Mark Skehel

15.1k total citations · 3 hit papers
151 papers, 9.9k citations indexed

About

Mark Skehel is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, Mark Skehel has authored 151 papers receiving a total of 9.9k indexed citations (citations by other indexed papers that have themselves been cited), including 117 papers in Molecular Biology, 24 papers in Cell Biology and 14 papers in Oncology. Recurrent topics in Mark Skehel's work include Mitochondrial Function and Pathology (26 papers), DNA Repair Mechanisms (22 papers) and RNA and protein synthesis mechanisms (19 papers). Mark Skehel is often cited by papers focused on Mitochondrial Function and Pathology (26 papers), DNA Repair Mechanisms (22 papers) and RNA and protein synthesis mechanisms (19 papers). Mark Skehel collaborates with scholars based in United Kingdom, United States and Germany. Mark Skehel's co-authors include Sarah Maslen, John E. Walker, Ian M. Fearnley, Helen R. Flynn, Stephen C. West, Simon J. Boulton, Gianluca Degliesposti, Michael J. Runswick, Miguel G. Blanco and Leonid A. Sazanov and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Mark Skehel

144 papers receiving 9.8k citations

Hit Papers

Atomic structure of the entire mammalian mitochondrial co... 2016 2026 2019 2022 2016 2020 2018 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark Skehel United Kingdom 54 8.0k 1.5k 1.1k 730 671 151 9.9k
Namrata D. Udeshi United States 37 7.7k 1.0× 3.0k 2.0× 1.1k 0.9× 888 1.2× 483 0.7× 81 10.0k
Chanchal Kumar Germany 26 8.4k 1.1× 1.2k 0.8× 1.4k 1.3× 506 0.7× 758 1.1× 35 10.8k
Florian Gnad Germany 37 11.3k 1.4× 1.7k 1.1× 1.9k 1.7× 775 1.1× 785 1.2× 54 13.6k
Chad A. Brautigam United States 47 5.1k 0.6× 1.5k 1.0× 418 0.4× 950 1.3× 413 0.6× 137 7.7k
Kalle Gehring Canada 53 7.0k 0.9× 1.8k 1.2× 598 0.5× 775 1.1× 1.2k 1.8× 198 9.3k
Sean A. Beausoleil United States 25 7.3k 0.9× 1.5k 1.0× 1.0k 0.9× 448 0.6× 813 1.2× 30 9.0k
Michael L. Nielsen Denmark 55 10.8k 1.3× 1.2k 0.8× 2.8k 2.5× 971 1.3× 741 1.1× 143 13.7k
Douglas Cyr United States 47 7.0k 0.9× 2.8k 1.9× 469 0.4× 834 1.1× 917 1.4× 113 9.2k
Daniel Heß Switzerland 53 6.6k 0.8× 1.1k 0.7× 1.2k 1.0× 735 1.0× 364 0.5× 126 8.6k
Philip Coffino United States 52 6.6k 0.8× 1.1k 0.7× 785 0.7× 553 0.8× 736 1.1× 131 7.6k

Countries citing papers authored by Mark Skehel

Since Specialization
Citations

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

Fields of papers citing papers by Mark Skehel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark Skehel

