Arthur J. Rowe

2.5k total citations
77 papers, 2.0k citations indexed

About

Arthur J. Rowe is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Arthur J. Rowe has authored 77 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 15 papers in Materials Chemistry and 11 papers in Organic Chemistry. Recurrent topics in Arthur J. Rowe's work include Protein purification and stability (14 papers), Glycosylation and Glycoproteins Research (11 papers) and Protein Structure and Dynamics (11 papers). Arthur J. Rowe is often cited by papers focused on Protein purification and stability (14 papers), Glycosylation and Glycoproteins Research (11 papers) and Protein Structure and Dynamics (11 papers). Arthur J. Rowe collaborates with scholars based in United Kingdom, United States and Türkiye. Arthur J. Rowe's co-authors include Stephen E. Harding, Gary G. Adams, J. H. M. Willison, Peter W. Andrew, Richard B. Gillis, Timothy J. Mitchell, Peter J. Morgan, Robert J.C. Gilbert, Olwyn Byron and Anthony Persechini and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Arthur J. Rowe

77 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Arthur J. Rowe United Kingdom 27 1.1k 271 213 187 175 77 2.0k
Roman I. Koning Netherlands 35 2.3k 2.0× 284 1.0× 300 1.4× 130 0.7× 105 0.6× 87 4.3k
Christine Péchoux France 35 1.7k 1.5× 393 1.5× 664 3.1× 196 1.0× 248 1.4× 77 3.7k
William R. Trumble United States 18 1.1k 1.0× 208 0.8× 79 0.4× 157 0.8× 113 0.6× 40 1.8k
Benjamin S. Schuster United States 23 1.4k 1.2× 180 0.7× 344 1.6× 140 0.7× 49 0.3× 49 2.5k
Olwyn Byron United Kingdom 29 1.5k 1.4× 279 1.0× 94 0.4× 72 0.4× 80 0.5× 78 2.5k
Trushar R. Patel Canada 29 1.7k 1.5× 440 1.6× 370 1.7× 73 0.4× 276 1.6× 108 3.5k
Manfred Roessle Germany 25 1.9k 1.8× 619 2.3× 152 0.7× 160 0.9× 74 0.4× 55 3.0k
Zhao Wang China 29 1.7k 1.5× 183 0.7× 179 0.8× 63 0.3× 83 0.5× 110 3.0k
Penelope E. Stein United Kingdom 27 2.2k 2.0× 273 1.0× 69 0.3× 138 0.7× 236 1.3× 48 4.5k
Jan T. Rasmussen Denmark 34 2.0k 1.9× 941 3.5× 128 0.6× 76 0.4× 321 1.8× 79 5.1k

Countries citing papers authored by Arthur J. Rowe

Since Specialization
Citations

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

Fields of papers citing papers by Arthur J. Rowe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Arthur J. Rowe

