Nicola Catone

464 total citations
12 papers, 373 citations indexed

About

Nicola Catone is a scholar working on Molecular Biology, Oncology and Epidemiology. According to data from OpenAlex, Nicola Catone has authored 12 papers receiving a total of 373 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 9 papers in Oncology and 3 papers in Epidemiology. Recurrent topics in Nicola Catone's work include Ubiquitin and proteasome pathways (10 papers), Peptidase Inhibition and Analysis (6 papers) and Autophagy in Disease and Therapy (3 papers). Nicola Catone is often cited by papers focused on Ubiquitin and proteasome pathways (10 papers), Peptidase Inhibition and Analysis (6 papers) and Autophagy in Disease and Therapy (3 papers). Nicola Catone collaborates with scholars based in Germany, Switzerland and United Kingdom. Nicola Catone's co-authors include Annette Aichem, Marcus Groettrup, Wiltrud Lederle, Norbert E. Fusenig, Alexandra Just, Sofia Depner, Margareta M. Mueller, Birte Kalveram, Terje Johansen and Carolin Sailer and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and PLoS ONE.

In The Last Decade

Nicola Catone

12 papers receiving 369 citations

Peers

Nicola Catone
Hugh Gannon United States
Anoosheh Ebaee United States
Mikhail Chernov United States
Saurav De United States
Hugh Gannon United States
Nicola Catone
Citations per year, relative to Nicola Catone Nicola Catone (= 1×) peers Hugh Gannon

Countries citing papers authored by Nicola Catone

Since Specialization
Citations

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

Fields of papers citing papers by Nicola Catone

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Nicola Catone

This figure shows the co-authorship network connecting the top 25 collaborators of Nicola Catone. A scholar is included among the top collaborators of Nicola Catone 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 Nicola Catone. Nicola Catone is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

12 of 12 papers shown
1.
Catone, Nicola, et al.. (2023). Tumor necrosis factor mediates USE1-independent FAT10ylation under inflammatory conditions. Life Science Alliance. 6(11). e202301985–e202301985. 4 indexed citations
2.
Catone, Nicola, et al.. (2023). FAT10 and NUB1L cooperate to activate the 26S proteasome. Life Science Alliance. 6(8). e202201463–e202201463. 5 indexed citations
3.
Mueller, Stefanie, et al.. (2023). The ubiquitin-like modifier FAT10 covalently modifies HUWE1 and strengthens the interaction of AMBRA1 and HUWE1. PLoS ONE. 18(8). e0290002–e0290002. 3 indexed citations
4.
Sailer, Carolin, et al.. (2021). Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy. Cell Reports. 34(11). 108857–108857. 32 indexed citations
5.
Catone, Nicola, et al.. (2020). The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation. Journal of Biological Chemistry. 295(42). 14402–14418. 8 indexed citations
6.
Aichem, Annette, et al.. (2019). Analysis of modification and proteolytic targeting by the ubiquitin-like modifier FAT10. Methods in enzymology on CD-ROM/Methods in enzymology. 618. 229–256. 11 indexed citations
7.
Catone, Nicola, et al.. (2019). The ubiquitin-like modifier FAT10 stimulates the activity of deubiquitylating enzyme OTUB1. Journal of Biological Chemistry. 294(12). 4315–4330. 24 indexed citations
8.
Aichem, Annette, Carolin Sailer, Nicola Catone, et al.. (2019). The ubiquitin-like modifier FAT10 interferes with SUMO activation. Nature Communications. 10(1). 4452–4452. 30 indexed citations
9.
Aichem, Annette, Nicola Catone, Andrej Berg, et al.. (2018). The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation. Nature Communications. 9(1). 3321–3321. 37 indexed citations
10.
Aichem, Annette, Nicola Catone, & Marcus Groettrup. (2014). Investigations into the auto‐FAT10ylation of the bispecific E2 conjugating enzyme UBA6‐specific E2 enzyme 1. FEBS Journal. 281(7). 1848–1859. 28 indexed citations
11.
Aichem, Annette, et al.. (2012). The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation. Journal of Cell Science. 125(Pt 19). 4576–85. 77 indexed citations
12.
Lederle, Wiltrud, Sofia Depner, Nicola Catone, et al.. (2010). IL‐6 promotes malignant growth of skin SCCs by regulating a network of autocrine and paracrine cytokines. International Journal of Cancer. 128(12). 2803–2814. 114 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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