D.K. Stammers

8.8k total citations · 1 hit paper
108 papers, 6.8k citations indexed

About

D.K. Stammers is a scholar working on Molecular Biology, Infectious Diseases and Virology. According to data from OpenAlex, D.K. Stammers has authored 108 papers receiving a total of 6.8k indexed citations (citations by other indexed papers that have themselves been cited), including 72 papers in Molecular Biology, 53 papers in Infectious Diseases and 39 papers in Virology. Recurrent topics in D.K. Stammers's work include HIV/AIDS drug development and treatment (47 papers), HIV Research and Treatment (38 papers) and Biochemical and Molecular Research (34 papers). D.K. Stammers is often cited by papers focused on HIV/AIDS drug development and treatment (47 papers), HIV Research and Treatment (38 papers) and Biochemical and Molecular Research (34 papers). D.K. Stammers collaborates with scholars based in United Kingdom, United States and Belgium. D.K. Stammers's co-authors include Jingshan Ren, David I. Stuart, Robert Esnouf, Carl Ross, E. Yvonne Jones, Hilary Muirhead, Andrew L. Hopkins, Michael Levine, Louise E. Bird and D.O. Somers and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

D.K. Stammers

108 papers receiving 6.6k citations

Hit Papers

Crystal structure of cat muscle pyruvate kinase at a reso... 1979 2026 1994 2010 1979 100 200 300
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
    1979 389 citations David I. Stuart, D.K. Stammers et al. Journal of Molecular Biology profile →

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 46 3.5k 3.3k 2.6k 1.1k 940 108 6.8k
Jingshan Ren United Kingdom 49 3.4k 1.0× 3.6k 1.1× 2.3k 0.9× 821 0.8× 1.1k 1.1× 122 7.4k
Karen S. Anderson United States 52 5.2k 1.5× 3.6k 1.1× 2.7k 1.0× 1.2k 1.1× 1.3k 1.4× 241 9.7k
Robert Esnouf United Kingdom 34 3.8k 1.1× 2.0k 0.6× 1.6k 0.6× 717 0.7× 636 0.7× 76 6.7k
Ben M. Dunn United States 44 3.4k 1.0× 1.7k 0.5× 1.4k 0.5× 622 0.6× 369 0.4× 214 6.1k
Kalyan Das United States 53 3.8k 1.1× 4.8k 1.4× 3.8k 1.5× 1.2k 1.1× 2.3k 2.4× 151 8.5k
Giovanni Maga Italy 51 5.5k 1.6× 2.2k 0.7× 1.3k 0.5× 2.4k 2.3× 878 0.9× 270 9.9k
Michael A. Parniak Canada 52 3.2k 0.9× 5.1k 1.5× 4.8k 1.8× 567 0.5× 1.2k 1.3× 183 7.8k
Jan Balzarini Belgium 46 3.8k 1.1× 2.2k 0.6× 1.2k 0.5× 2.7k 2.5× 1.4k 1.5× 213 7.6k
William G. Rice United States 39 3.1k 0.9× 1.2k 0.4× 1.1k 0.4× 972 0.9× 398 0.4× 108 5.4k
Carole A. Bewley United States 46 3.4k 1.0× 973 0.3× 1.4k 0.5× 1.7k 1.6× 396 0.4× 144 6.3k