This figure shows the co-authorship network connecting the top 25 collaborators of Arthur J. Rowe. A scholar is included among the top collaborators of Arthur J. Rowe 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 Arthur J. Rowe. Arthur J. Rowe 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.
Almutairi, Fahad M., Gary G. Adams, María Hayes, et al.. (2014). Hydrodynamic characterisation of chitosan and its interaction with two polyanions: DNA and xanthan. Carbohydrate Polymers. 122. 359–366. 15 indexed citations
2.
Adams, Gary G., et al.. (2014). Protein–like fully reversible tetramerisation and super-association of an aminocellulose. Scientific Reports. 4(1). 3861–3861. 19 indexed citations
3.
Gillis, Richard B., et al.. (2013). MultiSig: a new high-precision approach to the analysis of complex biomolecular systems. European Biophysics Journal. 42(10). 777–786. 26 indexed citations
4.
Schuck, Peter, Richard B. Gillis, Tabot M. D. Besong, et al.. (2013). SEDFIT–MSTAR: molecular weight and molecular weight distribution analysis of polymers by sedimentation equilibrium in the ultracentrifuge. The Analyst. 139(1). 79–92. 73 indexed citations
5.
Tetteh‐Quarcoo, Patience B., Christoph Q. Schmidt, Wai‐Hong Tham, et al.. (2012). Lack of Evidence from Studies of Soluble Protein Fragments that Knops Blood Group Polymorphisms in Complement Receptor-Type 1 Are Driven by Malaria. PLoS ONE. 7(4). e34820–e34820. 18 indexed citations
6.
Ross, Jacob A., Ermanno Gherardi, Arthur J. Rowe, et al.. (2011). Protein Engineered Variants of Hepatocyte Growth Factor/Scatter Factor Promote Proliferation of Primary Human Hepatocytes and in Rodent Liver. Gastroenterology. 142(4). 897–906. 23 indexed citations
7.
Heinze, Thomas, Tabot M. D. Besong, Peter Berlin, et al.. (2011). Protein‐like Oligomerization of Carbohydrates. Angewandte Chemie International Edition. 50(37). 8602–8604. 31 indexed citations
8.
Rowe, Arthur J., et al.. (2010). Evaluation of the Information Content of Sedimentation Equilibrium Data in Self‐Interacting Systems. Macromolecular Bioscience. 10(7). 798–807. 17 indexed citations
9.
Lü, Yanling, Stephen E. Harding, Alison Turner, et al.. (2007). Effect of PEGylation on the Solution Conformation of Antibody Fragments. Journal of Pharmaceutical Sciences. 97(6). 2062–2079. 48 indexed citations
10.
Errington, Neil & Arthur J. Rowe. (2003). Probing conformation and conformational change in proteins is optimally undertaken in relative mode. European Biophysics Journal. 32(5). 511–517. 16 indexed citations
11.
Rowe, Arthur J., et al.. (2000). Kinetic and hydrodynamic studies of the NodL O-acetyl transferase of Rhizobium leguminosarum: a random-order ternary complex mechanism for acetyl transfer by a roughly spherical trimeric protein. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1479(1-2). 203–213. 7 indexed citations
12.
Errington, Neil, Olwyn Byron, & Arthur J. Rowe. (1999). Conformational spectra — probing protein conformational changes. Biophysical Chemistry. 80(3). 189–197. 4 indexed citations
13.
Gilbert, Robert J.C., Richard K. Heenan, Peter A. Timmins, et al.. (1999). Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering 1 1Edited by M. F. Moody. Journal of Molecular Biology. 293(5). 1145–1160. 38 indexed citations
14.
Rossjohn, Jamie, Robert J.C. Gilbert, Dennis Crane, et al.. (1998). The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae 1 1Edited by J. Thornton. Journal of Molecular Biology. 284(2). 449–461. 88 indexed citations
15.
Gilbert, Robert J.C., Jamie Rossjohn, Michael W. Parker, et al.. (1998). Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae. Journal of Molecular Biology. 284(4). 1223–1237. 64 indexed citations
16.
Morgan, Peter J., Primrose Freestone, Dennis Crane, et al.. (1997). Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin. FEBS Letters. 412(3). 563–567. 5 indexed citations
17.
Rowe, Arthur J., et al.. (1997). Physical characterization and ATPase activity of 14S dynein fractions from Tetrahymena thermophila. Journal of Muscle Research and Cell Motility. 18(6). 697–709. 3 indexed citations
18.
Davis, Simon J., et al.. (1997). Characterisation of the low affinity interaction between rat cell adhesion molecules CD2 and CD48 by analytical ultracentrifugation. European Biophysics Journal. 25(5-6). 455–462. 22 indexed citations
19.
Rowe, Arthur J., et al.. (1991). A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity. Journal of Molecular Biology. 217(2). 323–335. 39 indexed citations
20.
Wells, Christine A., Antonio D. Molina García, Stephen E. Harding, & Arthur J. Rowe. (1990). Self-interaction of dynein fromTetrahymena cilia. Journal of Muscle Research and Cell Motility. 11(4). 344–350. 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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