Gerard W. Canters

10.4k total citations
264 papers, 8.8k citations indexed

About

Gerard W. Canters is a scholar working on Molecular Biology, Materials Chemistry and Electrical and Electronic Engineering. According to data from OpenAlex, Gerard W. Canters has authored 264 papers receiving a total of 8.8k indexed citations (citations by other indexed papers that have themselves been cited), including 175 papers in Molecular Biology, 87 papers in Materials Chemistry and 48 papers in Electrical and Electronic Engineering. Recurrent topics in Gerard W. Canters's work include Photosynthetic Processes and Mechanisms (86 papers), Enzyme Structure and Function (49 papers) and Porphyrin Metabolism and Disorders (45 papers). Gerard W. Canters is often cited by papers focused on Photosynthetic Processes and Mechanisms (86 papers), Enzyme Structure and Function (49 papers) and Porphyrin Metabolism and Disorders (45 papers). Gerard W. Canters collaborates with scholars based in Netherlands, Italy and United Kingdom. Gerard W. Canters's co-authors include Marcellus Ubbink, Mart van de Kamp, Erik Vijgenboom, Albrecht Messerschmidt, Herbert Nar, Martin Ph. Verbeet, Robert Huber, Christopher Dennison, Thijs J. Aartsma and Gianfranco Gilardi and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Advanced Materials.

In The Last Decade

Gerard W. Canters

262 papers receiving 8.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gerard W. Canters Netherlands 52 5.0k 2.3k 1.8k 1.6k 1.2k 264 8.8k
George McLendon United States 47 3.4k 0.7× 2.9k 1.3× 1.9k 1.0× 686 0.4× 790 0.6× 179 7.7k
Gordon Tollin United States 57 8.3k 1.7× 1.5k 0.6× 1.9k 1.0× 1.3k 0.8× 1.1k 0.9× 375 12.3k
Peter Hildebrandt Germany 63 7.1k 1.4× 2.7k 1.2× 3.1k 1.7× 1.7k 1.0× 2.5k 2.1× 412 15.3k
Bo G. Malmström Sweden 56 5.4k 1.1× 1.1k 0.5× 1.3k 0.7× 1.5k 0.9× 1.2k 0.9× 173 8.9k
Christopher C. Moser United States 41 5.8k 1.2× 1.8k 0.8× 1.8k 1.0× 1.2k 0.7× 786 0.6× 95 9.2k
Harry B. Gray United States 41 1.7k 0.3× 1.6k 0.7× 1.8k 1.0× 935 0.6× 849 0.7× 81 5.7k
A. Grant Mauk Canada 56 6.4k 1.3× 1.4k 0.6× 1.1k 0.6× 864 0.5× 763 0.6× 209 9.2k
John A. Shelnutt United States 56 3.8k 0.8× 7.5k 3.3× 1.4k 0.8× 1.7k 1.1× 361 0.3× 177 10.7k
Ǵerald Babcock United States 69 13.0k 2.6× 2.3k 1.0× 1.1k 0.6× 3.7k 2.3× 1.1k 0.9× 239 17.3k
Albrecht Messerschmidt Germany 41 3.6k 0.7× 1.7k 0.7× 574 0.3× 1.8k 1.1× 394 0.3× 100 7.1k

Countries citing papers authored by Gerard W. Canters

Since Specialization
Citations

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

Fields of papers citing papers by Gerard W. Canters

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gerard W. Canters. 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 Gerard W. Canters. The network helps show where Gerard W. Canters may publish in the future.

