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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:

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

Showing 1-25 of 185 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
Protein neddylation: beyond cullin–RING ligases
Radoslav I. Enchev, Brenda A. Schulman, Matthias Peter
Nature Reviews Molecular Cell Biology (2014) Vol. 16, Iss. 1, pp. 30-44
Open Access | Times Cited: 509
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
Advancing targeted protein degradation for cancer therapy
Brandon Dale, Meng Cheng, Kwang‐Su Park, et al.
Nature reviews. Cancer (2021) Vol. 21, Iss. 10, pp. 638-654
Open Access | Times Cited: 435
Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments
Jill J. Bouchard, Joel Otero, Daniel C. Scott, et al.
Molecular Cell (2018) Vol. 72, Iss. 1, pp. 19-36.e8
Open Access | Times Cited: 358
Keap1, the cysteine-based mammalian intracellular sensor for electrophiles and oxidants
Albena T. Dinkova‐Kostova, Rumen V. Kostov, Peter Canning
Archives of Biochemistry and Biophysics (2016) Vol. 617, pp. 84-93
Open Access | Times Cited: 274
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
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
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
Daniel C. Scott, David Y. Rhee, David M. Duda, et al.
Cell (2016) Vol. 166, Iss. 5, pp. 1198-1214.e24
Open Access | Times Cited: 202
Targeting Cullin–RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation
Emil Bulatov, Alessio Ciulli
Biochemical Journal (2015) Vol. 467, Iss. 3, pp. 365-386
Open Access | Times Cited: 199
Protein neddylation and its alterations in human cancers for targeted therapy
Lisha Zhou, Wenjuan Zhang, Yi Sun, et al.
Cellular Signalling (2018) Vol. 44, pp. 92-102
Open Access | Times Cited: 194
Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome
Simone Cavadini, Eric S. Fischer, R.D. Bunker, et al.
Nature (2016) Vol. 531, Iss. 7596, pp. 598-603
Closed Access | Times Cited: 193
Cullin-RING Ubiquitin Ligase Regulatory Circuits: A Quarter Century Beyond the F-Box Hypothesis
J. Wade Harper, Brenda A. Schulman
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 403-429
Open Access | Times Cited: 181
Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
Daniel Horn‐Ghetko, David T. Krist, J. Rajan Prabu, et al.
Nature (2021) Vol. 590, Iss. 7847, pp. 671-676
Open Access | Times Cited: 150
Development of a BCL-xL and BCL-2 dual degrader with improved anti-leukemic activity,
Dongwen Lv, Pratik Pal, Xingui Liu, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 108
Protein neddylation and its role in health and diseases
Shizhen Zhang, Qing Yu, Zhijian Li, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 36
Combination Therapy and Dual-Target Inhibitors Based on LSD1: New Emerging Tools in Cancer Therapy
Liang Shen, Bo Wang, ShaoPeng Wang, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 2, pp. 922-951
Closed Access | Times Cited: 17
Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting
Jerry Li, Nicholas Purser, Joanna Liwocha, et al.
Molecular Cell (2024) Vol. 84, Iss. 7, pp. 1304-1320.e16
Open Access | Times Cited: 17
Visualizing the complex functions and mechanisms of the anaphase promoting complex/cyclosome (APC/C)
Claudio Alfieri, Suyang Zhang, David Barford
Open Biology (2017) Vol. 7, Iss. 11, pp. 170204-170204
Open Access | Times Cited: 169
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C
Nicholas G. Brown, Ryan T. VanderLinden, Edmond R. Watson, et al.
Cell (2016) Vol. 165, Iss. 6, pp. 1440-1453
Open Access | Times Cited: 149
A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes
Monique P. C. Mulder, Katharina F. Witting, Ilana Berlin, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 7, pp. 523-530
Open Access | Times Cited: 142
Ubiquitylation, neddylation and the DNA damage response
Jessica Brown, Stephen P. Jackson
Open Biology (2015) Vol. 5, Iss. 4, pp. 150018-150018
Open Access | Times Cited: 130
Regulating the human HECT E3 ligases
Jasper D. Sluimer, Ben Distel
Cellular and Molecular Life Sciences (2018) Vol. 75, Iss. 17, pp. 3121-3141
Open Access | Times Cited: 130
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