Edith Sim

11.4k total citations
184 papers, 7.9k citations indexed

About

Edith Sim is a scholar working on Molecular Biology, Infectious Diseases and Immunology. According to data from OpenAlex, Edith Sim has authored 184 papers receiving a total of 7.9k indexed citations (citations by other indexed papers that have themselves been cited), including 114 papers in Molecular Biology, 27 papers in Infectious Diseases and 27 papers in Immunology. Recurrent topics in Edith Sim's work include Polyamine Metabolism and Applications (37 papers), Tuberculosis Research and Epidemiology (27 papers) and Complement system in diseases (23 papers). Edith Sim is often cited by papers focused on Polyamine Metabolism and Applications (37 papers), Tuberculosis Research and Epidemiology (27 papers) and Complement system in diseases (23 papers). Edith Sim collaborates with scholars based in United Kingdom, United States and France. Edith Sim's co-authors include Robert B. Sim, Isaac M. Westwood, Sotiria Boukouvala, M.E.M. Noble, Angela Risch, James Sandy, Adeel Mushtaq, Dean Hickman, Akane Kawamura and Elizabeth Fullam and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Lancet and Journal of the American Chemical Society.

In The Last Decade

Edith Sim

181 papers receiving 7.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edith Sim United Kingdom 50 4.5k 1.2k 995 972 916 184 7.9k
Gary H. Posner United States 60 5.0k 1.1× 342 0.3× 416 0.4× 762 0.8× 608 0.7× 363 15.4k
William Roush United States 66 6.6k 1.5× 881 0.7× 1.1k 1.1× 442 0.5× 340 0.4× 406 18.9k
Eliezer Huberman United States 55 5.9k 1.3× 2.5k 2.1× 779 0.8× 806 0.8× 362 0.4× 153 9.3k
TOMIO TAKEUCHI Japan 62 9.4k 2.1× 1.3k 1.1× 725 0.7× 463 0.5× 497 0.5× 621 16.6k
David T. Vistica United States 26 7.1k 1.6× 1.0k 0.8× 480 0.5× 833 0.9× 314 0.3× 56 14.2k
Yung‐Chi Cheng United States 54 5.5k 1.2× 455 0.4× 725 0.7× 711 0.7× 2.3k 2.5× 272 10.4k
Jai‐Sing Yang Taiwan 64 7.3k 1.6× 1.8k 1.5× 936 0.9× 1.2k 1.3× 188 0.2× 344 13.3k
Heidi R. Bokesch United States 25 5.4k 1.2× 754 0.6× 457 0.5× 607 0.6× 265 0.3× 61 10.9k
R. Stephen Lloyd United States 55 7.6k 1.7× 1.7k 1.4× 287 0.3× 555 0.6× 275 0.3× 283 9.9k
Liang Cao China 44 4.0k 0.9× 954 0.8× 748 0.8× 412 0.4× 454 0.5× 241 8.0k

