Wioletta Rut

1.9k total citations · 1 hit paper
32 papers, 1.3k citations indexed

About

Wioletta Rut is a scholar working on Molecular Biology, Oncology and Infectious Diseases. According to data from OpenAlex, Wioletta Rut has authored 32 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 12 papers in Oncology and 7 papers in Infectious Diseases. Recurrent topics in Wioletta Rut's work include Peptidase Inhibition and Analysis (11 papers), Ubiquitin and proteasome pathways (7 papers) and SARS-CoV-2 and COVID-19 Research (5 papers). Wioletta Rut is often cited by papers focused on Peptidase Inhibition and Analysis (11 papers), Ubiquitin and proteasome pathways (7 papers) and SARS-CoV-2 and COVID-19 Research (5 papers). Wioletta Rut collaborates with scholars based in Poland, United States and Germany. Wioletta Rut's co-authors include Marcin Drąg, Mikołaj Żmudziński, Marcin Poręba, Scott J. Snipas, Paulina Kasperkiewicz, Miklós Békés, Tony T. Huang, Shaun K. Olsen, Zongyang Lv and Katarzyna Groborz and has published in prestigious journals such as Chemical Reviews, Journal of the American Chemical Society and Nature Communications.

In The Last Decade

Wioletta Rut

31 papers receiving 1.3k citations

Hit Papers

Activity profiling and cr... 2020 2026 2022 2024 2020 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
Wioletta Rut Poland 20 632 485 348 229 211 32 1.3k
Francesco Saverio Di Leva Italy 28 1.0k 1.6× 306 0.6× 219 0.6× 445 1.9× 365 1.7× 67 1.8k
S. Betzi France 22 951 1.5× 238 0.5× 342 1.0× 215 0.9× 197 0.9× 38 1.5k
Simon Cocklin United States 28 942 1.5× 891 1.8× 132 0.4× 220 1.0× 394 1.9× 73 2.1k
René Coulombe Canada 19 768 1.2× 295 0.6× 102 0.3× 190 0.8× 252 1.2× 33 1.5k
Elena Arutyunova Canada 17 447 0.7× 390 0.8× 346 1.0× 110 0.5× 130 0.6× 30 1.0k
Scott E. Mottarella United States 7 1.2k 2.0× 198 0.4× 310 0.9× 156 0.7× 81 0.4× 9 1.7k
Tanggis Bohnuud United States 11 1.5k 2.4× 232 0.5× 373 1.1× 192 0.8× 88 0.4× 14 2.0k
Paul D. Kirchhoff United States 23 1.1k 1.7× 239 0.5× 367 1.1× 171 0.7× 257 1.2× 39 1.7k
Rose Ann Ferre United States 22 1.2k 1.9× 534 1.1× 285 0.8× 519 2.3× 451 2.1× 29 2.3k
Jinzhi Tan China 15 684 1.1× 376 0.8× 179 0.5× 105 0.5× 193 0.9× 25 1.1k

