Huib Ovaa

23.1k total citations · 3 hit papers
236 papers, 15.3k citations indexed

About

Huib Ovaa is a scholar working on Molecular Biology, Oncology and Immunology. According to data from OpenAlex, Huib Ovaa has authored 236 papers receiving a total of 15.3k indexed citations (citations by other indexed papers that have themselves been cited), including 207 papers in Molecular Biology, 94 papers in Oncology and 46 papers in Immunology. Recurrent topics in Huib Ovaa's work include Ubiquitin and proteasome pathways (148 papers), Peptidase Inhibition and Analysis (71 papers) and Protein Degradation and Inhibitors (43 papers). Huib Ovaa is often cited by papers focused on Ubiquitin and proteasome pathways (148 papers), Peptidase Inhibition and Analysis (71 papers) and Protein Degradation and Inhibitors (43 papers). Huib Ovaa collaborates with scholars based in Netherlands, United States and Germany. Huib Ovaa's co-authors include Hidde L. Ploegh, Celia R. Berkers, Jacques Neefjes, Farid El Oualid, Paul P. Geurink, Reggy Ekkebus, Benedikt M. Kessler, Titia K. Sixma, Boris Rodenko and David Komander and has published in prestigious journals such as Nature, Cell and Chemical Reviews.

In The Last Decade

Huib Ovaa

234 papers receiving 15.1k citations

Hit Papers

A novel orally active pro... 2005 2026 2012 2019 2005 2013 2018 100 200 300 400 500

Author Peers

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

Author Last Decade Papers Cites
Huib Ovaa 11.7k 4.4k 2.7k 1.9k 1.9k 236 15.3k
Jun O. Liu 8.9k 0.8× 2.7k 0.6× 1.5k 0.6× 1.3k 0.7× 1.4k 0.8× 210 14.2k
Ronen Marmorstein 12.8k 1.1× 3.8k 0.9× 969 0.4× 800 0.4× 1.6k 0.9× 205 16.1k
Tracy M. Handel 7.5k 0.6× 4.6k 1.1× 4.1k 1.5× 667 0.4× 1000 0.5× 163 13.4k
Laurence H. Pearl 18.0k 1.5× 2.5k 0.6× 2.1k 0.8× 1.1k 0.6× 897 0.5× 217 21.3k
Peter E. Czabotar 8.9k 0.8× 2.1k 0.5× 2.2k 0.8× 621 0.3× 1.2k 0.6× 98 11.8k
Patrick J. Casey 14.8k 1.3× 3.4k 0.8× 1.1k 0.4× 1.0k 0.5× 612 0.3× 247 19.3k
Ulf R. Rapp 18.9k 1.6× 5.1k 1.2× 3.7k 1.4× 657 0.3× 1.2k 0.6× 325 24.8k
Jane B. Trepel 11.8k 1.0× 4.4k 1.0× 2.2k 0.8× 439 0.2× 814 0.4× 290 17.6k
Daniel D. Billadeau 7.5k 0.6× 2.9k 0.7× 4.5k 1.7× 425 0.2× 918 0.5× 215 14.4k
Mark A. Lemmon 18.3k 1.6× 5.7k 1.3× 2.1k 0.8× 807 0.4× 860 0.5× 159 25.5k

Countries citing papers authored by Huib Ovaa

Since Specialization
Citations

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

Fields of papers citing papers by Huib Ovaa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Huib Ovaa

