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OpenAlex Citation Counts

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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:

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

Showing 1-25 of 99 citing articles:

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
SUMO conjugation – a mechanistic view
Andrea Pichler, Chronis Fatouros, Heekyoung Lee, et al.
BioMolecular Concepts (2017) Vol. 8, Iss. 1, pp. 13-36
Open Access | Times Cited: 226
Signalling mechanisms and cellular functions of SUMO
Alfred C.O. Vertegaal
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 11, pp. 715-731
Closed Access | Times Cited: 209
SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes
Xiaolan Zhao
Molecular Cell (2018) Vol. 71, Iss. 3, pp. 409-418
Open Access | Times Cited: 205
Genome-scale engineering of Saccharomyces cerevisiae with single-nucleotide precision
Zehua Bao, Mohammad HamediRad, Pu Xue, et al.
Nature Biotechnology (2018) Vol. 36, Iss. 6, pp. 505-508
Closed Access | Times Cited: 171
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 mechanisms of HECT-type ubiquitin ligases
Sonja Lorenz
Biological Chemistry (2017) Vol. 399, Iss. 2, pp. 127-145
Open Access | Times Cited: 120
Structural insights into Ubr1-mediated N-degron polyubiquitination
Man Pan, Qingyun Zheng, Tian Wang, et al.
Nature (2021) Vol. 600, Iss. 7888, pp. 334-338
Open Access | Times Cited: 94
BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1
Samuel R. Witus, Anika L. Burrell, Daniel P. Farrell, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 3, pp. 268-277
Open Access | Times Cited: 74
SUMO-SIM interactions: From structure to biological functions
Jara Lascorz, Joan Codina-Fabra, David Reverter, et al.
Seminars in Cell and Developmental Biology (2021) Vol. 132, pp. 193-202
Closed Access | Times Cited: 58
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
A eukaryotic-like ubiquitination system in bacterial antiviral defence
Lydia R. Chambers, Qiaozhen Ye, Jiaxi Cai, et al.
Nature (2024) Vol. 631, Iss. 8022, pp. 843-849
Closed Access | Times Cited: 9
Molecular mechanisms in SUMO conjugation
Nathalia Varejão, Jara Lascorz, Ying Li, et al.
Biochemical Society Transactions (2019) Vol. 48, Iss. 1, pp. 123-135
Closed Access | Times Cited: 70
Sumoylation in plants: mechanistic insights and its role in drought stress
Reyes Benlloch, L. María Lois
Journal of Experimental Botany (2018) Vol. 69, Iss. 19, pp. 4539-4554
Open Access | Times Cited: 64
Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility
Chongyang Li, Francis P. McManus, Cédric Plutoni, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 64
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
Structural basis for RING-Cys-Relay E3 ligase activity and its role in axon integrity
Peter D. Mabbitt, Andrea Loreto, Marc-André Déry, et al.
Nature Chemical Biology (2020) Vol. 16, Iss. 11, pp. 1227-1236
Open Access | Times Cited: 56
Integrative analysis reveals unique structural and functional features of the Smc5/6 complex
You Yu, Shibai Li, Zheng Ser, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 19
Open Access | Times Cited: 47
Decoding the messaging of the ubiquitin system using chemical and protein probes
Lukas T. Henneberg, Brenda A. Schulman
Cell chemical biology (2021) Vol. 28, Iss. 7, pp. 889-902
Open Access | Times Cited: 42
RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination
L. Kiss, Dean Clift, Nadine Renner, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 41
SUMO is a pervasive regulator of meiosis
Nikhil R. Bhagwat, Shannon Owens, Masaru Ito, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 41
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
Mechanistic insights into nucleosomal H2B monoubiquitylation mediated by yeast Bre1-Rad6 and its human homolog RNF20/RNF40-hRAD6A
Zhiheng Deng, Huasong Ai, Maoshen Sun, et al.
Molecular Cell (2023) Vol. 83, Iss. 17, pp. 3080-3094.e14
Open Access | Times Cited: 17
DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex
Nathalia Varejão, Eva Ibars, Jara Lascorz, et al.
The EMBO Journal (2018) Vol. 37, Iss. 12
Open Access | Times Cited: 48
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