1.1× 2.3k 4.6× 118 0.3× 242 0.6× 64 4.3k
Ajit K. Basak United Kingdom 23 829 0.3× 296 0.6× 896 1.8× 129 0.3× 199 0.5× 33 1.8k

Countries citing papers authored by Robert Clubb

Since Specialization
Citations

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

Fields of papers citing papers by Robert Clubb

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert Clubb. 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 Robert Clubb. The network helps show where Robert Clubb may publish in the future.

Co-authorship network of co-authors of Robert Clubb

This figure shows the co-authorship network connecting the top 25 collaborators of Robert Clubb. A scholar is included among the top collaborators of Robert Clubb 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 Robert Clubb. Robert Clubb 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.
Chen, Min, et al.. (2025). Structural basis of heme scavenging by the ChtA and HtaA hemophores in Corynebacterium diphtheriae. Journal of Biological Chemistry. 301(10). 110633–110633.
2.
Ha, Sung Min, et al.. (2024). A genomic analysis reveals the diversity of cellulosome displaying bacteria. Frontiers in Microbiology. 15. 1473396–1473396. 3 indexed citations
3.
Ellis‐Guardiola, Ken, et al.. (2024). Molecular basis of hemoglobin binding and heme removal in Corynebacterium diphtheriae. Proceedings of the National Academy of Sciences. 122(1). e2411833122–e2411833122. 2 indexed citations
4.
5.
Zhou, Anqi, et al.. (2022). The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins Structure Function and Bioinformatics. 90(7). 1457–1467. 5 indexed citations
6.
Cascio, Duilio, Martin L. Phillips, Musleh M. Muthana, et al.. (2021). Insight into the molecular basis of substrate recognition by the wall teichoic acid glycosyltransferase TagA. Journal of Biological Chemistry. 298(2). 101464–101464. 3 indexed citations
7.
Sjodt, Megan, Joseph Clayton, John S. Olson, et al.. (2018). Energetics underlying hemin extraction from human hemoglobin by Staphylococcus aureus. Journal of Biological Chemistry. 293(18). 6942–6957. 20 indexed citations
8.
Chan, Albert H., Andrew Duong, Danielle L. Sexton, et al.. (2016). Crystal Structure of the Streptomyces coelicolor Sortase E1 Transpeptidase Provides Insight into the Binding Mode of the Novel Class E Sorting Signal. PLoS ONE. 11(12). e0167763–e0167763. 20 indexed citations
9.
Amer, Brendan R., et al.. (2016). Rapid addition of unlabeled silent solubility tags to proteins using a new substrate-fused sortase reagent. Journal of Biomolecular NMR. 64(3). 197–205. 10 indexed citations
10.
Jeong, Sun‐Young, Megan Sjodt, Cary Retterer, et al.. (2015). Identification of agents effective against multiple toxins and viruses by host-oriented cell targeting. Scientific Reports. 5(1). 13476–13476. 30 indexed citations
11.
Malmirchegini, G. Reza, Megan Sjodt, M.R. Sawaya, et al.. (2014). Novel Mechanism of Hemin Capture by Hbp2, the Hemoglobin-binding Hemophore from Listeria monocytogenes. Journal of Biological Chemistry. 289(50). 34886–34899. 26 indexed citations
12.
Spirig, Thomas, G. Reza Malmirchegini, Jiang Zhang, et al.. (2012). Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme. Journal of Biological Chemistry. 288(2). 1065–1078. 47 indexed citations
13.
Spirig, Thomas, et al.. (2011). Sortase enzymes in Gram‐positive bacteria. Molecular Microbiology. 82(5). 1044–1059. 259 indexed citations
14.
Spirig, Thomas & Robert Clubb. (2011). Backbone 1H, 13C and 15N resonance assignments of the 39 kDa staphylococcal hemoglobin receptor IsdH. Biomolecular NMR Assignments. 6(2). 169–172. 8 indexed citations
15.
Wilkinson, Thomas A., Kurt Januszyk, Martin L. Phillips, et al.. (2009). Identifying and Characterizing a Functional HIV-1 Reverse Transcriptase-binding Site on Integrase. Journal of Biological Chemistry. 284(12). 7931–7939. 55 indexed citations
16.
Sam, My D., Duilio Cascio, Reid C. Johnson, & Robert Clubb. (2004). Crystal Structure of the Excisionase–DNA Complex from Bacteriophage Lambda. Journal of Molecular Biology. 338(2). 229–240. 47 indexed citations
17.
Connolly, Kevin M., Brenton T. Smith, Rosemarie Pilpa, et al.. (2003). Sortase from Staphylococcus aureus Does Not Contain a Thiolate-Imidazolium Ion Pair in Its Active Site. Journal of Biological Chemistry. 278(36). 34061–34065. 69 indexed citations
18.
Sam, My D., Kevin M. Connolly, Junji Iwahara, et al.. (2002). Regulation of Directionality in Bacteriophage λ Site-specific Recombination: Structure of the Xis Protein. Journal of Molecular Biology. 324(4). 791–805. 44 indexed citations
19.
Fejzo, Jasna, Felicia A. Etzkorn, Robert Clubb, et al.. (1994). The Mutant Escherichia coli F112W Cyclophilin Binds Cyclosporin A in Nearly Identical Conformation as Human Cyclophilin. Biochemistry. 33(19). 5711–5720. 26 indexed citations
20.
Clubb, Robert, V. Thanabal, Charles Osborne, & Gerhard Wagner. (1991). Proton and nitrogen-15 resonance assignments of oxidized flavodoxin from Anacystis nidulans with 3D NMR. Biochemistry. 30(31). 7718–7730. 30 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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