Countries citing papers authored by Wioletta Rut

Since Specialization
Citations

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

Fields of papers citing papers by Wioletta Rut

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Wioletta Rut

This figure shows the co-authorship network connecting the top 25 collaborators of Wioletta Rut. A scholar is included among the top collaborators of Wioletta Rut 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 Wioletta Rut. Wioletta Rut 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.
Rut, Wioletta, Ronald J. Holewinski, Kiall F. Suazo, et al.. (2025). Chemical tools to define and manipulate interferon-inducible Ubl protease USP18. Nature Communications. 16(1). 957–957.
2.
Snipas, Scott J., et al.. (2023). Differential specificity of SARS‐CoV ‐2 main protease variants on peptide versus protein‐based substrates. FEBS Journal. 291(1). 61–69. 1 indexed citations
3.
Żmudziński, Mikołaj, Wioletta Rut, Jarosław M. Granda, et al.. (2023). Ebselen derivatives inhibit SARS-CoV-2 replication by inhibition of its essential proteins: PLpro and Mpro proteases, and nsp14 guanine N7-methyltransferase. Scientific Reports. 13(1). 9161–9161. 25 indexed citations
4.
Rut, Wioletta, et al.. (2023). Mapping the substrate-binding subsite specificity of a Porphyromonas gingivalis Tpr peptidase. Acta Biochimica Polonica. 70(4). 963–968. 1 indexed citations
5.
Talma, Michał, Wioletta Rut, Mikołaj Żmudziński, et al.. (2022). Evaluation of the anti-SARS-CoV-2 properties of essential oils and aromatic extracts. Scientific Reports. 12(1). 14230–14230. 12 indexed citations
6.
Patchett, Stephanie, Zongyang Lv, Wioletta Rut, et al.. (2021). A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease. Cell Reports. 36(13). 109754–109754. 35 indexed citations
7.
Rut, Wioletta, Katarzyna Groborz, Linlin Zhang, et al.. (2020). SARS-CoV-2 Mpro inhibitors and activity-based probes for patient-sample imaging. Nature Chemical Biology. 17(2). 222–228. 212 indexed citations
8.
Poręba, Marcin, Katarzyna Groborz, Wioletta Rut, et al.. (2020). Multiplexed Probing of Proteolytic Enzymes Using Mass Cytometry-Compatible Activity-Based Probes. Journal of the American Chemical Society. 142(39). 16704–16715. 30 indexed citations
9.
Rut, Wioletta, Katarzyna Groborz, Linlin Zhang, et al.. (2020). Profiling of flaviviral NS2B-NS3 protease specificity provides a structural basis for the development of selective chemical tools that differentiate Dengue from Zika and West Nile viruses. Antiviral Research. 175. 104731–104731. 18 indexed citations
10.
Rut, Wioletta, et al.. (2019). Fluorescent activity-based probe for the selective detection of Factor VII activating protease (FSAP) in human plasma. Thrombosis Research. 182. 124–132. 9 indexed citations
11.
Poręba, Marcin, Wioletta Rut, Katarzyna Groborz, et al.. (2019). Potent and selective caspase-2 inhibitor prevents MDM-2 cleavage in reversine-treated colon cancer cells. Cell Death and Differentiation. 26(12). 2695–2709. 27 indexed citations
12.
Zdzalik, Michal, Radosław Kitel, A. Karim, et al.. (2018). Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus. Structure. 26(4). 572–579.e4. 25 indexed citations
14.
Poręba, Marcin, Wioletta Rut, Paulina Kasperkiewicz, et al.. (2017). Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families. Scientific Reports. 7(1). 43135–43135. 59 indexed citations
15.
Haugen, Mads H., Solveig Pettersen, Wioletta Rut, et al.. (2017). Glycosylation is important for legumain localization and processing to active forms but not for cystatin E/M inhibitory functions. Biochimie. 139. 27–37. 23 indexed citations
16.
Poręba, Marcin, Rigmor Solberg, Wioletta Rut, et al.. (2016). Counter Selection Substrate Library Strategy for Developing Specific Protease Substrates and Probes. Cell chemical biology. 23(8). 1023–1035. 45 indexed citations
17.
Rut, Wioletta, Linlin Zhang, Paulina Kasperkiewicz, et al.. (2016). Extended substrate specificity and first potent irreversible inhibitor/activity-based probe design for Zika virus NS2B-NS3 protease. Antiviral Research. 139. 88–94. 48 indexed citations
18.
Drinkwater, Nyssa, Rebecca S. Bamert, Wioletta Rut, et al.. (2016). Structure and substrate fingerprint of aminopeptidase P from Plasmodium falciparum. Biochemical Journal. 473(19). 3189–3204. 13 indexed citations
20.
Modak, Joyanta K., Wioletta Rut, Lakshmi C. Wijeyewickrema, et al.. (2015). Structural basis for substrate specificity of Helicobacter pylori M17 aminopeptidase. Biochimie. 121. 60–71. 21 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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