D.K. Stammers

8.8k citations
113 papers · 7.1k · h-index 47

Impact in

  • Virology top 0.1%
    • HIV Research and Treatment
  • Infectious Diseases top 0.2%
    • HIV/AIDS drug development and treatment
    • HIV/AIDS Research and Interventions

Papers in

  • Molecular Biology 72
    • Biochemical and Molecular Research 35
    • RNA and protein synthesis mechanisms 13
  • Infectious Diseases 54
    • HIV/AIDS drug development and treatment 48
    • HIV/AIDS Research and Interventions 7
Co-authors
Jingshan Ren (50 shared papers)David I. Stuart (28 shared papers)Robert Esnouf (12 shared papers)Carl Ross (12 shared papers)E. Yvonne Jones (11 shared papers)Hilary Muirhead (6 shared papers)Andrew L. Hopkins (8 shared papers)Michael Levine (3 shared papers)
Journals
Journal of Biological Chemistry (12 papers)Journal of Medicinal Chemistry (9 papers)Journal of Molecular Biology (9 papers)FEBS Letters (7 papers)Protein Science (5 papers)
Partner nations
United KingdomUnited StatesBelgium

In The Last Decade

D.K. Stammers

112 papers receiving 6.9k citations

Peers

D.K. Stammers
Comparison fields: 5 of 126
  • Virology 2.6k
  • Infectious Diseases 3.4k
  • Molecular Biology 3.6k
  • Organic Chemistry 1.1k
  • Epidemiology 949
Replace Jingshan Ren with:
Jingshan Ren United Kingdom
Robert Esnouf United Kingdom
Giovanni Maga Italy
Paul L. Darke United States
Michael A. Parniak Canada
Ben M. Dunn United States
Kalyan Das United States
William G. Rice United States
Jan Balzarini Belgium
Carole A. Bewley United States
D.K. Stammers relative to Jingshan Ren United Kingdom Jingshan Ren's profile →
Citations per field
00.5×1.5×
Jingshan Ren · 1×
Citations per year

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-authors

The 25 scholars most cited alongside D.K. Stammers, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.

Border = papers with D.K. Stammers Line = papers co-authored together D.K. Stammers links everyone, so they are left out of the graph.

All Works

20 of 20 papers shown

Showing the 20 most-cited of 113 papers — load more, or switch the sort, to bring in the rest.

