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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Activation of a Primed RING E3-E2–Ubiquitin Complex by Non-Covalent Ubiquitin
Lori Buetow, Mads Gabrielsen, Nahoum G. Anthony, et al.
Molecular Cell (2015) Vol. 58, Iss. 2, pp. 297-310
Closed Access | Times Cited: 123

Showing 1-25 of 123 citing articles:

Ubiquitin Ligases: Structure, Function, and Regulation
Ning Zheng, Nitzan Shabek
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 129-157
Closed Access | Times Cited: 1207
Structural insights into the catalysis and regulation of E3 ubiquitin ligases
Lori Buetow, Danny T. Huang
Nature Reviews Molecular Cell Biology (2016) Vol. 17, Iss. 10, pp. 626-642
Open Access | Times Cited: 531
E2 enzymes: more than just middle men
Mikaela D. Stewart, Tobias Ritterhoff, Rachel E. Klevit, et al.
Cell Research (2016) Vol. 26, Iss. 4, pp. 423-440
Open Access | Times Cited: 486
Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism
Laurent Cappadocia, Christopher D. Lima
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 889-918
Open Access | Times Cited: 468
NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly
Kheewoong Baek, David T. Krist, J. Rajan Prabu, et al.
Nature (2020) Vol. 578, Iss. 7795, pp. 461-466
Open Access | Times Cited: 229
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Kheewoong Baek, Daniel C. Scott, Brenda A. Schulman
Current Opinion in Structural Biology (2020) Vol. 67, pp. 101-109
Open Access | Times Cited: 122
Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase
Laurent Cappadocia, Andrea Pichler, Christopher D. Lima
Nature Structural & Molecular Biology (2015) Vol. 22, Iss. 12, pp. 968-975
Open Access | Times Cited: 119
BMI1–RING1B is an autoinhibited RING E3 ubiquitin ligase
Asad M. Taherbhoy, Oscar W. Huang, Andrea G. Cochran
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 114
Capturing a substrate in an activated RING E3/E2–SUMO complex
Frederick C. Streich, Christopher D. Lima
Nature (2016) Vol. 536, Iss. 7616, pp. 304-308
Open Access | Times Cited: 99
Enzymatic Logic of Ubiquitin Chain Assembly
Kirandeep K. Deol, Sonja Lorenz, Eric R. Strieter
Frontiers in Physiology (2019) Vol. 10
Open Access | Times Cited: 98
Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases
Chatrin Chatrin, Mads Gabrielsen, Lori Buetow, et al.
Science Advances (2020) Vol. 6, Iss. 38
Open Access | Times Cited: 77
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Kang Zhu, Marcin J. Suskiewicz, Andrea Hloušek-Kasun, et al.
Science Advances (2022) Vol. 8, Iss. 40
Open Access | Times Cited: 67
A non‐canonical scaffold‐type E3 ligase complex mediates protein UFMylation
Joshua Peter, H Magnussen, Paul A. DaRosa, et al.
The EMBO Journal (2022) Vol. 41, Iss. 21
Open Access | Times Cited: 50
UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4
Lucy Barnsby-Greer, Peter D. Mabbitt, Marc-André Déry, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 351-363
Open Access | Times Cited: 13
Mechanisms of RNF168 nucleosome recognition and ubiquitylation
Qi Hu, Debiao Zhao, Gaofeng Cui, et al.
Molecular Cell (2024) Vol. 84, Iss. 5, pp. 839-853.e12
Open Access | Times Cited: 11
Critical Role of the UBL Domain in Stimulating the E3 Ubiquitin Ligase Activity of UHRF1 toward Chromatin
Benjamin M. Foster, Paul Stolz, Christopher B. Mulholland, et al.
Molecular Cell (2018) Vol. 72, Iss. 4, pp. 739-752.e9
Open Access | Times Cited: 82
Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3
Arno F. Alpi, Viduth K. Chaugule, Helen Walden
Biochemical Journal (2016) Vol. 473, Iss. 20, pp. 3401-3419
Open Access | Times Cited: 73
A Bifunctional Role for the UHRF1 UBL Domain in the Control of Hemi-methylated DNA-Dependent Histone Ubiquitylation
Paul A. DaRosa, Joseph S. Harrison, Alex Zelter, et al.
Molecular Cell (2018) Vol. 72, Iss. 4, pp. 753-765.e6
Open Access | Times Cited: 72
A General Strategy for Discovery of Inhibitors and Activators of RING and U-box E3 Ligases with Ubiquitin Variants
Mads Gabrielsen, Lori Buetow, Mark A. Nakasone, et al.
Molecular Cell (2017) Vol. 68, Iss. 2, pp. 456-470.e10
Open Access | Times Cited: 69
A conformational switch regulates the ubiquitin ligase HUWE1
Bodo Sander, Wenshan Xu, Martin Eilers, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 67
Structural basis of generic versus specific E2–RING E3 interactions in protein ubiquitination
Mehmet Gundogdu, Helen Walden
Protein Science (2019) Vol. 28, Iss. 10, pp. 1758-1770
Open Access | Times Cited: 58
Ubiquitination in the ERAD Process
Anna Lopata, Andreas Kniss, Frank Löhr, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 15, pp. 5369-5369
Open Access | Times Cited: 58
Structure of UBE2K–Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension
Mark A. Nakasone, K.A. Majorek, Mads Gabrielsen, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 4, pp. 422-431
Open Access | Times Cited: 33
Acetylation, Phosphorylation, Ubiquitination (Oh My!): Following Post-Translational Modifications on the Ubiquitin Road
Rachel E. Lacoursiere, Dania Hadi, Gary S. Shaw
Biomolecules (2022) Vol. 12, Iss. 3, pp. 467-467
Open Access | Times Cited: 33
Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity
Koji Nomura, Marta Klejnot, Dominika Kowalczyk, et al.
Nature Structural & Molecular Biology (2017) Vol. 24, Iss. 7, pp. 578-587
Open Access | Times Cited: 59
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