Eric R. Strieter

3.3k total citations
46 papers, 2.7k citations indexed

About

Eric R. Strieter is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, Eric R. Strieter has authored 46 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 14 papers in Organic Chemistry and 9 papers in Oncology. Recurrent topics in Eric R. Strieter's work include Ubiquitin and proteasome pathways (27 papers), Glycosylation and Glycoproteins Research (11 papers) and Catalytic Cross-Coupling Reactions (8 papers). Eric R. Strieter is often cited by papers focused on Ubiquitin and proteasome pathways (27 papers), Glycosylation and Glycoproteins Research (11 papers) and Catalytic Cross-Coupling Reactions (8 papers). Eric R. Strieter collaborates with scholars based in United States, Germany and United Kingdom. Eric R. Strieter's co-authors include Stephen L. Buchwald, Donna G. Blackmond, Brijesh Bhayana, Kirandeep K. Deol, Ying Ge, Philipp Krattiger, Brett P. Fors, Jiale Du, Per Ryberg and Shashank Shekhar and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Eric R. Strieter

46 papers receiving 2.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eric R. Strieter United States 24 1.6k 1.3k 360 308 207 46 2.7k
Anthony G. Coyne United Kingdom 22 1.7k 1.1× 1.1k 0.8× 270 0.8× 98 0.3× 110 0.5× 62 2.7k
Christopher W. am Ende United States 27 1.7k 1.1× 1.3k 1.0× 224 0.6× 171 0.6× 79 0.4× 52 2.7k
Ming‐Sheng Xie China 38 3.4k 2.2× 1.1k 0.9× 649 1.8× 166 0.5× 107 0.5× 149 4.4k
Jie Luo China 33 1.8k 1.1× 1.8k 1.5× 586 1.6× 115 0.4× 229 1.1× 74 3.8k
Bruno Linclau United Kingdom 28 1.7k 1.1× 1.1k 0.9× 317 0.9× 106 0.3× 256 1.2× 128 2.6k
Neelakandha S. Mani United States 24 1.4k 0.9× 893 0.7× 191 0.5× 169 0.5× 110 0.5× 75 2.9k
James L. Gleason Canada 28 2.4k 1.5× 1.0k 0.8× 471 1.3× 135 0.4× 129 0.6× 79 3.1k
Mark C. Noe United States 28 2.0k 1.3× 973 0.8× 580 1.6× 170 0.6× 298 1.4× 45 2.7k
Soo Y. Ko South Korea 24 2.5k 1.6× 1.2k 0.9× 337 0.9× 115 0.4× 331 1.6× 54 3.2k
Leslie W. Deady Australia 26 1.3k 0.9× 691 0.5× 167 0.5× 272 0.9× 179 0.9× 109 2.3k

Countries citing papers authored by Eric R. Strieter

Since Specialization
Citations

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

Fields of papers citing papers by Eric R. Strieter

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eric R. Strieter. 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 Eric R. Strieter. The network helps show where Eric R. Strieter may publish in the future.

