Christopher J. Schofield

62.5k total citations · 8 hit papers
803 papers, 45.6k citations indexed

About

Christopher J. Schofield is a scholar working on Molecular Biology, Cancer Research and Molecular Medicine. According to data from OpenAlex, Christopher J. Schofield has authored 803 papers receiving a total of 45.6k indexed citations (citations by other indexed papers that have themselves been cited), including 511 papers in Molecular Biology, 185 papers in Cancer Research and 103 papers in Molecular Medicine. Recurrent topics in Christopher J. Schofield's work include Cancer, Hypoxia, and Metabolism (177 papers), Epigenetics and DNA Methylation (107 papers) and Antibiotic Resistance in Bacteria (103 papers). Christopher J. Schofield is often cited by papers focused on Cancer, Hypoxia, and Metabolism (177 papers), Epigenetics and DNA Methylation (107 papers) and Antibiotic Resistance in Bacteria (103 papers). Christopher J. Schofield collaborates with scholars based in United Kingdom, United States and Germany. Christopher J. Schofield's co-authors include Peter J. Ratcliffe, M.A. McDonough, Christopher W. Pugh, Jack E. Baldwin, Ya‐Min Tian, Kirsty S. Hewitson, Christoph Loenarz, I.J. Clifton, David R. Mole and Patrick H. Maxwell and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Christopher J. Schofield

795 papers receiving 44.7k citations

Hit Papers

Targeting of HIF-α to the... 1989 2026 2001 2013 2001 2001 2004 2011 2002 1000 2.0k 3.0k 4.0k
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. Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
    2001 4.5k citations Panu Jaakkola, David R. Mole et al. Science profile →
  2. C. elegans EGL-9 and Mammalian Homologs Define a Family of Dioxygenases that Regulate HIF by Prolyl Hydroxylation
    2001 2.7k citations Luke A. McNeill, Kirsty S. Hewitson et al. profile →
  3. Oxygen sensing by HIF hydroxylases
    2004 1.6k citations Christopher J. Schofield, Peter J. Ratcliffe profile →
  4. The oncometabolite 2‐hydroxyglutarate inhibits histone lysine demethylases
    2011 762 citations Rasheduzzaman Chowdhury, Ya‐Min Tian et al. profile →
  5. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
    2002 611 citations Michael Wilson, Timothy D. W. Claridge et al. profile →
  6. Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family
    2002 602 citations Kirsty S. Hewitson, Luke A. McNeill et al. Journal of Biological Chemistry profile →
  7. UNDP/World Bank/WHO special programme for research and training in tropical diseases (TDR)
    1989 321 citations Christopher J. Schofield profile →
  8. Synthesis of meta-substituted arene bioisosteres from [3.1.1]propellane
    2022 175 citations Christopher J. Schofield et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Christopher J. Schofield 27.9k 15.3k 4.5k 4.3k 4.1k 803 45.6k
Robert Huber 46.8k 1.7× 6.3k 0.4× 5.0k 1.1× 2.1k 0.5× 3.5k 0.9× 600 66.7k
Ralf W. Grosse‐Kunstleve 48.2k 1.7× 1.3k 0.1× 8.0k 1.8× 3.9k 0.9× 3.3k 0.8× 65 67.1k
Takashi Sügimura 24.4k 0.9× 13.6k 0.9× 4.2k 0.9× 1.7k 0.4× 5.6k 1.4× 1.2k 50.0k
Carl Nathan 23.9k 0.9× 4.3k 0.3× 2.9k 0.7× 10.6k 2.5× 2.0k 0.5× 318 73.0k
Stuart L. Schreiber 66.7k 2.4× 9.4k 0.6× 4.7k 1.0× 3.7k 0.9× 19.9k 4.8× 600 91.9k
Kevin Cowtan 44.2k 1.6× 1.1k 0.1× 7.3k 1.6× 3.8k 0.9× 3.1k 0.8× 63 62.9k
Airlie J. McCoy 43.0k 1.5× 1.2k 0.1× 6.7k 1.5× 3.7k 0.9× 2.7k 0.7× 96 60.1k
John A. Tainer 30.1k 1.1× 2.3k 0.2× 4.5k 1.0× 1.2k 0.3× 1.4k 0.3× 452 41.2k
Paul Emsley 44.0k 1.6× 1.1k 0.1× 7.1k 1.6× 3.8k 0.9× 3.1k 0.7× 45 61.8k
Gautam Sethi 26.2k 0.9× 9.1k 0.6× 1.4k 0.3× 3.3k 0.8× 3.3k 0.8× 615 48.2k