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

20 of 20 papers shown
1.
Ren, Jingshan & D.K. Stammers. (2008). Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase. Virus Research. 134(1-2). 157–170. 116 indexed citations
2.
Lamb, Heather K., D.K. Stammers, & Alastair R. Hawkins. (2008). Dinucleotide-Sensing Proteins: Linking Signaling Networks and Regulating Transcription. Science Signaling. 1(33). pe38–pe38. 13 indexed citations
3.
Ren, Jingshan, Philip P. Chamberlain, Anna Stamp, et al.. (2008). Structural Basis for the Improved Drug Resistance Profile of New Generation Benzophenone Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors. Journal of Medicinal Chemistry. 51(16). 5000–5008. 64 indexed citations
4.
Cader, M. Zameel, Jingshan Ren, Paul A. James, et al.. (2007). Crystal structure of human wildtype and S581L‐mutant glycyl‐tRNA synthetase, an enzyme underlying distal spinal muscular atrophy. FEBS Letters. 581(16). 2959–2964. 30 indexed citations
5.
Ren, Jingshan, Charles E. Nichols, Philip P. Chamberlain, et al.. (2007). Relationship of Potency and Resilience to Drug Resistant Mutations for GW420867X Revealed by Crystal Structures of Inhibitor Complexes for Wild-Type, Leu100Ile, Lys101Glu, and Tyr188Cys Mutant HIV-1 Reverse Transcriptases. Journal of Medicinal Chemistry. 50(10). 2301–2309. 55 indexed citations
6.
Omari, Kamel El, B. Dhaliwal, M. Lockyer, et al.. (2006). Structure ofStaphylococcus aureusguanylate monophosphate kinase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(10). 949–953. 11 indexed citations
7.
Omari, Kamel El, Nicola Solaroli, Anna Karlsson, Jan Balzarini, & D.K. Stammers. (2006). Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design. BMC Structural Biology. 6(1). 22–22. 28 indexed citations
8.
Omari, Kamel El, Annelies Bronckaers, Sandra Liekens, et al.. (2006). Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implications for drug design. Biochemical Journal. 399(2). 199–204. 36 indexed citations
9.
Nettleship, Joanne E., Thomas S. Walter, Robin T. Aplin, D.K. Stammers, & Raymond J. Owens. (2005). Sample preparation and mass-spectrometric characterization of crystal-derived protein samples. Acta Crystallographica Section D Biological Crystallography. 61(5). 643–645. 3 indexed citations
10.
Nichols, C.E., A R Hawkins, & D.K. Stammers. (2004). Structure of the `open' form ofAspergillus nidulans3-dehydroquinate synthase at 1.7 Å resolution from crystals grown following enzyme turnover. Acta Crystallographica Section D Biological Crystallography. 60(5). 971–973. 8 indexed citations
11.
Lamb, Heather K., Kris Leslie, Margaret Nutley, et al.. (2003). The Negative Transcriptional Regulator NmrA Discriminates between Oxidized and Reduced Dinucleotides. Journal of Biological Chemistry. 278(34). 32107–32114. 63 indexed citations
12.
Bird, Louise E., Philip P. Chamberlain, Guillaume B. E. Stewart-Jones, et al.. (2002). Cloning, expression, purification, and crystallisation of HIV-2 reverse transcriptase. Protein Expression and Purification. 27(1). 12–18. 9 indexed citations
13.
14.
Ren, Jingshan, Jonathan M. Diprose, Jonathan Warren, et al.. (2000). Phenylethylthiazolylthiourea (PETT) Non-nucleoside Inhibitors of HIV-1 and HIV-2 Reverse Transcriptases. Journal of Biological Chemistry. 275(8). 5633–5639. 102 indexed citations
15.
Esnouf, Robert, Jingshan Ren, Carl Ross, et al.. (1995). Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. Nature Structural & Molecular Biology. 2(4). 303–308. 369 indexed citations
16.
Ren, Jingshan, Robert Esnouf, Andrew L. Hopkins, et al.. (1995). The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design. Structure. 3(9). 915–926. 150 indexed citations
17.
Stammers, D.K., D.O. Somers, Carl Ross, et al.. (1994). Crystals of HIV-1 Reverse Transcriptase Diffracting to 2·2 Å Resolution. Journal of Molecular Biology. 242(4). 586–588. 54 indexed citations
18.
19.
Stammers, D.K., Carl Ross, Haitham Idriss, & Denise M. Lowe. (1992). Formatin of heterodimers of human‐immunodeficiency‐virus‐type‐1 reverse transcriptase by recombination of separately purified subunits. European Journal of Biochemistry. 206(2). 437–440. 8 indexed citations
20.
Idriss, Haitham, D.K. Stammers, Carl Ross, & Roy G. Burns. (1991). The dynamic instability of microtubules is not modulated by α‐tubulin tyrosinylation. Cell Motility and the Cytoskeleton. 20(1). 30–37. 19 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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