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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:

Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector
Anıl Aktürk, David J. Wasilko, Xiaochun Wu, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 729-733
Open Access | Times Cited: 87

Showing 1-25 of 87 citing articles:

Post-translational regulation of ubiquitin signaling
Lei Song, Zhao‐Qing Luo
The Journal of Cell Biology (2019) Vol. 218, Iss. 6, pp. 1776-1786
Open Access | Times Cited: 274
An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 225
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
Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination
Sissy Kalayil, Sagar Bhogaraju, Florian Bonn, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 734-738
Open Access | Times Cited: 105
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
A new dawn beyond lysine ubiquitination
Daniel R. Squair, Satpal Virdee
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 802-811
Closed Access | Times Cited: 60
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
The ubiquitin codes in cellular stress responses
Xiangpeng Sheng, Zhixiong Xia, Hanting Yang, et al.
Protein & Cell (2023) Vol. 15, Iss. 3, pp. 157-190
Open Access | Times Cited: 39
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: 12
Structural basis of ubiquitin modification by the Legionella effector SdeA
Yanan Dong, Yajuan Mu, Yongchao Xie, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 674-678
Closed Access | Times Cited: 81
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
ADP-ribosylation systems in bacteria and viruses
Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 2366-2383
Open Access | Times Cited: 48
To Ub or not to Ub: a regulatory question in TGF-β signaling
Jinquan Liu, Jianping Jin, Tingbo Liang, et al.
Trends in Biochemical Sciences (2022) Vol. 47, Iss. 12, pp. 1059-1072
Closed Access | Times Cited: 37
The Legionella pneumophila Dot/Icm type IV secretion system and its effectors
Daniel C. Lockwood, Himani Amin, Tiago R. D. Costa, et al.
Microbiology (2022) Vol. 168, Iss. 5
Open Access | Times Cited: 32
Ubiquitination of non-protein substrates
Jun-Ichi Sakamaki, Noboru Mizushima
Trends in Cell Biology (2023) Vol. 33, Iss. 11, pp. 991-1003
Open Access | Times Cited: 20
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
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
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: 6
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
Divergence of Legionella Effectors Reversing Conventional and Unconventional Ubiquitination
Tomoe Kitao, Hiroki Nagai, Tomoko Kubori
Frontiers in Cellular and Infection Microbiology (2020) Vol. 10
Open Access | Times Cited: 37
Legionella hijacks the host Golgi-to-ER retrograde pathway for the association of Legionella-containing vacuole with the ER
Mio Kawabata, Honoka Matsuo, Takumi Koito, et al.
PLoS Pathogens (2021) Vol. 17, Iss. 3, pp. e1009437-e1009437
Open Access | Times Cited: 32
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
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