Countries citing papers authored by Christopher J. Schofield

Since Specialization
Citations

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

Fields of papers citing papers by Christopher J. Schofield

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher J. Schofield

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher J. Schofield. A scholar is included among the top collaborators of Christopher J. Schofield 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 Christopher J. Schofield. Christopher J. Schofield 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.
Calvopiña, Karina, Philip Hinchliffe, Catherine L. Tooke, et al.. (2025). Electrostatic interactions influence diazabicyclooctane inhibitor potency against OXA-48-like β-lactamases. RSC Medicinal Chemistry. 16(11). 5441–5455. 1 indexed citations
2.
Salah, E., Bhaskar Bhushan, A. Szykowska, et al.. (2024). Focused Screening Identifies Different Sensitivities of Human TET Oxygenases to the Oncometabolite 2-Hydroxyglutarate. Journal of Medicinal Chemistry. 67(6). 4525–4540. 4 indexed citations
3.
Miura, Takashi, Tika R. Malla, Lennart Brewitz, et al.. (2024). Cyclic β2,3-amino acids improve the serum stability of macrocyclic peptide inhibitors targeting the SARS-CoV-2 main protease. Bulletin of the Chemical Society of Japan. 97(5). uoae018–uoae018. 12 indexed citations
4.
Zhang, Zhihong, et al.. (2024). Substitution of 2-oxoglutarate alters reaction outcomes of the Pseudomonas savastanoi ethylene-forming enzyme. Journal of Biological Chemistry. 300(8). 107546–107546. 5 indexed citations
5.
Brewitz, Lennart, et al.. (2024). Thiophene-fused γ-lactams inhibit the SARS-CoV-2 main protease via reversible covalent acylation. Chemical Science. 15(20). 7667–7678. 1 indexed citations
6.
Pedroso, Marcelo Monteiro, et al.. (2023). Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup—emerging targets to combat antibiotic resistance. Frontiers in Chemistry. 11. 1196073–1196073. 8 indexed citations
7.
Chaturvedi, Shobhit S., et al.. (2023). Dioxygen Binding Is Controlled by the Protein Environment in Non‐heme FeII and 2‐Oxoglutarate Oxygenases: A Study on Histone Demethylase PHF8 and an Ethylene‐Forming Enzyme. Chemistry - A European Journal. 29(24). e202300138–e202300138. 10 indexed citations
8.
Sueldo, Daniela J., Farnusch Kaschani, Daniel Krahn, et al.. (2023). Activity‐based proteomics uncovers suppressed hydrolases and a neo‐functionalised antibacterial enzyme at the plant–pathogen interface. New Phytologist. 241(1). 394–408. 10 indexed citations
9.
Schofield, Christopher J., et al.. (2023). Electrochemical Nanoreactor Provides a Comprehensive View of Isocitrate Dehydrogenase Cancer‐drug Kinetics. Angewandte Chemie International Edition. 62(42). e202309149–e202309149. 7 indexed citations
10.
Brewitz, Lennart, Anthony Tumber, Armin Thalhammer, et al.. (2020). Synthesis of Novel Pyridine‐Carboxylates as Small‐Molecule Inhibitors of Human Aspartate/Asparagine‐β‐Hydroxylase. ChemMedChem. 15(13). 1139–1149. 18 indexed citations
11.
Pai, Chen‐Chun, Kuo‐Feng Hsu, Andrea Keszthelyi, et al.. (2019). An essential role for dNTP homeostasis following CDK-induced replication stress. Journal of Cell Science. 132(6). 14 indexed citations
12.
Lippl, Kerstin, et al.. (2018). Born to sense: biophysical analyses of the oxygen sensing prolyl hydroxylase from the simplest animal Trichoplax adhaerens. SHILAP Revista de lepidopterología. 1 indexed citations
13.
Emir, Uzay, Sarah J. Larkin, Nick de Pennington, et al.. (2015). Noninvasive Quantification of 2-Hydroxyglutarate in Human Gliomas with IDH1 and IDH2 Mutations. Cancer Research. 76(1). 43–49. 94 indexed citations
14.
Hopkinson, Richard J., Louise J. Walport, Martin Münzel, et al.. (2013). Is JmjC Oxygenase Catalysis Limited to Demethylation?. Angewandte Chemie. 125(30). 7863–7867. 4 indexed citations
15.
Webby, Celia J., Alexander Wolf, Natalia Gromak, et al.. (2009). Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing. Science. 325(5936). 90–93. 315 indexed citations
16.
McDonough, M.A., et al.. (2008). Asparagine β-hydroxylation stabilizes the ankyrin repeat domain fold. Molecular BioSystems. 5(1). 52–58. 52 indexed citations
17.
McDonough, M.A., Vivian Li, Emily Flashman, et al.. (2006). Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proceedings of the National Academy of Sciences. 103(26). 9814–9819. 295 indexed citations
18.
Hewitson, Kirsty S., et al.. (2005). Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling. Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences. 363(1829). 807–828. 48 indexed citations
19.
Jaakkola, Panu, David R. Mole, Ya‐Min Tian, et al.. (2001). Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation. Science. 292(5516). 468–472. 4523 indexed citations breakdown →
20.
Baldwin, Jack E., Jonathan M. Blackburn, Christopher J. Schofield, & John D. Sutherland. (1990). High level expression inEscherichia coliof a fungal gene under the control of strong promoters. FEMS Microbiology Letters. 68(1-2). 45–51. 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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