Amanda K. Chaplin

1.3k total citations
39 papers, 869 citations indexed

About

Amanda K. Chaplin is a scholar working on Molecular Biology, Materials Chemistry and Inorganic Chemistry. According to data from OpenAlex, Amanda K. Chaplin has authored 39 papers receiving a total of 869 indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 11 papers in Materials Chemistry and 9 papers in Inorganic Chemistry. Recurrent topics in Amanda K. Chaplin's work include DNA Repair Mechanisms (13 papers), Enzyme Structure and Function (9 papers) and Metal-Catalyzed Oxygenation Mechanisms (8 papers). Amanda K. Chaplin is often cited by papers focused on DNA Repair Mechanisms (13 papers), Enzyme Structure and Function (9 papers) and Metal-Catalyzed Oxygenation Mechanisms (8 papers). Amanda K. Chaplin collaborates with scholars based in United Kingdom, Netherlands and France. Amanda K. Chaplin's co-authors include Jonathan A. R. Worrall, Tom L. Blundell, Michael A. Hough, Erik Vijgenboom, Michael T. Wilson, Steven W. Hardwick, Dimitri Y. Chirgadze, Dimitri A. Svistunenko, Shikang Liang and Taianá Maia de Oliveira and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Amanda K. Chaplin

38 papers receiving 862 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Amanda K. Chaplin United Kingdom 18 580 164 154 111 109 39 869
Ezra Peisach United States 16 1.1k 1.8× 379 2.3× 144 0.9× 70 0.6× 42 0.4× 23 1.4k
Douglas A. Hansen United States 17 792 1.4× 83 0.5× 88 0.6× 66 0.6× 53 0.5× 21 1.2k
K.B. Handing United States 11 500 0.9× 199 1.2× 32 0.2× 76 0.7× 16 0.1× 11 729
Shabbir Ahmad United States 13 399 0.7× 118 0.7× 21 0.1× 136 1.2× 147 1.3× 20 665
E. Niedzialkowska United States 13 718 1.2× 93 0.6× 131 0.9× 64 0.6× 39 0.4× 20 830
Roberto A. Chica Canada 20 1.2k 2.1× 334 2.0× 62 0.4× 24 0.2× 30 0.3× 42 1.5k
José Trincão Portugal 16 641 1.1× 142 0.9× 45 0.3× 79 0.7× 158 1.4× 37 1.1k
Ruchi Anand India 20 969 1.7× 184 1.1× 93 0.6× 83 0.7× 43 0.4× 59 1.2k
W.R. Melik-Adamyan Russia 14 545 0.9× 229 1.4× 209 1.4× 116 1.0× 217 2.0× 18 852
Yasuhito Shomura Japan 19 1.1k 1.8× 400 2.4× 55 0.4× 36 0.3× 84 0.8× 39 1.5k

Countries citing papers authored by Amanda K. Chaplin

Since Specialization
Citations

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

Fields of papers citing papers by Amanda K. Chaplin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Amanda K. Chaplin. 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 Amanda K. Chaplin. The network helps show where Amanda K. Chaplin may publish in the future.

Co-authorship network of co-authors of Amanda K. Chaplin

This figure shows the co-authorship network connecting the top 25 collaborators of Amanda K. Chaplin. A scholar is included among the top collaborators of Amanda K. Chaplin 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 Amanda K. Chaplin. Amanda K. Chaplin 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.
Clarke, Thomas A., et al.. (2024). The oligomeric states of dye‐decolorizing peroxidases from Streptomyces lividans and their implications for mechanism of substrate oxidation. Protein Science. 33(7). e5073–e5073. 1 indexed citations
2.
Bueno-Alejo, Carlos J., Amanda K. Chaplin, Glenn A. Burley, et al.. (2022). Surface Passivation with a Perfluoroalkane Brush Improves the Precision of Single-Molecule Measurements. ACS Applied Materials & Interfaces. 14(44). 49604–49616. 11 indexed citations
3.
Hnı́zda, Aleš, Petr Těšina, Thanh Nguyen, et al.. (2021). SAP domain forms a flexible part of DNA aperture in Ku70/80. FEBS Journal. 288(14). 4382–4393. 11 indexed citations
4.
Blundell, Tom L. & Amanda K. Chaplin. (2021). The resolution revolution in X-ray diffraction, Cryo-EM and other Technologies. Progress in Biophysics and Molecular Biology. 160. 2–4. 15 indexed citations
5.
Munir, Asma, Michael T. Wilson, Steven W. Hardwick, et al.. (2021). Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis. Structure. 29(8). 899–912.e4. 16 indexed citations
6.
Chaplin, Amanda K., Steven W. Hardwick, Christopher J. Buehl, et al.. (2021). Cryo-EM of NHEJ supercomplexes provides insights into DNA repair. Molecular Cell. 81(16). 3400–3409.e3. 63 indexed citations
7.
Chaplin, Amanda K., Florian Dworkowski, Michael T. Wilson, et al.. (2020). A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases fromStreptomyces lividans. Dalton Transactions. 49(5). 1620–1636. 16 indexed citations
8.
Svistunenko, Dimitri A., Michael T. Wilson, Amanda K. Chaplin, et al.. (2020). Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in FeIV=O Formation. Angewandte Chemie International Edition. 59(48). 21656–21662. 29 indexed citations
9.
Svistunenko, Dimitri A., Michael T. Wilson, Amanda K. Chaplin, et al.. (2020). Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in FeIV=O Formation. Angewandte Chemie. 132(48). 21840–21846. 2 indexed citations
10.
Chaplin, Amanda K., Steven W. Hardwick, Shikang Liang, et al.. (2020). Dimers of DNA-PK create a stage for DNA double-strand break repair. Nature Structural & Molecular Biology. 28(1). 13–19. 75 indexed citations
11.
Ebrahim, Ali, Martin V. Appleby, Amanda K. Chaplin, et al.. (2019). Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins. IUCrJ. 6(4). 543–551. 60 indexed citations
12.
Ebrahim, Ali, Danny Axford, Martin V. Appleby, et al.. (2019). High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography. IUCrJ. 6(6). 1074–1085. 32 indexed citations
13.
Chaplin, Amanda K., et al.. (2019). An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry - A European Journal. 25(24). 6141–6153. 26 indexed citations
14.
Chaplin, Amanda K., Michael A. Hough, Jordi Paps, et al.. (2017). A cytosolic copper storage protein provides a second level of copper tolerance inStreptomyces lividans. Metallomics. 10(1). 180–193. 22 indexed citations
15.
Chaplin, Amanda K., Caterina Bernini, Adalgisa Sinicropi, et al.. (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie. 129(23). 6602–6606. 4 indexed citations
16.
Chaplin, Amanda K., Caterina Bernini, Adalgisa Sinicropi, et al.. (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie International Edition. 56(23). 6502–6506. 14 indexed citations
17.
Chaplin, Amanda K., Michael T. Wilson, & Jonathan A. R. Worrall. (2017). Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: new insight into the mechanism of anthraquinone dye decolourisation. Dalton Transactions. 46(29). 9420–9429. 25 indexed citations
18.
Vijgenboom, Erik, et al.. (2016). The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis inStreptomyces. Open Biology. 6(1). 150149–150149. 52 indexed citations
19.
Chaplin, Amanda K., Michael A. Hough, Dimitri A. Svistunenko, et al.. (2015). GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividans. Biochemical Journal. 469(3). 433–444. 52 indexed citations
20.
Chaplin, Amanda K., et al.. (2012). Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR). Journal of Biological Chemistry. 287(21). 17833–17847. 50 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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