Co-authorship network of co-authors of Eric R. Strieter

This figure shows the co-authorship network connecting the top 25 collaborators of Eric R. Strieter. A scholar is included among the top collaborators of Eric R. Strieter 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 Eric R. Strieter. Eric R. Strieter 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.
Schafer, Johanna M., Marzena Dyba, Sergey G. Tarasov, et al.. (2025). Optimized isolation of enzymatically active ubiquitin E3 ligase E6AP/UBE3A from mammalian cells. Protein Expression and Purification. 228. 106661–106661. 1 indexed citations
2.
Sayers, Jessica, et al.. (2024). Facile Access to Branched Multispecific Proteins. Bioconjugate Chemistry. 35(7). 954–962. 1 indexed citations
3.
Strieter, Eric R., et al.. (2023). Uncovering DUB Selectivity through an Ion Mobility-Based Assessment of Ubiquitin Chain Isomers. Analytical Chemistry. 95(47). 17416–17423. 2 indexed citations
4.
Xu, Peng, Nathaniel L. Hepowit, Nicholas S. Diab, et al.. (2022). Ubiquitination drives COPI priming and Golgi SNARE localization. eLife. 11. 10 indexed citations
5.
Du, Jiale, Yanfeng Li, Kirandeep K. Deol, et al.. (2022). A cryptic K48 ubiquitin chain binding site on UCH37 is required for its role in proteasomal degradation. eLife. 11. 18 indexed citations
6.
Li, Yanfeng, et al.. (2022). A Strategy for Accessing Nanobody-Based Electrochemical Sensors for Analyte Detection in Complex Media. PubMed. 1(1). 10601–10601. 118 indexed citations
7.
Deol, Kirandeep K. & Eric R. Strieter. (2021). The ubiquitin proteoform problem. Current Opinion in Chemical Biology. 63. 95–104. 16 indexed citations
8.
Deol, Kirandeep K., et al.. (2020). Proteasome-Bound UCH37/UCHL5 Debranches Ubiquitin Chains to Promote Degradation. Molecular Cell. 80(5). 796–809.e9. 58 indexed citations
9.
Deol, Kirandeep K., Stephen J. Eyles, & Eric R. Strieter. (2020). Quantitative Middle-Down MS Analysis of Parkin-Mediated Ubiquitin Chain Assembly. Journal of the American Society for Mass Spectrometry. 31(5). 1132–1139. 17 indexed citations
10.
Deol, Kirandeep K., Sonja Lorenz, & Eric R. Strieter. (2019). Enzymatic Logic of Ubiquitin Chain Assembly. Frontiers in Physiology. 10. 835–835. 81 indexed citations
11.
Deol, Kirandeep K., et al.. (2019). Analysis of ubiquitin recognition by the HECT ligase E6AP provides insight into its linkage specificity. Journal of Biological Chemistry. 294(15). 6113–6129. 15 indexed citations
12.
Du, Jiale & Eric R. Strieter. (2018). A fluorescence polarization-based competition assay for measuring interactions between unlabeled ubiquitin chains and UCH37•RPN13. Analytical Biochemistry. 550. 84–89. 5 indexed citations
13.
Strieter, Eric R., et al.. (2015). Peeling away the layers of ubiquitin signaling complexities with synthetic ubiquitin–protein conjugates. Current Opinion in Chemical Biology. 28. 57–65. 20 indexed citations
14.
Rodgers, Margaret L., et al.. (2014). Chemoenzymatic Synthesis of Bifunctional Polyubiquitin Substrates for Monitoring Ubiquitin Chain Remodeling. ChemBioChem. 15(11). 1563–1568. 11 indexed citations
15.
Hebert, Alexander S., Anna E. Merrill, Derek J. Bailey, et al.. (2013). Neutron-encoded mass signatures for multiplexed proteome quantification. Nature Methods. 10(4). 332–334. 142 indexed citations
16.
Minami, Shoko, et al.. (2012). Nonenzymatic Polymerization of Ubiquitin: Single‐Step Synthesis and Isolation of Discrete Ubiquitin Oligomers. Angewandte Chemie International Edition. 51(52). 13085–13088. 59 indexed citations
17.
Koglin, Alexander, Frank Löhr, Frank Bernhard, et al.. (2008). Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature. 454(7206). 907–911. 108 indexed citations
18.
Strieter, Eric R. & Stephen L. Buchwald. (2006). Evidence for the Formation and Structure of Palladacycles during Pd‐Catalyzed CN Bond Formation with Catalysts Derived from Bulky Monophosphinobiaryl Ligands. Angewandte Chemie International Edition. 45(6). 925–928. 75 indexed citations
19.
Shekhar, Shashank, Per Ryberg, John F. Hartwig, et al.. (2006). Reevaluation of the Mechanism of the Amination of Aryl Halides Catalyzed by BINAP-Ligated Palladium Complexes. Journal of the American Chemical Society. 128(11). 3584–3591. 233 indexed citations
20.
Singh, Utpal, Eric R. Strieter, Donna G. Blackmond, & Stephen L. Buchwald. (2002). Mechanistic Insights into the Pd(BINAP)-Catalyzed Amination of Aryl Bromides:  Kinetic Studies under Synthetically Relevant Conditions. Journal of the American Chemical Society. 124(47). 14104–14114. 124 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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