David Hargreaves

2.0k total citations
35 papers, 893 citations indexed

About

David Hargreaves is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, David Hargreaves has authored 35 papers receiving a total of 893 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 10 papers in Materials Chemistry and 6 papers in Genetics. Recurrent topics in David Hargreaves's work include Enzyme Structure and Function (10 papers), Protein Structure and Dynamics (7 papers) and Bacterial Genetics and Biotechnology (6 papers). David Hargreaves is often cited by papers focused on Enzyme Structure and Function (10 papers), Protein Structure and Dynamics (7 papers) and Bacterial Genetics and Biotechnology (6 papers). David Hargreaves collaborates with scholars based in United Kingdom, United States and Netherlands. David Hargreaves's co-authors include John B. Rafferty, David W. Rice, Robert G. Lloyd, Peter J. Artymiuk, Svetlana E. Sedelnikova, Gary J. Sharples, Julie Wilson, Patrick J. Baker, Akeel A. Mahdi and Simon O’Keefe and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Bioinformatics.

In The Last Decade

David Hargreaves

35 papers receiving 857 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David Hargreaves United Kingdom 16 594 248 107 83 75 35 893
Benjamin T. Porebski Australia 19 769 1.3× 122 0.5× 153 1.4× 76 0.9× 50 0.7× 30 1.1k
Philippe Cuniasse France 19 625 1.1× 82 0.3× 89 0.8× 147 1.8× 45 0.6× 31 968
John F. Reidhaar-Olson United States 8 862 1.5× 162 0.7× 211 2.0× 125 1.5× 77 1.0× 15 1.0k
Clarissa G. Jakob United States 17 594 1.0× 238 1.0× 80 0.7× 158 1.9× 18 0.2× 23 1.0k
D. Ogg United Kingdom 16 673 1.1× 136 0.5× 92 0.9× 81 1.0× 60 0.8× 23 990
Kush Dalal Canada 18 748 1.3× 344 1.4× 34 0.3× 142 1.7× 74 1.0× 40 1.2k
Jakob Fuhrmann United States 20 947 1.6× 177 0.7× 92 0.9× 219 2.6× 128 1.7× 27 1.4k
S. Abdel‐Meguid United States 9 444 0.7× 134 0.5× 144 1.3× 85 1.0× 66 0.9× 15 841
Miljan Simonović United States 24 1.0k 1.7× 171 0.7× 72 0.7× 54 0.7× 32 0.4× 41 1.5k
Michael D. Ward United States 17 991 1.7× 84 0.3× 93 0.9× 107 1.3× 89 1.2× 33 1.5k

