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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:

Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3
Hao Dou, Lori Buetow, Gary Sibbet, et al.
Nature Structural & Molecular Biology (2013) Vol. 20, Iss. 8, pp. 982-986
Open Access | Times Cited: 127

Showing 1-25 of 127 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
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Agne Kazlauskaite, Chandana Kondapalli, Robert Gourlay, et al.
Biochemical Journal (2014) Vol. 460, Iss. 1, pp. 127-141
Open Access | Times Cited: 754
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
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
Perilous journey: a tour of the ubiquitin–proteasome system
Gary Kleiger, Thibault Mayor
Trends in Cell Biology (2014) Vol. 24, Iss. 6, pp. 352-359
Open Access | Times Cited: 330
Human BRCA1–BARD1 ubiquitin ligase activity counteracts chromatin barriers to DNA resection
Ruth M. Densham, Alexander J. Garvin, Helen R Stone, et al.
Nature Structural & Molecular Biology (2016) Vol. 23, Iss. 7, pp. 647-655
Open Access | Times Cited: 269
RBR E3 ubiquitin ligases: new structures, new insights, new questions
Donald E. Spratt, Helen Walden, Gary S. Shaw
Biochemical Journal (2014) Vol. 458, Iss. 3, pp. 421-437
Open Access | Times Cited: 266
Atomic structure of the APC/C and its mechanism of protein ubiquitination
Leifu Chang, Ziguo Zhang, Jing Yang, et al.
Nature (2015) Vol. 522, Iss. 7557, pp. 450-454
Open Access | Times Cited: 231
Structural Diversity of Ubiquitin E3 Ligase
Sachiko Toma-Fukai, Toshiyuki Shimizu
Molecules (2021) Vol. 26, Iss. 21, pp. 6682-6682
Open Access | Times Cited: 105
Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8
Daniel C. Scott, Vladislav O. Sviderskiy, Julie K. Monda, et al.
Cell (2014) Vol. 157, Iss. 7, pp. 1671-1684
Open Access | Times Cited: 185
Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity
Marios G. Koliopoulos, Diego Esposito, Evangelos Christodoulou, et al.
The EMBO Journal (2016) Vol. 35, Iss. 11, pp. 1204-1218
Open Access | Times Cited: 158
Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways
Francesca Mattiroli, Titia K. Sixma
Nature Structural & Molecular Biology (2014) Vol. 21, Iss. 4, pp. 308-316
Closed Access | Times Cited: 154
Structural and Functional Insights to Ubiquitin-Like Protein Conjugation
Frederick C. Streich, Christopher D. Lima
Annual Review of Biophysics (2014) Vol. 43, Iss. 1, pp. 357-379
Open Access | Times Cited: 147
Structural insights into the TRIM family of ubiquitin E3 ligases
Yang Li, Han Wu, Wei Wu, et al.
Cell Research (2014) Vol. 24, Iss. 6, pp. 762-765
Open Access | Times Cited: 134
Structural determinants of TRIM protein function
Diego Esposito, Marios G. Koliopoulos, Katrin Rittinger
Biochemical Society Transactions (2017) Vol. 45, Iss. 1, pp. 183-191
Closed Access | Times Cited: 129
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
Ubiquitin enzymes in the regulation of immune responses
Petra Ebner, Gijs A. Versteeg, Fumiyo Ikeda
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 52, Iss. 4, pp. 425-460
Open Access | Times Cited: 123
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 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
Skp2 in the ubiquitin‐proteasome system: A comprehensive review
Moges Dessale Asmamaw, Ying Liu, Yi‐Chao Zheng, et al.
Medicinal Research Reviews (2020) Vol. 40, Iss. 5, pp. 1920-1949
Closed Access | Times Cited: 114
Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly
Nicholas G. Brown, Edmond R. Watson, Florian Weissmann, et al.
Molecular Cell (2014) Vol. 56, Iss. 2, pp. 246-260
Open Access | Times Cited: 113
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
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