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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:

A bacterial effector deubiquitinase specifically hydrolyses linear ubiquitin chains to inhibit host inflammatory signalling
Muyang Wan, Xiaofei Wang, Chunfeng Huang, et al.
Nature Microbiology (2019) Vol. 4, Iss. 8, pp. 1282-1293
Closed Access | Times Cited: 70

Showing 26-50 of 70 citing articles:

LUBAC-mediated linear ubiquitination: a crucial regulator of immune signaling
Kazuhiro Iwaï
Proceedings of the Japan Academy Series B (2021) Vol. 97, Iss. 3, pp. 120-133
Open Access | Times Cited: 25
Discovery of linear ubiquitination, a crucial regulator for immune signaling and cell death
Kazuhiro Iwaï
FEBS Journal (2020) Vol. 288, Iss. 4, pp. 1060-1069
Open Access | Times Cited: 24
An evolutionary approach to systematic discovery of novel deubiquitinases, applied to Legionella
Thomas Hermanns, Ilka Woiwode, Ricardo Guerreiro, et al.
Life Science Alliance (2020) Vol. 3, Iss. 9, pp. e202000838-e202000838
Open Access | Times Cited: 24
Bacteria make surgical strikes on host ubiquitin signaling
Tyler G. Franklin, Jonathan N. Pruneda
PLoS Pathogens (2021) Vol. 17, Iss. 3, pp. e1009341-e1009341
Open Access | Times Cited: 21
Concept about the Virulence Factor of Legionella
Jin-Lei Yang, Danyang Li, Xiao-Yong Zhan
Microorganisms (2022) Vol. 11, Iss. 1, pp. 74-74
Open Access | Times Cited: 14
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
Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination: Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase
Yasuhiro Fuseya, Kazuhiro Iwaï
Cells (2021) Vol. 10, Iss. 10, pp. 2706-2706
Open Access | Times Cited: 18
Legionella pneumophila-mediated host posttranslational modifications
Yi Yang, Ligang Mei, Jing Chen, et al.
Journal of Molecular Cell Biology (2023) Vol. 15, Iss. 5
Open Access | Times Cited: 7
Ovarian tumor domain proteases in pathogen infection
Dirk Schlüter, Eric Schulze, Matthias Stein, et al.
Trends in Microbiology (2021) Vol. 30, Iss. 1, pp. 22-33
Closed Access | Times Cited: 17
The subversion of toll-like receptor signaling by bacterial and viral proteases during the development of infectious diseases
Izabela Ciastoń, Ewelina Dobosz, Jan Potempa, et al.
Molecular Aspects of Medicine (2022) Vol. 88, pp. 101143-101143
Open Access | Times Cited: 12
Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs
Jiaxing Tan, Yan Xu, Xiaofei Wang, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 4, pp. 463-472
Closed Access | Times Cited: 6
Functional and structural diversity in deubiquitinases of the Chlamydia-like bacterium Simkania negevensis
Vanessa Boll, Thomas Hermanns, Matthias Uthoff, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 6
The emerging role and therapeutic implications of bacterial and parasitic deubiquitinating enzymes
Markus Wehrmann, David Vı́lchez
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 6
Structural insights into ubiquitin chain cleavage byLegionellaovarian tumor deubiquitinases
Sangwoo Kang, Gyuhee Kim, Minhyeong Choi, et al.
Life Science Alliance (2023) Vol. 6, Iss. 7, pp. e202201876-e202201876
Open Access | Times Cited: 5
Global atlas of predicted functional domains inLegionella pneumophilaDot/Icm translocated effectors
D. Patel, P.J. Stogios, Lukasz Jaroszewski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Enteroviral 3C protease cleaves N4BP1 to impair the host inflammatory response
Dongjie Zhang, Yifan Xie, Jie Cao, et al.
Journal of Virology (2024) Vol. 99, Iss. 1
Open Access | Times Cited: 1
Structures, functions, and inhibitors of LUBAC and its related diseases
Shuo Ning, Lingling Luo, Beiming Yu, et al.
Journal of Leukocyte Biology (2022) Vol. 112, Iss. 4, pp. 799-811
Closed Access | Times Cited: 7
Ubiquitin-regulating effector proteins from Legionella
Minwoo Jeong, Hayoung Jeon, Dong Hyuk Shin
BMB Reports (2022) Vol. 55, Iss. 7, pp. 316-322
Open Access | Times Cited: 7
Control of host PTMs by intracellular bacteria: An opportunity toward novel anti-infective agents
Virginie Stévenin, Jacques Neefjes
Cell chemical biology (2022) Vol. 29, Iss. 5, pp. 741-756
Open Access | Times Cited: 5
Genome‐wide genetic screen identifies host ubiquitination as important for Legionella pneumophila Dot/Icm effector translocation
Sze Ying Ong, Ralf Schuelein, Rachelia R. Wibawa, et al.
Cellular Microbiology (2021) Vol. 23, Iss. 10
Open Access | Times Cited: 7
Structural biology of the invasion arsenal of Gram‐negative bacterial pathogens
Andrey M. Grishin, Kevin Voth, Alla Gagarinova, et al.
FEBS Journal (2021) Vol. 289, Iss. 6, pp. 1385-1427
Open Access | Times Cited: 7
An evolutionary approach to systematic discovery of novel deubiquitinases, applied to Legionella
Thomas Hermanns, Ilka Woiwode, Ricardo F. M. Guerreiro, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 6
Structural insights into ubiquitin chain cleavage byLegionellaovarian tumor deubiquitinases
Sangwoo Kang, Gyuhee Kim, Minhyung Choi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Bacterial usurpation of the OTU deubiquitinase fold
Jonathan N. Pruneda, Justine Nguyen, Hiroki Nagai, et al.
FEBS Journal (2023) Vol. 291, Iss. 15, pp. 3303-3316
Open Access | Times Cited: 2
Legionella longbeachae Regulates the Association of Polyubiquitinated Proteins on Bacterial Phagosome with Multiple Deubiquitinases
Yunjia Shi, Hongtao Liu, Kelong Ma, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 2
Open Access | Times Cited: 2

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