Karen J. Edwards

906 total citations
20 papers, 775 citations indexed

About

Karen J. Edwards is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Karen J. Edwards has authored 20 papers receiving a total of 775 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 7 papers in Materials Chemistry and 5 papers in Oncology. Recurrent topics in Karen J. Edwards's work include Enzyme Structure and Function (7 papers), Metal complexes synthesis and properties (3 papers) and Plant and Fungal Species Descriptions (3 papers). Karen J. Edwards is often cited by papers focused on Enzyme Structure and Function (7 papers), Metal complexes synthesis and properties (3 papers) and Plant and Fungal Species Descriptions (3 papers). Karen J. Edwards collaborates with scholars based in Australia, United Kingdom and South Africa. Karen J. Edwards's co-authors include Stephen Neidle, Terence C. Jenkins, David L. Ollis, Paul A. Gadek, Nicholas E. Dixon, Stephen Neidle, Jane V. Skelly, David G. Brown, Jennifer M. Thorn and Mark W. Chase and has published in prestigious journals such as Journal of Molecular Biology, Biochemistry and FEBS Letters.

In The Last Decade

Karen J. Edwards

20 papers receiving 750 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Karen J. Edwards Australia 12 554 123 101 101 91 20 775
G. King Farrington United States 14 477 0.9× 103 0.8× 149 1.5× 98 1.0× 34 0.4× 19 845
Tatsuki Kashiwagi Japan 14 525 0.9× 31 0.3× 38 0.4× 137 1.4× 65 0.7× 40 915
Leslie E. Eisele United States 20 680 1.2× 83 0.7× 54 0.5× 33 0.3× 109 1.2× 37 1.1k
Der‐Ing Liao United States 13 722 1.3× 29 0.2× 83 0.8× 237 2.3× 47 0.5× 15 909
Akira Murakami Japan 13 486 0.9× 75 0.6× 96 1.0× 58 0.6× 41 0.5× 33 785
T. Lundqvist Sweden 18 856 1.5× 38 0.3× 70 0.7× 275 2.7× 63 0.7× 24 1.2k
Loubna A. Hammad United States 20 429 0.8× 51 0.4× 116 1.1× 53 0.5× 104 1.1× 26 818
Chi H. Trinh United Kingdom 21 719 1.3× 35 0.3× 98 1.0× 141 1.4× 48 0.5× 46 1.2k
Sergio E. Martinez United States 18 1.2k 2.2× 30 0.2× 100 1.0× 117 1.2× 77 0.8× 27 1.5k
J.P. Bacik United States 17 615 1.1× 28 0.2× 154 1.5× 98 1.0× 107 1.2× 28 906

Countries citing papers authored by Karen J. Edwards

Since Specialization
Citations

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

Fields of papers citing papers by Karen J. Edwards

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Karen J. Edwards

This figure shows the co-authorship network connecting the top 25 collaborators of Karen J. Edwards. A scholar is included among the top collaborators of Karen J. Edwards 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 Karen J. Edwards. Karen J. Edwards 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.
Harrington, Mark G., et al.. (2005). Phylogenetic Inference in Sapindaceae sensu lato Using Plastid <I>matK</I> and <I>rbcL</I> DNA Sequences. Systematic Botany. 30(2). 366–382. 104 indexed citations
2.
Gadek, Paul A., et al.. (2003). Divergence, diversity and species of the Australasian Callitris (Cupressaceae) and allied genera: evidence from ITS sequence data. Australian Systematic Botany. 16(4). 505–514. 24 indexed citations
3.
Edwards, Karen J. & Paul A. Gadek. (2001). Evolution and Biogeography of Alectryon (Sapindaceae). Molecular Phylogenetics and Evolution. 20(1). 14–26. 24 indexed citations
4.
Robinson, Anna, et al.. (2000). Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF). Acta Crystallographica Section D Biological Crystallography. 56(11). 1376–1384. 11 indexed citations
5.
Edwards, Karen J., David L. Ollis, & Nicholas E. Dixon. (1997). Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation. Journal of Molecular Biology. 271(2). 258–265. 31 indexed citations
6.
Edwards, Karen J., et al.. (1996). Structural and Sequence Comparisons of Quinone Oxidoreductase, ζ-Crystallin, and Glucose and Alcohol Dehydrogenases. Archives of Biochemistry and Biophysics. 328(1). 173–183. 64 indexed citations
7.
Cheah, Eong, et al.. (1996). The role of the T‐loop of the signal transducing protein PII from Escherichia coli. FEBS Letters. 391(1-2). 223–228. 40 indexed citations
8.
Carr, Paul D., et al.. (1996). Ice-free cryo-cooling of protein crystals. Journal of Applied Crystallography. 29(4). 469–470. 4 indexed citations
9.
Edwards, Karen J., et al.. (1996). New crystal forms ofEscherichia coliPIIcomplexed with various ligands and structure solution of PII/ATP/2-ketoglutarate. Acta Crystallographica Section A Foundations of Crystallography. 52(a1). C232–C233. 2 indexed citations
10.
Edwards, Karen J., et al.. (1996). Crystallization and Preliminary X-ray Diffraction Studies of New Crystal Forms ofEscherichia coliPIIComplexed with Various Ligands. Acta Crystallographica Section D Biological Crystallography. 52(4). 738–742. 2 indexed citations
12.
Thorn, Jennifer M., et al.. (1995). Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed with NADPH. Journal of Molecular Biology. 249(4). 785–799. 100 indexed citations
13.
Hardcastle, Ian R., Martin Rowlands, Iris B. Parr, et al.. (1995). Rationally Designed Analogs of Tamoxifen with Improved Calmodulin Antagonism. Journal of Medicinal Chemistry. 38(2). 241–248. 33 indexed citations
14.
Edwards, Karen J., et al.. (1994). Crystallization and Preliminary X-ray Diffraction Studies on a Soluble Escherichia coli Quinone Oxidoreductase. Journal of Molecular Biology. 240(5). 501–503. 8 indexed citations
15.
Edwards, Karen J., et al.. (1992). Molecular structure of the B-DNA dodecamer d(CGCAAATTTGCG)2 An examination of propeller twist and minor-groove water structure at 2·2Åresolution. Journal of Molecular Biology. 226(4). 1161–1173. 126 indexed citations
16.
Edwards, Karen J., Charles A. Laughton, & Stephen Neidle. (1992). A molecular-modeling study of the interactions between the antiestrogen drug tamoxifen and several derivatives, and the calcium-binding protein calmodulin. Journal of Medicinal Chemistry. 35(15). 2753–2761. 19 indexed citations
17.
Edwards, Karen J., Charles A. Laughton, & Stephen Neidle. (1992). A note on the conformational flexibility of the antiestrogenic drug tamoxifen: preferred conformations in the free state and bound to the protein calmodulin. Acta Crystallographica Section B Structural Science. 48(4). 511–514. 2 indexed citations
18.
Edwards, Karen J., Terence C. Jenkins, & Stephen Neidle. (1992). Crystal structure of a pentamidine-oligonucleotide complex: implications for DNA-binding properties. Biochemistry. 31(31). 7104–7109. 158 indexed citations
19.
Edwards, Karen J., et al.. (1991). Penta- and heptanuclear π-toluene derivatives of ruthenium. Journal of Organometallic Chemistry. 402(1). 113–123. 7 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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