#Work
1
High resolution structures of HIV-1 RT from four RT–inhibitor complexes
Nature Structural & Molecular Biology ·Jingshan Ren, Robert Esnouf, Elspeth F. Garman, D.O. Somers, Carl Ross, Ian Kirby, James Keeling, G. Darby, E. Yvonne Jones, David I. Stuart, D.K. Stammers
1995453
2
Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
Journal of Molecular Biology ·David I. Stuart, Michael Levine, Hilary Muirhead, D.K. Stammers
1979400
3
Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors
Nature Structural & Molecular Biology ·Robert Esnouf, Jingshan Ren, Carl Ross, E. Yvonne Jones, D.K. Stammers, David I. Stuart
1995388
4
Complexes of HIV-1 Reverse Transcriptase with Inhibitors of the HEPT Series Reveal Conformational Changes Relevant to the Design of Potent Non-Nucleoside Inhibitors
Journal of Medicinal Chemistry ·Andrew L. Hopkins, Jingshan Ren, Robert Esnouf, Benjamin E. Willcox, E. Yvonne Jones, Carl Ross, Tadashi Miyasaka, Richard Walker, Hiromichi Tanaka, D.K. Stammers, David I. Stuart
1996314
5
Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase
Nature Structural Biology ·Aniruddha Achari, (unknown), J.N. Champness, P.K. Bryant, J. Rosemond, D.K. Stammers
1997248
6
Electron density map of apoferritin at 2.8-Å resolution
Nature ·Stephen Banyard, D.K. Stammers, Pauline M. Harrison
1978240
7
Structural Basis for the Resilience of Efavirenz (DMP-266) to Drug Resistance Mutations in HIV-1 Reverse Transcriptase
Structure ·Jingshan Ren, John Milton, Kurt Weaver, Steven A. Short, David I. Stuart, D.K. Stammers
2000233
8
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.
Nature Structural Biology ·Karl Harlos, Christopher J. Schofield, Zhihong Zhang, Jingshan Ren, D.K. Stammers, Jack E. Baldwin
2000228
9
A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization
Acta Crystallographica Section D Biological Crystallography ·Thomas S. Walter, Jonathan M. Diprose, Chris Mayo, Christian Siebold, Mike G. Pickford, Lester Carter, Geoff Sutton, (unknown), James Brown, (unknown), Guillaume B. E. Stewart-Jones, Jonathan M. Grimes, D.K. Stammers, Robert Esnouf, E. Yvonne Jones, Raymond J. Owens, David I. Stuart, Karl Harlos
2005214
10
Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor
Proceedings of the National Academy of Sciences ·Robert Esnouf, Jingshan Ren, Andrew L. Hopkins, Carl Ross, E. Yvonne Jones, D.K. Stammers, David I. Stuart
1997166
11
Structure of HIV-2 reverse transcriptase at 2.35-Å resolution and the mechanism of resistance to non-nucleoside inhibitors
Proceedings of the National Academy of Sciences ·Jingshan Ren, Louise E. Bird, Philip P. Chamberlain, Guillaume B. E. Stewart-Jones, David I. Stuart, D.K. Stammers
2002163
12
Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors 1 1Edited by J. Karn
Journal of Molecular Biology ·Jingshan Ren, C.E. Nichols, Louise E. Bird, Philip P. Chamberlain, Kurt Weaver, Sarah J. Short, David I. Stuart, D.K. Stammers
2001158
13
The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design
Structure ·Jingshan Ren, Robert Esnouf, Andrew L. Hopkins, Carl Ross, E. Yvonne Jones, D.K. Stammers, David I. Stuart
1995156
14
Structure−Activity Relationship Studies of Novel Benzophenones Leading to the Discovery of a Potent, Next Generation HIV Nonnucleoside Reverse Transcriptase Inhibitor
Journal of Medicinal Chemistry ·Karen R. Romines, George A. Freeman, Lee T. Schaller, Jill R. Cowan, Steve S. Gonzales, Jeffrey H. Tidwell, C. Webster Andrews, D.K. Stammers, Richard Hazen, Robert G. Ferris, Steven A. Short, Joseph H. Chan, Lawrence R. Boone
2005148
15
A Family of Insertion Mutations between Codons 67 and 70 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confer Multinucleoside Analog Resistance
Antimicrobial Agents and Chemotherapy ·Brendan Larder, Stuart Bloor, Sharon D. Kemp, Kurt Hertogs, Rémi Desmet, Veronica Miller, Martin Stürmer, Schlomo Staszewski, Jingshan Ren, D.K. Stammers, David I. Stuart, Rudi Pauwels
1999145
16
HIV-1 reverse transcriptase: crystallization and analysis of domain structure by limited proteolysis
Biochemistry ·Denise M. Lowe, Alastair Aitken, Christopher Bradley, G. Darby, Brendan Larder, Kenneth L. Powell, D. J. M. Purifoy, Margaret Tisdale, D.K. Stammers
1988135
17
Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase
Virus Research ·Jingshan Ren, D.K. Stammers
2008120
18
Design of MKC-442 (Emivirine) Analogues with Improved Activity Against Drug-Resistant HIV Mutants
Journal of Medicinal Chemistry ·Andrew L. Hopkins, Jingshan Ren, Hiromichi Tanaka, Masanori Baba, Mika Okamato, David I. Stuart, D.K. Stammers
1999107
19
Binding of the Second Generation Non-nucleoside Inhibitor S-1153 to HIV-1 Reverse Transcriptase Involves Extensive Main Chain Hydrogen Bonding
Journal of Biological Chemistry ·Jingshan Ren, Charles E. Nichols, Louise E. Bird, Tamio Fujiwara, Hirohiko Sugimoto, David I. Stuart, D.K. Stammers
2000106
20
Phenylethylthiazolylthiourea (PETT) Non-nucleoside Inhibitors of HIV-1 and HIV-2 Reverse Transcriptases
Journal of Biological Chemistry ·Jingshan Ren, Jonathan M. Diprose, Jonathan Warren, Robert Esnouf, Louise E. Bird, Shinji Ikemizu, Martin J. Slater, John Milton, Jan Balzarini, David I. Stuart, D.K. Stammers
2000104

About D.K. Stammers

D.K. Stammers is a scholar working on Molecular Biology, Infectious Diseases, Virology, Materials Chemistry and Epidemiology, having authored 113 papers that have together received 7.1k indexed citations. Recurring topics across this work include HIV/AIDS drug development and treatment (48 papers), HIV Research and Treatment (38 papers), Biochemical and Molecular Research (35 papers), Enzyme Structure and Function (24 papers), RNA and protein synthesis mechanisms (13 papers), Bacterial Genetics and Biotechnology (12 papers), Pneumocystis jirovecii pneumonia detection and treatment (11 papers) and HIV/AIDS Research and Interventions (7 papers). The work is most often cited by research in Virology (2.6k citations), Infectious Diseases (3.4k citations), Molecular Biology (3.6k citations), Organic Chemistry (1.1k citations) and Epidemiology (949 citations). D.K. Stammers has collaborated with scholars based in United Kingdom, United States and Belgium. Frequent 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 J.N. Champness. Their work appears in journals such as Journal of Biological Chemistry, Journal of Medicinal Chemistry, Journal of Molecular Biology, FEBS Letters and Protein Science.

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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