Countries citing papers authored by David Hargreaves

Since Specialization
Citations

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

Fields of papers citing papers by David Hargreaves

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Hargreaves

This figure shows the co-authorship network connecting the top 25 collaborators of David Hargreaves. A scholar is included among the top collaborators of David Hargreaves 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 David Hargreaves. David Hargreaves 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.
Chen, Qian, et al.. (2023). Not getting in too deep: A practical deep learning approach to routine crystallisation image classification. PLoS ONE. 18(3). e0282562–e0282562. 4 indexed citations
2.
Hargreaves, David, Rodrigo J. Carbajo, Michael S. Bodnarchuk, et al.. (2023). Design of rigid protein–protein interaction inhibitors enables targeting of undruggable Mcl-1. Proceedings of the National Academy of Sciences. 120(21). e2221967120–e2221967120. 5 indexed citations
3.
Petrović, Dušan, James S. Scott, Michael S. Bodnarchuk, et al.. (2022). Virtual Screening in the Cloud Identifies Potent and Selective ROS1 Kinase Inhibitors. Journal of Chemical Information and Modeling. 62(16). 3832–3843. 9 indexed citations
4.
Wilson, Julie, et al.. (2020). Predicting the Effect of Chemical Factors on the pH of Crystallization Trials. iScience. 23(6). 101219–101219. 3 indexed citations
5.
Lupták, Jakub, Michał Biśta, David I. Fisher, et al.. (2019). Antibody fragments structurally enable a drug-discovery campaign on the cancer target Mcl-1. Acta Crystallographica Section D Structural Biology. 75(11). 1003–1014. 7 indexed citations
6.
Nimrod, Guy, Sharon Fischman, Mark Austin, et al.. (2018). Computational Design of Epitope-Specific Functional Antibodies. Cell Reports. 25(8). 2121–2131.e5. 53 indexed citations
7.
Hargreaves, David, et al.. (2015). Using isoelectric point to determine the pH for initial protein crystallization trials. Bioinformatics. 31(9). 1444–1451. 43 indexed citations
8.
Wilson, Julie, et al.. (2014). A high-throughput colourimetric method for the determination of pH in crystallization screens. Acta Crystallographica Section D Biological Crystallography. 70(9). 2367–2375. 7 indexed citations
9.
Waring, Michael J., Scott Boyd, Leonie Campbell, et al.. (2013). Optimising pharmacokinetics of glucokinase activators with matched triplicate design sets – the discovery of AZD3651 and AZD9485. MedChemComm. 4(4). 663–663. 6 indexed citations
10.
Hargreaves, David. (2011). A manual low-cost protein-crystallization plate jig forin situdiffraction in the home laboratory. Journal of Applied Crystallography. 45(1). 138–140. 13 indexed citations
11.
Savi, Chris De, Andrew Morley, Attilla Ting, et al.. (2011). Selective non zinc binding inhibitors of MMP13. Bioorganic & Medicinal Chemistry Letters. 21(14). 4215–4219. 18 indexed citations
12.
Lowe, David C., S. Gerhardt, Alison Ward, et al.. (2010). Engineering a High-Affinity Anti-IL-15 Antibody: Crystal Structure Reveals an α-Helix in VH CDR3 as Key Component of Paratope. Journal of Molecular Biology. 406(1). 160–175. 14 indexed citations
13.
Gerhardt, S., Eileen McCall, Liz Flavell, et al.. (2007). Crystal Structures of Human ADAMTS-1 Reveal a Conserved Catalytic Domain and a Disintegrin-like Domain with a Fold Homologous to Cysteine-Rich Domains. Journal of Molecular Biology. 373(4). 891–902. 68 indexed citations
14.
Hargreaves, David, Rafael Giraldo, Sandra Santos‐Sierra, et al.. (2002). Crystallization and preliminary X-ray crystallographic studies on theparD-encoded protein Kid fromEscherichia coliplasmid R1. Acta Crystallographica Section D Biological Crystallography. 58(2). 355–358. 10 indexed citations
15.
Hargreaves, David, Sandra Santos‐Sierra, Rafael Giraldo, et al.. (2002). Structural and Functional Analysis of the Kid Toxin Protein from E. coli Plasmid R1. Structure. 10(10). 1425–1433. 69 indexed citations
16.
Hargreaves, David, et al.. (1999). Crystallization ofEscherichia coliRuvA complexed with a synthetic Holliday junction. Acta Crystallographica Section D Biological Crystallography. 55(1). 263–265. 4 indexed citations
17.
Rafferty, John B., David Hargreaves, Peter J. Artymiuk, et al.. (1998). Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the holliday junction. Journal of Molecular Biology. 278(1). 105–116. 22 indexed citations
18.
Hargreaves, David, David W. Rice, Svetlana E. Sedelnikova, et al.. (1998). Crystal structure of E.coli RuvA with bound DNA Holliday junction at 6 Å resolution. Nature Structural Biology. 5(6). 441–446. 123 indexed citations
19.
Simmonds, Peter, P.L. Yap, Peter Balfe, et al.. (1990). The polymerase chain reaction in the diagnosis of vertically transmitted HIV infection. AIDS. 4(5). 393–398. 32 indexed citations
20.
Hargreaves, David, Stuart Egginton, & O Hudlická. (1990). Changes in capillary perfusion induced by different patterns of activity in rat skeletal muscle. Microvascular Research. 40(1). 14–28. 32 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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