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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:

Structural Insights into Non-canonical Ubiquitination Catalyzed by SidE
Yong Wang, Miao Shi, Han Feng, et al.
Cell (2018) Vol. 173, Iss. 5, pp. 1231-1243.e16
Open Access | Times Cited: 67

Showing 1-25 of 67 citing articles:

The role of ubiquitination in tumorigenesis and targeted drug discovery
Lu Deng, Tong Meng, Lei Chen, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 529
The protein complex crystallography beamline (BL19U1) at the Shanghai Synchrotron Radiation Facility
Weizhe Zhang, Jianchao Tang, Si-Sheng Wang, et al.
Nuclear Science and Techniques (2019) Vol. 30, Iss. 11
Closed Access | Times Cited: 167
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases
Miles H. Black, Adam Osinski, Marcin Gradowski, et al.
Science (2019) Vol. 364, Iss. 6442, pp. 787-792
Open Access | Times Cited: 134
Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB
Dong Hyuk Shin, Rukmini Mukherjee, Yaobin Liu, et al.
Molecular Cell (2019) Vol. 77, Iss. 1, pp. 164-179.e6
Open Access | Times Cited: 120
Deubiquitination of phosphoribosyl-ubiquitin conjugates by phosphodiesterase-domain–containingLegionellaeffectors
Min Wan, Alan Sulpizio, Anıl Aktürk, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 47, pp. 23518-23526
Open Access | Times Cited: 84
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
Amoebae as training grounds for microbial pathogens
Christopher T. D. Price, Hannah E. Hanford, Tasneem Al‐Quadan, et al.
mBio (2024) Vol. 15, Iss. 8
Open Access | Times Cited: 10
Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ
Alan Sulpizio, Marena E. Minelli, Min Wan, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 67
Ubiquitin‐targeted bacterial effectors: rule breakers of the ubiquitin system
Cameron G. Roberts, Tyler G. Franklin, Jonathan N. Pruneda
The EMBO Journal (2023) Vol. 42, Iss. 18
Open Access | Times Cited: 19
The role of ubiquitination in health and disease
Yan Liao, Wangzheqi Zhang, Yang Liu, et al.
MedComm (2024) Vol. 5, Iss. 10
Open Access | Times Cited: 7
Bacterial DUBs: deubiquitination beyond the seven classes
Thomas Hermanns, Kay Hofmann
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1857-1866
Closed Access | Times Cited: 45
Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27
The Sde phosphoribosyl–linked ubiquitin transferases protect the Legionella pneumophila vacuole from degradation by the host
Seongok Kim, Ralph R. Isberg
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 33
Open Access | Times Cited: 13
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
Yaobin Liu, Rukmini Mukherjee, Florian Bonn, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 10, pp. 2957-2969
Open Access | Times Cited: 29
HECW1 induces NCOA4-regulated ferroptosis in glioma through the ubiquitination and degradation of ZNF350
Yuancai Lin, Hailong Gong, Jinliang Liu, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 12
Open Access | Times Cited: 11
Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognition
Min Wan, Marena E. Minelli, Qiuye Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
The Legionella pneumophila Metaeffector Lpg2505 (MesI) Regulates SidI-Mediated Translation Inhibition and Novel Glycosyl Hydrolase Activity
Ashley M. Joseph, Adrienne E. Pohl, Theodore J. Ball, et al.
Infection and Immunity (2020) Vol. 88, Iss. 5
Open Access | Times Cited: 30
Members of the Legionella pneumophila Sde family target tyrosine residues for phosphoribosyl-linked ubiquitination
Mengyun Zhang, Joseph M. McEwen, Nicole M. Sjoblom, et al.
RSC Chemical Biology (2021) Vol. 2, Iss. 5, pp. 1509-1519
Open Access | Times Cited: 24
The roles of protein ubiquitination in tumorigenesis and targeted drug discovery in lung cancer
Zhen Ye, Jingru Yang, Hanming Jiang, et al.
Frontiers in Endocrinology (2023) Vol. 14
Open Access | Times Cited: 9
Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila
Leehyeon Kim, Do Hoon Kwon, Bong Heon Kim, et al.
Journal of Molecular Biology (2018) Vol. 430, Iss. 17, pp. 2843-2856
Closed Access | Times Cited: 28
Bacterial virulence mediated by orthogonal post-translational modification
Kaitlin A. Chambers, Rebecca A. Scheck
Nature Chemical Biology (2020) Vol. 16, Iss. 10, pp. 1043-1051
Closed Access | Times Cited: 27
Structural and mechanistic basis for protein glutamylation by the kinase fold
Adam Osinski, Miles H. Black, Krzysztof Pawłowski, et al.
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4527-4539.e8
Open Access | Times Cited: 23
Evolution and Adaptation of Legionella pneumophila to Manipulate the Ubiquitination Machinery of Its Amoebae and Mammalian Hosts
Christopher T. D. Price, Yousef Abu Kwaik
Biomolecules (2021) Vol. 11, Iss. 1, pp. 112-112
Open Access | Times Cited: 19
A Legionella effector ADP-ribosyltransferase inactivates glutamate dehydrogenase
Miles H. Black, Adam Osinski, Gina J. Park, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100301-100301
Open Access | Times Cited: 19
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