D.K. Stammers

783 total citations
14 papers, 652 citations indexed

About

D.K. Stammers is a scholar working on Molecular Biology, Infectious Diseases and Epidemiology. According to data from OpenAlex, D.K. Stammers has authored 14 papers receiving a total of 652 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Biology, 5 papers in Infectious Diseases and 3 papers in Epidemiology. Recurrent topics in D.K. Stammers's work include HIV/AIDS drug development and treatment (5 papers), Pneumocystis jirovecii pneumonia detection and treatment (3 papers) and Biochemical and Molecular Research (3 papers). D.K. Stammers is often cited by papers focused on HIV/AIDS drug development and treatment (5 papers), Pneumocystis jirovecii pneumonia detection and treatment (3 papers) and Biochemical and Molecular Research (3 papers). D.K. Stammers collaborates with scholars based in United Kingdom and United States. D.K. Stammers's co-authors include C.R. Beddell, J.N. Champness, J.T. Bolin, David A. Matthews, David J. Filman, Bernard T. Kaufman, J. Kraut, Jane M. Burridge, Karl Volz and John G. Dann and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemical Journal.

In The Last Decade

D.K. Stammers

14 papers receiving 624 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
D.K. Stammers United Kingdom 13 443 157 143 96 87 14 652
H. M. Krishna Murthy United States 14 403 0.9× 135 0.9× 138 1.0× 48 0.5× 89 1.0× 23 892
Tavner J. Delcamp United States 17 611 1.4× 185 1.2× 91 0.6× 63 0.7× 126 1.4× 29 814
Amy L. Swain United States 8 550 1.2× 131 0.8× 167 1.2× 28 0.3× 114 1.3× 12 789
John G. Dann United Kingdom 11 387 0.9× 150 1.0× 85 0.6× 42 0.4× 82 0.9× 12 523
Sandra K. Freeman United States 14 344 0.8× 101 0.6× 153 1.1× 193 2.0× 151 1.7× 25 666
Kathy M. Perry United States 8 745 1.7× 382 2.4× 103 0.7× 51 0.5× 105 1.2× 10 848
Robert M. Stroud United States 11 785 1.8× 245 1.6× 70 0.5× 40 0.4× 45 0.5× 19 857
B.K. Biswal India 16 332 0.7× 118 0.8× 223 1.6× 147 1.5× 38 0.4× 36 723
Myra N. Williams United States 11 473 1.1× 149 0.9× 66 0.5× 23 0.2× 52 0.6× 13 606
Genbin Shi United States 16 594 1.3× 51 0.3× 145 1.0× 212 2.2× 165 1.9× 30 708

Countries citing papers authored by D.K. Stammers

Since Specialization
Citations

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

Fields of papers citing papers by D.K. Stammers

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of D.K. Stammers

This figure shows the co-authorship network connecting the top 25 collaborators of D.K. Stammers. A scholar is included among the top collaborators of D.K. Stammers 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 D.K. Stammers. D.K. Stammers is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

14 of 14 papers shown
1.
Nichols, C.E., Heather K. Lamb, Peter M. Thompson, et al.. (2013). Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD–YeaZ–YjeE complex. Protein Science. 22(5). 628–640. 30 indexed citations
2.
Nichols, C.E., et al.. (2006). Structural characterization of Salmonella typhimurium YeaZ, an M22 O‐sialoglycoprotein endopeptidase homolog. Proteins Structure Function and Bioinformatics. 64(1). 111–123. 36 indexed citations
3.
Nichols, C.E., Jingshan Ren, Kris Leslie, et al.. (2004). Comparison of Ligand-induced Conformational Changes and Domain Closure Mechanisms, Between Prokaryotic and Eukaryotic Dehydroquinate Synthases. Journal of Molecular Biology. 343(3). 533–546. 18 indexed citations
4.
Achari, A., et al.. (1994). The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 å resolution. Structure. 2(10). 915–924. 82 indexed citations
5.
Stammers, D.K., C. J. Delves, S. Ballantine, et al.. (1993). Preliminary Crystallographic Data for Pneumocystis carinii Dihydrofolate Reductase. Journal of Molecular Biology. 230(2). 679–680. 4 indexed citations
6.
Delves, C. J., S. Ballantine, Robert L. Tansik, David P. Baccanari, & D.K. Stammers. (1993). Refolding of Recombinant Pneumocystis carinii Dihydrofolate Reductase and Characterization of the Enzyme. Protein Expression and Purification. 4(1). 16–23. 17 indexed citations
7.
Stammers, D.K., John G. Dann, C.J. Harris, & Dana R. Smith. (1987). Comparison of angiotensinogen and tetradecapeptide as substrates for human renin. Archives of Biochemistry and Biophysics. 258(2). 413–420. 17 indexed citations
8.
Stammers, D.K., J.N. Champness, C.R. Beddell, et al.. (1987). The structure of mouse L1210 dihydrofolate reductase‐drug complexes and the construction of a model of human enzyme. FEBS Letters. 218(1). 178–184. 78 indexed citations
9.
Dann, John G., et al.. (1986). Human renin: A new class of inhibitors. Biochemical and Biophysical Research Communications. 134(1). 71–77. 27 indexed citations
10.
Stammers, D.K., et al.. (1986). Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin. Biochemical Journal. 239(2). 387–392. 17 indexed citations
11.
Matthews, David A., J.T. Bolin, Jane M. Burridge, et al.. (1985). Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim.. Journal of Biological Chemistry. 260(1). 381–391. 240 indexed citations
12.
13.
Beddell, C.R., P. J. Goodford, D.K. Stammers, & R Wootton. (1979). SPECIES DIFFERENCES IN THE BINDING OF COMPOUNDS DESIGNED TO FIT A SITE OF KNOWN STRUCTURE IN ADULT HUMAN HAEMOGLOBIN. British Journal of Pharmacology. 65(3). 535–543. 15 indexed citations
14.
Duée, E., et al.. (1972). X-Ray Diffraction Studies on Enzymes in the Glycolytic Pathway. Cold Spring Harbor Symposia on Quantitative Biology. 36(0). 165–170. 55 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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