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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: 52

Showing 1-25 of 52 citing articles:

Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains
Lining Lu, Xiaoguo Zhai, Xiaolong Li, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 64
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
Threonine ADP-Ribosylation of Ubiquitin by a Bacterial Effector Family Blocks Host Ubiquitination
Fujie Yan, Chunfeng Huang, Xiaofei Wang, et al.
Molecular Cell (2020) Vol. 78, Iss. 4, pp. 641-652.e9
Open Access | Times Cited: 64
Identification and characterization of diverse OTU deubiquitinases in bacteria
Alexander F. Schubert, Justine Nguyen, Tyler G. Franklin, et al.
The EMBO Journal (2020) Vol. 39, Iss. 15
Open Access | Times Cited: 63
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
The Ubiquitination System within Bacterial Host–Pathogen Interactions
Vera Vozandychova, Pavla Stojková, Kamil Hercík, et al.
Microorganisms (2021) Vol. 9, Iss. 3, pp. 638-638
Open Access | Times Cited: 44
Met1-linked ubiquitin signalling in health and disease: inflammation, immunity, cancer, and beyond
Akhee Sabiha Jahan, Camilla Reiter Elbæk, Rune Busk Damgaard
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 473-492
Open Access | Times Cited: 43
Identification and classification of papain-like cysteine proteinases
Fatih Ozhelvaci, Kamil Steczkiewicz
Journal of Biological Chemistry (2023) Vol. 299, Iss. 6, pp. 104801-104801
Open Access | Times Cited: 19
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
Altered Metabolism and Inflammation Driven by Post-translational Modifications in Intervertebral Disc Degeneration
Dingchao Zhu, Huaizhen Liang, Cheng‐Feng Du, et al.
Research (2024) Vol. 7
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
The ubiquitin ligation machinery in the defense against bacterial pathogens
Ishita Tripathi‐Giesgen, Christian Behrends, Arno F. Alpi
EMBO Reports (2021) Vol. 22, Iss. 11
Open Access | Times Cited: 40
Legionella pneumophila regulates host cell motility by targeting Phldb2 with a 14-3-3ζ-dependent protease effector
Lei Song, Jingjing Luo, Hongou Wang, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 25
Viewing Legionella pneumophila Pathogenesis through an Immunological Lens
Xin Liu, Sunny Shin
Journal of Molecular Biology (2019) Vol. 431, Iss. 21, pp. 4321-4344
Open Access | Times Cited: 41
The bacterial deubiquitinase Ceg23 regulates the association of Lys-63–linked polyubiquitin molecules on the Legionella phagosome
Kelong Ma, Xiangkai Zhen, Biao Zhou, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 6, pp. 1646-1657
Open Access | Times Cited: 39
The Functional Deubiquitinating Enzymes in Control of Innate Antiviral Immunity
Zhi Zong, Zhengkui Zhang, Liming Wu, et al.
Advanced Science (2020) Vol. 8, