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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:

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

Showing 1-25 of 134 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: 225
Discovery of Deactivation Phenomenon in NiCo2S4/NiS2 Electromagnetic Wave Absorbent and Its Reactivation Mechanism
Hongsheng Liang, Shengchong Hui, Geng Chen, et al.
Small Methods (2024)
Closed Access | Times Cited: 24
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
Inhibition of bacterial ubiquitin ligases by SidJ–calmodulin catalysed glutamylation
Sagar Bhogaraju, Florian Bonn, Rukmini Mukherjee, et al.
Nature (2019) Vol. 572, Iss. 7769, pp. 382-386
Open Access | Times Cited: 117
Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase
Ninghai Gan, Xiangkai Zhen, Yao Liu, et al.
Nature (2019) Vol. 572, Iss. 7769, pp. 387-391
Open Access | Times Cited: 112
Emerging concepts in pseudoenzyme classification, evolution, and signaling
António J. M. Ribeiro, Sayoni Das, Natalie L. Dawson, et al.
Science Signaling (2019) Vol. 12, Iss. 594
Closed Access | Times Cited: 88
Pathogenicity and Virulence ofLegionella: Intracellular replication and host response
Deepika Chauhan, Stephanie R. Shames
Virulence (2021) Vol. 12, Iss. 1, pp. 1122-1144
Open Access | Times Cited: 87
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
There’s more to death than life: Noncatalytic functions in kinase and pseudokinase signaling
Peter D. Mace, James M. Murphy
Journal of Biological Chemistry (2021) Vol. 296, pp. 100705-100705
Open Access | Times Cited: 83
Small proline-rich protein 2A is a gut bactericidal protein deployed during helminth infection
Zehan Hu, Chenlu Zhang, Luis Sifuentes-Dominguez, et al.
Science (2021) Vol. 374, Iss. 6568
Open Access | Times Cited: 71
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
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
Molecular Mimicry: a Paradigm of Host-Microbe Coevolution Illustrated by Legionella
Sonia Mondino, Silke Schmidt, Carmen Buchrieser
mBio (2020) Vol. 11, Iss. 5
Open Access | Times Cited: 66
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
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
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
Exaptation of Inactivated Host Enzymes for Structural Roles in Orthopoxviruses and Novel Folds of Virus Proteins Revealed by Protein Structure Modeling
Pascal Mutz, Wolfgang Resch, Guilhem Faure, et al.
mBio (2023) Vol. 14, Iss. 2
Open Access | Times Cited: 21
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
Legionella pneumophila regulates the activity of UBE 2N by deamidase‐mediated deubiquitination
Ninghai Gan, Hongxin Guan, Yini Huang, et al.
The EMBO Journal (2019) Vol. 39, Iss. 4
Open Access | Times Cited: 51
Cataloguing the dead: breathing new life into pseudokinase research
Safal Shrestha, Dominic P. Byrne, John A. Harris, et al.
FEBS Journal (2020) Vol. 287, Iss. 19, pp. 4150-4169
Open Access | Times Cited: 48
The dead phosphatases society: a review of the emerging roles of pseudophosphatases
Veronika Reiterer, Krzysztof Pawłowski, Guillaume Desrochers, et al.
FEBS Journal (2020) Vol. 287, Iss. 19, pp. 4198-4220
Open Access | Times Cited: 40
Bacterial OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
Dong Hyuk Shin, Anshu Bhattacharya, Yi-Lin Cheng, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 40
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