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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:

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

Showing 1-25 of 84 citing articles:

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: 223
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
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: 37
Legionella effector LnaB is a phosphoryl-AMPylase that impairs phosphosignalling
Ting Wang, Xiaonan Song, Jiaxing Tan, et al.
Nature (2024) Vol. 631, Iss. 8020, pp. 393-401
Closed Access | Times Cited: 9
Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms
Jiaqi Fu, Siying Li, Hongxin Guan, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9
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
The Met1-linked ubiquitin machinery in inflammation and infection
Berthe Katrine Fiil, Mads Gyrd‐Hansen
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 557-569
Open Access | Times Cited: 52
Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes
Shuxin Liu, Jiwei Luo, Xiangkai Zhen, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 51
Role of phosphodiesterase 1 in the pathophysiology of diseases and potential therapeutic opportunities
Arun Samidurai, Lei Xi, Anindita Das, et al.
Pharmacology & Therapeutics (2021) Vol. 226, pp. 107858-107858
Open Access | Times Cited: 41
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: 31
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
Bacterial ubiquitin ligases hijack the host deubiquitinase OTUB1 to inhibit MTORC1 signaling and promote autophagy
Kelong Ma, Wei Xian, Hongtao Liu, et al.
Autophagy (2024) Vol. 20, Iss. 9, pp. 1968-1983
Closed 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
The Legionella Effector SdjA Is a Bifunctional Enzyme That Distinctly Regulates Phosphoribosyl Ubiquitination
Lei Song, Yongchao Xie, Chuang Li, et al.
mBio (2021) Vol. 12, Iss. 5
Open Access | Times Cited: 38
Ubiquitin and Legionella: From bench to bedside
Ines Tomašković, Alexis González, Ivan Đikić
Seminars in Cell and Developmental Biology (2022) Vol. 132, pp. 230-241
Open Access | Times Cited: 26
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
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
Mycobacterium tuberculosis protein kinase G acts as an unusual ubiquitinating enzyme to impair host immunity
Jing Wang, Pupu Ge, Zehui Lei, et al.
EMBO Reports (2021) Vol. 22, Iss. 6
Open Access | Times Cited: 31
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
Exploitation of the Host Ubiquitin System: Means by Legionella pneumophila
Jingjing Luo, Lidong Wang, Lei Song, et al.
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 27
Arginine ADP-Ribosylation: Chemical Synthesis of Post-Translationally Modified Ubiquitin Proteins
Jim Voorneveld, Max S. Kloet, Sven Wijngaarden, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 45, pp. 20582-20589
Open Access | Times Cited: 20
Phosphoribosyl-linked serine ubiquitination of USP14 by the SidE family effectors of Legionella excludes p62 from the bacterial phagosome
Jinli Ge, Ying Wang, Xindi Chen, et al.
Cell Reports (2023) Vol. 42, Iss. 8, pp. 112817-112817
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
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