This figure shows the co-authorship network connecting the top 25 collaborators of Mark Skehel. A scholar is included among the top collaborators of Mark Skehel 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 Mark Skehel. Mark Skehel 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.
Dudley-Fraser, Jane, Diego Esposito, Sarah Maslen, et al.. (2025). Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2. RSC Chemical Biology. 7(1). 153–168.
2.
Patel, Avnish, Helen R. Flynn, Konstantinos Koussis, et al.. (2024). Plasmodium falciparum protein phosphatase PP7 is required for early ring-stage development. mBio. 15(11). e0253924–e0253924.
3.
Rowe, Sam M., Alan R. Rendina, Emma K. Grant, et al.. (2024). Expedited SARS‐CoV‐2 Main Protease Inhibitor Discovery through Modular ‘Direct‐to‐Biology’ Screening. Angewandte Chemie. 137(6). 1 indexed citations
4.
Wrobel, Antoni G., Sarah Maslen, Antonio Torres-Méndez, et al.. (2024). The V-ATPase/ATG16L1 axis is controlled by the V1H subunit. Molecular Cell. 84(15). 2966–2983.e9. 12 indexed citations
5.
Salzano, Giulia, Theodora Sideri, Steven Howell, et al.. (2023). The yeast RNA methylation complex consists of conserved yet reconfigured components with m6A-dependent and independent roles. eLife. 12. 1 indexed citations
6.
Mali, Girish R., Ferdos Abid Ali, Clinton K. Lau, et al.. (2021). Shulin packages axonemal outer dynein arms for ciliary targeting. Science. 371(6532). 910–916. 35 indexed citations
7.
Peak‐Chew, Sew‐Yeu, Amy Switzer, Lynn Burchell, et al.. (2021). Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A. Antioxidants. 10(6). 841–841. 15 indexed citations
8.
Tremel, Shirley, Yohei Ohashi, Dustin R. Morado, et al.. (2021). Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes. Nature Communications. 12(1). 1564–1564. 76 indexed citations
9.
Malvezzi, Francesca, Christopher J. Stubbs, Thomas A. Jowitt, et al.. (2021). Phosphorylation-dependent BRD4 dimerization and implications for therapeutic inhibition of BET family proteins. Communications Biology. 4(1). 1273–1273. 14 indexed citations
10.
Querido, Jailson Brito, Masaaki Sokabe, S.H.W. Kraatz, et al.. (2020). Structure of a human 48 S translational initiation complex. Science. 369(6508). 1220–1227. 149 indexed citations
11.
Alvira, Sara, Daniel W. Watkins, William J. Allen, et al.. (2020). Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis. eLife. 9. 37 indexed citations
12.
Pye, Valerie E., Annachiara Rosa, Weston B. Struwe, et al.. (2020). A bipartite structural organization defines the SERINC family of HIV-1 restriction factors. Nature Structural & Molecular Biology. 27(1). 78–83. 41 indexed citations
13.
Bellelli, Roberto, Ondrej Beláň, Valerie E. Pye, et al.. (2018). POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication. Molecular Cell. 72(1). 112–126.e5. 94 indexed citations
14.
Martino, Fabrizio, Mohinder Pal, Hugo Muñoz-Hernández, et al.. (2018). RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nature Communications. 9(1). 1501–1501. 53 indexed citations
15.
Degliesposti, Gianluca, M.L. Kilkenny, Sarah Maslen, et al.. (2017). Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin. Nucleic Acids Research. 45(9). 5555–5563. 12 indexed citations
16.
Willmann, Katharina, Siim Pauklin, Rangam Gopinath, et al.. (2012). A role for the RNA pol II–associated PAF complex in AID-induced immune diversification. The Journal of Experimental Medicine. 209(11). 2099–2111. 53 indexed citations
17.
Gari, Kerstin, Ana M. Ortiz, Valérie Borel, et al.. (2012). MMS19 Links Cytoplasmic Iron-Sulfur Cluster Assembly to DNA Metabolism. Science. 337(6091). 243–245. 180 indexed citations
18.
Mochida, Satoru, Sarah Maslen, Mark Skehel, & Tim Hunt. (2010). Greatwall Phosphorylates an Inhibitor of Protein Phosphatase 2Α That Is Essential for Mitosis. Science. 330(6011). 1670–1673. 340 indexed citations
19.
Hořejšı́, Zuzana, Nicola Wiechens, Sophie E. Polo, et al.. (2009). Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1. Science. 325(5945). 1240–1243. 467 indexed citations
20.
White, Ian R., Russell Pickford, John Wood, et al.. (2004). A statistical comparison of silver and SYPRO Ruby staining for proteomic analysis. Electrophoresis. 25(17). 3048–3054. 58 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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