Erin C. Dueber

4.0k total citations · 2 hit papers
20 papers, 2.2k citations indexed

About

Erin C. Dueber is a scholar working on Molecular Biology, Oncology and Immunology. According to data from OpenAlex, Erin C. Dueber has authored 20 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 5 papers in Oncology and 5 papers in Immunology. Recurrent topics in Erin C. Dueber's work include Ubiquitin and proteasome pathways (13 papers), Cancer-related Molecular Pathways (4 papers) and interferon and immune responses (3 papers). Erin C. Dueber is often cited by papers focused on Ubiquitin and proteasome pathways (13 papers), Cancer-related Molecular Pathways (4 papers) and interferon and immune responses (3 papers). Erin C. Dueber collaborates with scholars based in United States, France and Germany. Erin C. Dueber's co-authors include Elizabeth Helgason, Peter S. Liu, Alberto Estevez, Vishva M. Dixit, Nobuhiko Kayagaki, Claudio Ciferri, Qui Phung, Wayne J. Fairbrother, Anna Fedorova and Domagoj Vucic and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Erin C. Dueber

19 papers receiving 2.1k citations

Hit Papers

GsdmD p30 elicited by caspase-11 during pyroptosis forms ... 2016 2026 2019 2022 2016 2017 200 400 600

Peers

Erin C. Dueber
Tara L. Roberts Australia
John D. Lich United States
Anke Peters Germany
Alberto Estevez United States
Erin C. Dueber
Citations per year, relative to Erin C. Dueber Erin C. Dueber (= 1×) peers Christopher J. Farady

Countries citing papers authored by Erin C. Dueber

Since Specialization
Citations

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

Fields of papers citing papers by Erin C. Dueber

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Erin C. Dueber. 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 Erin C. Dueber. The network helps show where Erin C. Dueber may publish in the future.

Co-authorship network of co-authors of Erin C. Dueber

This figure shows the co-authorship network connecting the top 25 collaborators of Erin C. Dueber. A scholar is included among the top collaborators of Erin C. Dueber 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 Erin C. Dueber. Erin C. Dueber 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.
Miranda, Rafael de Souza, Shannon T. Smith, Mark Ultsch, et al.. (2025). Discovery and characterization of potent macrocycle inhibitors of ubiquitin-specific protease-7. Structure. 33(4). 705–717.e4.
2.
Peng, Lingling, Elizabeth Helgason, Rafael de Souza Miranda, et al.. (2024). N-tert-Butoxycarbonyl-N-(2-(tritylthio)ethoxy)glycine as a Building Block for Peptide Ubiquitination. Bioconjugate Chemistry. 35(2). 245–253. 1 indexed citations
3.
Schoeffler, Allyn J., Elizabeth Helgason, Nataliya Popovych, & Erin C. Dueber. (2021). Diagnosing and mitigating method-based avidity artifacts that confound polyubiquitin-binding assays. SHILAP Revista de lepidopterología. 1(2). 100033–100033. 2 indexed citations
4.
Besten, Willem den, Kshitij Verma, Sayumi Yamazoe, et al.. (2021). Primary Amine Tethered Small Molecules Promote the Degradation of X-Linked Inhibitor of Apoptosis Protein. Journal of the American Chemical Society. 143(28). 10571–10575. 10 indexed citations
5.
Bashore, Charlene, Priyadarshini Jaishankar, Nicholas J. Skelton, et al.. (2020). Cyanopyrrolidine Inhibitors of Ubiquitin Specific Protease 7 Mediate Desulfhydration of the Active-Site Cysteine. ACS Chemical Biology. 15(6). 1392–1400. 22 indexed citations
6.
Holliday, Michael, Axel Witt, Alejandro Rodríguez Gama, et al.. (2019). Structures of autoinhibited and polymerized forms of CARD9 reveal mechanisms of CARD9 and CARD11 activation. Nature Communications. 10(1). 26 indexed citations
7.
Holliday, Michael, Ryan Ferrao, Gladys de Leon Boenig, et al.. (2018). Picomolar zinc binding modulates formation of Bcl10-nucleating assemblies of the caspase recruitment domain (CARD) of CARD9. Journal of Biological Chemistry. 293(43). 16803–16817. 9 indexed citations
8.
Özen, Ayşegül, Lionel Rougé, Charlene Bashore, et al.. (2017). Selectively Modulating Conformational States of USP7 Catalytic Domain for Activation. Structure. 26(1). 72–84.e7. 21 indexed citations
9.
Dueber, Erin C., et al.. (2017). Recent Insights into the Molecular Mechanisms Underlying Pyroptosis and Gasdermin Family Functions. Trends in Immunology. 38(4). 261–271. 307 indexed citations breakdown →
10.
Estevez, Alberto, Peter S. Liu, Nobuhiko Kayagaki, et al.. (2016). GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes. Proceedings of the National Academy of Sciences. 113(28). 7858–7863. 717 indexed citations breakdown →
11.
Yin, Jianping, Allyn J. Schoeffler, Katherine E. Wickliffe, et al.. (2015). Structural Insights into WD-Repeat 48 Activation of Ubiquitin-Specific Protease 46. Structure. 23(11). 2043–2054. 62 indexed citations
12.
Phillips, Aaron H., Allyn J. Schoeffler, Tsutomu Matsui, et al.. (2014). Internal Motions Prime cIAP1 for Rapid Activation. Biophysical Journal. 106(2). 253a–253a. 1 indexed citations
13.
Phillips, Aaron H., Allyn J. Schoeffler, Tsutomu Matsui, et al.. (2014). Internal motions prime cIAP1 for rapid activation. Nature Structural & Molecular Biology. 21(12). 1068–1074. 18 indexed citations
14.
15.
Ma, Xiaolei, Elizabeth Helgason, Qui Phung, et al.. (2012). Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation. Proceedings of the National Academy of Sciences. 109(24). 9378–9383. 190 indexed citations
16.
Dong, Ken C., Elizabeth Helgason, Christine Yu, et al.. (2011). Preparation of Distinct Ubiquitin Chain Reagents of High Purity and Yield. Structure. 19(8). 1053–1063. 72 indexed citations
17.
Dueber, Erin C., Alessandro Costa, Jacob E. Corn, Stephen D. Bell, & James M. Berger. (2011). Molecular determinants of origin discrimination by Orc1 initiators in archaea. Nucleic Acids Research. 39(9). 3621–3631. 38 indexed citations
18.
Giannetti, Anthony M., Harvey Wong, Gerrit J.P. Dijkgraaf, et al.. (2011). Identification, Characterization, and Implications of Species-Dependent Plasma Protein Binding for the Oral Hedgehog Pathway Inhibitor Vismodegib (GDC-0449). Journal of Medicinal Chemistry. 54(8). 2592–2601. 60 indexed citations
19.
Dueber, Erin C., Allyn J. Schoeffler, Andreas Lingel, et al.. (2011). Antagonists Induce a Conformational Change in cIAP1 That Promotes Autoubiquitination. Science. 334(6054). 376–380. 169 indexed citations
20.
Dynek, Jasmin N., Tatiana Goncharov, Erin C. Dueber, et al.. (2010). c‐IAP1 and UbcH5 promote K11‐linked polyubiquitination of RIP1 in TNF signalling. The EMBO Journal. 29(24). 4198–4209. 288 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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