Co-authorship network of co-authors of Gerard W. Canters

This figure shows the co-authorship network connecting the top 25 collaborators of Gerard W. Canters. A scholar is included among the top collaborators of Gerard W. Canters 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 Gerard W. Canters. Gerard W. Canters 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.
Jeuken, Lars J. C., Michel Orrit, & Gerard W. Canters. (2022). Single-molecule fluorescence in redox chemistry. Current Opinion in Electrochemistry. 37. 101196–101196. 8 indexed citations
2.
Goldsmith, Randall H., Leandro C. Tabares, Christopher Dennison, et al.. (2011). Redox cycling and kinetic analysis of single molecules of solution-phase nitrite reductase. Proceedings of the National Academy of Sciences. 108(42). 17269–17274. 46 indexed citations
3.
Tepper, Armand W.J.W., Thijs J. Aartsma, & Gerard W. Canters. (2010). Channeling of electrons within SLAC, the small laccase from Streptomyces coelicolor. Faraday Discussions. 148. 161–171. 10 indexed citations
4.
Wijma, Hein J., Lars J. C. Jeuken, Martin Ph. Verbeet, Fräser A. Armstrong, & Gerard W. Canters. (2007). Protein Film Voltammetry of Copper-Containing Nitrite Reductase Reveals Reversible Inactivation. Journal of the American Chemical Society. 129(27). 8557–8565. 41 indexed citations
5.
Cioni, Patrizia, Ellen de Waal, Gerard W. Canters, & Giovanni B. Strambini. (2004). Effects of Cavity-Forming Mutations on the Internal Dynamics of Azurin. Biophysical Journal. 86(2). 1149–1159. 18 indexed citations
6.
Wijma, Hein J., Gerard W. Canters, Simon de Vries, & Martin Ph. Verbeet. (2004). Bidirectional Catalysis by Copper-Containing Nitrite Reductase. Biochemistry. 43(32). 10467–10474. 56 indexed citations
7.
Ubbink, Marcellus, et al.. (2003). Messung eines Cu‐Cu‐Abstands von 26 Å mit einer gepulsten EPR‐Methode. Angewandte Chemie. 115(1). 64–67. 13 indexed citations
8.
Vanwetswinkel, Sophie, G.R. Andersen, Peter Güntert, et al.. (2003). Solution Structure of the 162 Residue C-terminal Domain of Human Elongation Factor 1Bγ. Journal of Biological Chemistry. 278(44). 43443–43451. 13 indexed citations
9.
Battaini, Giuseppe, Enrico Monzani, Luigi Casella, et al.. (2002). Tyrosinase-catalyzed Oxidation of Fluorophenols. Journal of Biological Chemistry. 277(47). 44606–44612. 67 indexed citations
10.
Berendsen, H. J. C., et al.. (2001). Density functional theory and molecular dynamics results for copper proteins. Journal of Inorganic Biochemistry. 86(1). 445–445. 5 indexed citations
11.
Gastel, Maurice van, Martin J. Boulanger, Gerard W. Canters, et al.. (2001). A Single-Crystal Electron Paramagnetic Resonance Study at 95 GHz of the Type 1 Copper Site of the Green Nitrite Reductase of Alcaligenes faecalis. The Journal of Physical Chemistry B. 105(11). 2236–2243. 14 indexed citations
12.
Gastel, Maurice van, Luigi Bubacco, E. J. J. Groenen, Erik Vijgenboom, & Gerard W. Canters. (2000). EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus. FEBS Letters. 474(2-3). 228–232. 37 indexed citations
13.
Canters, Gerard W., et al.. (1998). Time-Resolved Fluorescence Study of Azurin Variants: Conformational Heterogeneity and Tryptophan Mobility. Biophysical Journal. 75(5). 2441–2450. 37 indexed citations
14.
Meskers, Stefan C. J., Marcellus Ubbink, Gerard W. Canters, & Harry P. J. M. Dekkers. (1998). pH dependence of the enantioselective excited-state quenching of Λ,Δ-Tb(III) and Λ,Δ-Eu(III)tris(pyridine-2,6-dicarboxylate) chelates by ferricytochrome c from horse heart and ferricytochrome c-550 from Paracoccus versutus. JBIC Journal of Biological Inorganic Chemistry. 3(5). 463–469. 9 indexed citations
15.
Hammann, Christian, Gertie van Pouderoyen, Herbert Nar, et al.. (1997). Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin a aEdited by I. A. Wilson. Journal of Molecular Biology. 266(2). 357–365. 19 indexed citations
16.
Ubbink, Marcellus, Mark Pfuhl, John van der Oost, Axel Berg, & Gerard W. Canters. (1996). NMR assignments and relaxation studies of Thiobacillus versutus ferrocytochrome c‐550 indicate the presence of a highly mobile 13‐residues long C‐terminal tail. Protein Science. 5(12). 2494–2505. 13 indexed citations
17.
Vijgenboom, Erik, et al.. (1995). Physiological role and expression of the blue copper protein azurin in Pseudomonas aeruginosa. Journal of Inorganic Biochemistry. 59(2-3). 720–720. 2 indexed citations
18.
Romero, Antonio, Herbert Nar, Robert Huber, et al.. (1994). Crystal structure analysis and refinement at 2·15Å resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus. Journal of Molecular Biology. 236(4). 1196–1211. 59 indexed citations
19.
20.
Canters, Gerard W., et al.. (1984). A proton NMR study of the electron exchange between reduced and oxidized azurin from Pseudomonas aeruginosa. Journal of Magnetic Resonance (1969). 57(1). 1–23. 22 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by George McLendon Breakdown of academic impact, for papers by Gordon Tollin Breakdown of academic impact, for papers by Peter Hildebrandt Breakdown of academic impact, for papers by Bo G. Malmström Breakdown of academic impact, for papers by Christopher C. Moser Breakdown of academic impact, for papers by Harry B. Gray Breakdown of academic impact, for papers by A. Grant Mauk Breakdown of academic impact, for papers by John A. Shelnutt Breakdown of academic impact, for papers by Ǵerald Babcock Breakdown of academic impact, for papers by Albrecht Messerschmidt
Rankless by CCL
2026