Ingrid Dreveny

2.0k total citations
38 papers, 1.5k citations indexed

About

Ingrid Dreveny is a scholar working on Molecular Biology, Genetics and Cell Biology. According to data from OpenAlex, Ingrid Dreveny has authored 38 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 7 papers in Genetics and 7 papers in Cell Biology. Recurrent topics in Ingrid Dreveny's work include Ubiquitin and proteasome pathways (10 papers), Endoplasmic Reticulum Stress and Disease (7 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (7 papers). Ingrid Dreveny is often cited by papers focused on Ubiquitin and proteasome pathways (10 papers), Endoplasmic Reticulum Stress and Disease (7 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (7 papers). Ingrid Dreveny collaborates with scholars based in United Kingdom, Austria and United States. Ingrid Dreveny's co-authors include Xiaodong Zhang, Paul S. Freemont, Karl Gruber, Jonas Emsley, Hisao Kondo, Keiji Uchiyama, Anton Glieder, Christoph Kratky, Fabienne Beuron and Anthony W. Shaw and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Ingrid Dreveny

36 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ingrid Dreveny United Kingdom 24 1.2k 424 161 142 140 38 1.5k
Tomoko Komiyama Japan 18 821 0.7× 241 0.6× 93 0.6× 45 0.3× 71 0.5× 38 1.3k
Joyce Chiu Australia 18 759 0.7× 323 0.8× 86 0.5× 33 0.2× 45 0.3× 38 1.3k
Daniel J. Anderson United States 17 1.8k 1.6× 609 1.4× 114 0.7× 38 0.3× 68 0.5× 27 2.2k
Russell Bell United States 19 1.1k 1.0× 172 0.4× 96 0.6× 54 0.4× 46 0.3× 29 1.7k
Klaus Godl Germany 20 1.0k 0.9× 154 0.4× 112 0.7× 57 0.4× 50 0.4× 23 1.5k
Christian N. Cunningham United States 12 822 0.7× 341 0.8× 187 1.2× 40 0.3× 78 0.6× 22 1.2k
Robin A. Weinberg United States 15 802 0.7× 140 0.3× 79 0.5× 58 0.4× 67 0.5× 19 1.2k
Qingxiang Sun China 20 1.0k 0.9× 213 0.5× 79 0.5× 51 0.4× 54 0.4× 59 1.4k
Hendrik L. De Bondt Belgium 14 1.1k 1.0× 356 0.8× 78 0.5× 46 0.3× 213 1.5× 22 1.6k
Rochelle C. J. D’Souza Germany 11 1.4k 1.2× 237 0.6× 108 0.7× 55 0.4× 52 0.4× 17 1.7k