This figure shows the co-authorship network connecting the top 25 collaborators of Huib Ovaa. A scholar is included among the top collaborators of Huib Ovaa 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 Huib Ovaa. Huib Ovaa 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.
Zacarı́as, Natalia V. Ortiz, Sascha Röth, Bo‐Tao Xin, et al.. (2025). Leveraging Targeted Protein Degradation for G Protein-Coupled Receptors: The Development of CCR2 Molecular Degraders. Journal of Medicinal Chemistry. 68(24). 26525–26546.
2.
Jin, Gan, J. de Vries, Jimmy J.L.L. Akkermans, et al.. (2023). Cellular Validation of a Chemically Improved Inhibitor Identifies Monoubiquitination on OTUB2. ACS Chemical Biology. 18(9). 2003–2013. 5 indexed citations
3.
Xie, Feng, Xiaoxue Zhou, Heyu Li, et al.. (2022). USP8 promotes cancer progression and extracellular vesicle‐mediated CD8 + T cell exhaustion by deubiquitinating the TGF ‐β receptor TβRII. The EMBO Journal. 41(16). e108791–e108791. 54 indexed citations
4.
Horn‐Ghetko, Daniel, David T. Krist, J. Rajan Prabu, et al.. (2021). Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly. Nature. 590(7847). 671–676. 126 indexed citations
5.
Gangaev, Anastasia, Steven L. C. Ketelaars, Olga I. Isaeva, et al.. (2021). Identification and characterization of a SARS-CoV-2 specific CD8+ T cell response with immunodominant features. Nature Communications. 12(1). 2593–2593. 69 indexed citations
6.
Krist, David T., Gerbrand J. van der Heden van Noort, Fynn M. Hansen, et al.. (2020). Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler. Nature Chemical Biology. 17(3). 272–279. 32 indexed citations
7.
Shin, Dong Hyuk, Anshu Bhattacharya, Ahmad Reza Mehdipour, et al.. (2020). Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection. eLife. 9. 30 indexed citations
8.
Schubert, Alexander F., Paul P. Geurink, Cameron G. Roberts, et al.. (2020). Identification and characterization of diverse OTU deubiquitinases in bacteria. The EMBO Journal. 39(15). e105127–e105127. 43 indexed citations
9.
Sapmaz, Ayşegül, et al.. (2019). Development of a DUB-selective fluorogenic substrate. Chemical Science. 10(44). 10290–10296. 16 indexed citations
10.
Liu, Sijia, Román González‐Prieto, Mengdi Zhang, et al.. (2019). Deubiquitinase Activity Profiling Identifies UCHL1 as a Candidate Oncoprotein That Promotes TGFβ-Induced Breast Cancer Metastasis. Clinical Cancer Research. 26(6). 1460–1473. 106 indexed citations
11.
Vertegaal, Alfred C.O., et al.. (2019). Chemical Tools and Biochemical Assays for SUMO Specific Proteases (SENPs). ACS Chemical Biology. 14(11). 2389–2395. 19 indexed citations
12.
Narasimhan, Siddarth, Alessandra Lucini Paioni, Johan van der Zwan, et al.. (2019). DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells. Angewandte Chemie International Edition. 58(37). 12969–12973. 89 indexed citations
13.
Narasimhan, Siddarth, Alessandra Lucini Paioni, Johan van der Zwan, et al.. (2019). DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells. Angewandte Chemie. 131(37). 13103–13107. 22 indexed citations
14.
Hameed, Dharjath S., et al.. (2019). Development of Ubiquitin‐Based Probe for Metalloprotease Deubiquitinases. Angewandte Chemie International Edition. 58(41). 14477–14482. 17 indexed citations
15.
Teunisse, Amina F.A.S., et al.. (2018). Selective PKCδ Inhibitor B106 Elicits Uveal Melanoma Growth Inhibitory Effects Independent of Activated PKC Isoforms. ACS Chemical Biology. 14(1). 132–136. 4 indexed citations
16.
Kasteren, Sander I. van, Jacques Neefjes, & Huib Ovaa. (2018). Creating molecules that modulate immune responses. Nature Reviews Chemistry. 2(8). 184–193. 17 indexed citations
17.
Jong, Annemieke de, Katharina F. Witting, Raymond Kooij, Dennis Flierman, & Huib Ovaa. (2017). Release of Enzymatically Active Deubiquitinating Enzymes upon Reversible Capture by Disulfide Ubiquitin Reagents. Angewandte Chemie International Edition. 56(42). 12967–12970. 25 indexed citations
18.
Garstka, Malgorzata, Alexander Fish, Patrick H. N. Celie, et al.. (2015). The first step of peptide selection in antigen presentation by MHC class I molecules. Proceedings of the National Academy of Sciences. 112(5). 1505–1510. 66 indexed citations
19.
Basters, Anja, Paul P. Geurink, Farid El Oualid, et al.. (2014). Molecular characterization of ubiquitin‐specific protease 18 reveals substrate specificity for interferon‐stimulated gene 15. FEBS Journal. 281(7). 1918–1928. 43 indexed citations
20.
Schmidt‐Supprian, Marc, Jane Tian, Ethan Grant, et al.. (2004). Differential dependence of CD4 + CD25 + regulatory and natural killer-like T cells on signals leading to NF-κB activation. Proceedings of the National Academy of Sciences. 101(13). 4566–4571. 202 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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