Countries citing papers authored by Edith Sim

Since Specialization
Citations

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

Fields of papers citing papers by Edith Sim

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Edith Sim

This figure shows the co-authorship network connecting the top 25 collaborators of Edith Sim. A scholar is included among the top collaborators of Edith Sim 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 Edith Sim. Edith Sim 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.
Sim, Edith, et al.. (2024). Self‐Assembled BODIPY@Au Core‐Shell Structures for Durable Neuroprotective Phototherapy. ChemBioChem. 26(3). e202400562–e202400562.
2.
Thinnes, Cyrille C., Peter Seden, Nicola Laurieri, et al.. (2014). Structure–activity relationships and colorimetric properties of specific probes for the putative cancer biomarker human arylamine N-acetyltransferase 1. Bioorganic & Medicinal Chemistry. 22(11). 3030–3054. 24 indexed citations
3.
Laurieri, Nicola, Akane Kawamura, Isaac M. Westwood, et al.. (2014). Differences between murine arylamine N-acetyltransferase type 1 and human arylamine N-acetyltransferase type 2 defined by substrate specificity and inhibitor binding. BMC Pharmacology and Toxicology. 15(1). 68–68. 10 indexed citations
4.
Abuhammad, Areej, E.D. Lowe, M.A. McDonough, Edith Sim, & Elspeth F. Garman. (2013). Structure of arylamineN-acetyltransferase fromM. tuberculosis: triumph over adversity. Acta Crystallographica Section A Foundations of Crystallography. 69(a1). s83–s83. 2 indexed citations
5.
Fullam, Elizabeth, James Talbot, Isaac M. Westwood, et al.. (2013). Design, synthesis and structure–activity relationships of 3,5-diaryl-1H-pyrazoles as inhibitors of arylamine N-acetyltransferase. Bioorganic & Medicinal Chemistry Letters. 23(9). 2759–2764. 21 indexed citations
6.
Laurieri, Nicola, Cyrille C. Thinnes, Camilo Quevedo, et al.. (2013). A Novel Color Change Mechanism for Breast Cancer Biomarker Detection: Naphthoquinones as Specific Ligands of Human Arylamine N-Acetyltransferase 1. PLoS ONE. 8(8). e70600–e70600. 14 indexed citations
7.
Fullam, Elizabeth, et al.. (2009). Comparison of the Arylamine N-Acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis. The Protein Journal. 28(6). 281–293. 20 indexed citations
8.
Carroll, Maria V., Nathan A. Lack, Edith Sim, Anders Krarup, & Robert B. Sim. (2009). Multiple routes of complement activation by Mycobacterium bovis BCG. Molecular Immunology. 46(16). 3367–3378. 67 indexed citations
9.
Kawamura, Akane, Isaac M. Westwood, Larissa Wakefield, et al.. (2008). Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1. Biochemical Pharmacology. 75(7). 1550–1560. 37 indexed citations
10.
Sim, Edith. (2007). Arylamine N-acetyltransferases 3. ˜The œbiomedical & life sciences collection.. 2007(10). e1004279–e1004279.
11.
Wakefield, Larissa, et al.. (2006). N-Acetyltransferase (Nat) 1 and 2 Expression in Nat2 Knockout Mice. Journal of Pharmacology and Experimental Therapeutics. 319(2). 724–728. 20 indexed citations
12.
Dairou, Julien, Delphine Flatters, Alain Chaffotte, et al.. (2006). Insight into the structure of Mesorhizobium loti arylamine N‐acetyltransferase 2 (MLNAT2): A biochemical and computational study. FEBS Letters. 580(7). 1780–1788. 11 indexed citations
13.
Davies, Stephen G., et al.. (2003). An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases. Bioorganic & Medicinal Chemistry. 11(7). 1227–1234. 73 indexed citations
14.
Pompeo, Frédérique, Adeel Mushtaq, & Edith Sim. (2002). Expression and Purification of the Rifamycin Amide Synthase, RifF, an Enzyme Homologous to the Prokaryotic Arylamine N-Acetyltransferases. Protein Expression and Purification. 24(1). 138–151. 23 indexed citations
15.
Vineis, Paolo, Herman Autrup, Jürgen Brockmöller, et al.. (2001). Current Smoking, Occupation, N-Acetyltransferase-2 and Bladder Cancer. Cancer Epidemiology and Prevention Biomarkers. 10(12). 1249–1252. 1 indexed citations
16.
17.
Hickman, Dean, Jairam Palamanda, Jashvant D. Unadkat, & Edith Sim. (1995). Enzyme kinetic properties of human recombinant arylamine n-acetyltransferase 2 allotypic variants expressed in Escherichia coli. Biochemical Pharmacology. 50(5). 697–703. 48 indexed citations
18.
Vatsis, Kostas P., Wendell W. Weber, Douglas A. Bell, et al.. (1995). Nomenclature for N-acetyltransferases. Pharmacogenetics. 5(1). 1–17. 318 indexed citations
19.
Sim, Edith, et al.. (1991). Expression of N-Acetyl Transferase in a Human Monocytic Cell-Line, U937. Human & Experimental Toxicology. 10(1). 33–38. 10 indexed citations
20.
Sim, Edith, et al.. (1990). Arylamine N-acetyltransferase from fast (C57BL6) and slow (A/J) N-Acetylating strains of mice. Biochemical Pharmacology. 39(4). 647–654. 8 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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