Countries citing papers authored by Ingrid Dreveny

Since Specialization
Citations

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

Fields of papers citing papers by Ingrid Dreveny

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ingrid Dreveny

This figure shows the co-authorship network connecting the top 25 collaborators of Ingrid Dreveny. A scholar is included among the top collaborators of Ingrid Dreveny 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 Ingrid Dreveny. Ingrid Dreveny 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.
Allen, John T., et al.. (2025). A versatile fluorescence polarization-based deubiquitination assay using an isopeptide bond substrate mimetic (IsoMim). Journal of Biological Chemistry. 301(7). 110342–110342.
2.
Saleem, Muhammad, Monika Pathak, Shabir Najmudin, et al.. (2025). Crystal structure of coagulation factor XII N-terminal domains 1–5. Acta Crystallographica Section D Structural Biology. 81(7). 380–393.
3.
Li, Chan, Szu Shen Wong, Hyo Jung Kim, et al.. (2023). Structures of factor XI and prekallikrein bound to domain 6 of high–molecular weight kininogen reveal alternate domain 6 conformations and exosites. Journal of Thrombosis and Haemostasis. 21(9). 2378–2389. 10 indexed citations
4.
Ducker, Charles, Monika Pathak, Ingrid Dreveny, et al.. (2023). Characterisation of geranylgeranyl diphosphate synthase from the sandfly Lutzomyia longipalpis. Insect Biochemistry and Molecular Biology. 161. 104001–104001. 6 indexed citations
5.
Owen, Jonathan P., et al.. (2022). Next-Generation Phage Display to Identify Peptide Ligands of Deubiquitinases. Methods in molecular biology. 2591. 189–218. 3 indexed citations
6.
Sánchez-Bailón, María Pilar, Karan Sharma, Gavin S. McNee, et al.. (2021). Arginine methylation and ubiquitylation crosstalk controls DNA end-resection and homologous recombination repair. Nature Communications. 12(1). 6313–6313. 26 indexed citations
7.
Davies, Clare C., et al.. (2020). Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4). Biochemical Journal. 477(4). 787–800. 14 indexed citations
8.
Slater, Alexandre, Keith R. McCrae, Ingrid Dreveny, et al.. (2020). Factor XII and kininogen asymmetric assembly with gC1qR/C1QBP/P32 is governed by allostery. Blood. 136(14). 1685–1697. 23 indexed citations
9.
Li, Chan, Monika Pathak, Keith R. McCrae, et al.. (2019). Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI. Journal of Thrombosis and Haemostasis. 17(5). 759–770. 22 indexed citations
10.
Pathak, Monika, Chan Li, Benny Danilo Belviso, et al.. (2019). Crystal structures of the recombinant β-factor XIIa protease with bound Thr-Arg and Pro-Arg substrate mimetics. Acta Crystallographica Section D Structural Biology. 75(6). 578–591. 16 indexed citations
11.
Emsley, Jonas, et al.. (2018). The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel. Journal of Biological Chemistry. 293(45). 17362–17374. 40 indexed citations
12.
Densham, Ruth M., Ben C. Maddison, Joanna R. Morris, et al.. (2018). Discovery of peptide ligands targeting a specific ubiquitin-like domain–binding site in the deubiquitinase USP11. Journal of Biological Chemistry. 294(2). 424–436. 25 indexed citations
13.
Drees, Steffen L., Chan Li, Muhammad Saleem, et al.. (2016). PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal. Journal of Biological Chemistry. 291(13). 6610–6624. 56 indexed citations
14.
Pathak, Monika, Pascal G. Wilmann, Peter M. Fischer, et al.. (2015). Coagulation factor XII protease domain crystal structure. Journal of Thrombosis and Haemostasis. 13(4). 580–591. 49 indexed citations
15.
Dreveny, Ingrid, Baigong Yue, Marie C. Messmer, et al.. (2013). The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Research. 42(2). 822–835. 64 indexed citations
16.
Rengachari, Srinivasan, G.A. Bezerra, Christian Gruber, et al.. (2012). The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1821(7). 1012–1021. 43 indexed citations
17.
Dreveny, Ingrid, Aleksandra Andryushkova, Anton Glieder, Karl Gruber, & Christoph Kratky. (2009). Substrate Binding in the FAD-Dependent Hydroxynitrile Lyase from Almond Provides Insight into the Mechanism of Cyanohydrin Formation and Explains the Absence of Dehydrogenation Activity,. Biochemistry. 48(15). 3370–3377. 31 indexed citations
18.
Beuron, Fabienne, Ingrid Dreveny, Xuemei Yuan, et al.. (2006). Conformational changes in the AAA ATPase p97–p47 adaptor complex. The EMBO Journal. 25(9). 1967–1976. 86 indexed citations
19.
Uchiyama, Keiji, Go Totsukawa, Maija Puhka, et al.. (2006). p37 Is a p97 Adaptor Required for Golgi and ER Biogenesis in Interphase and at the End of Mitosis. Developmental Cell. 11(6). 803–816. 89 indexed citations
20.
Dreveny, Ingrid, Christoph Kratky, & Karl Gruber. (2002). The active site of hydroxynitrile lyase from Prunus amygdalus: Modeling studies provide new insights into the mechanism of cyanogenesis. Protein Science. 11(2). 292–300. 37 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026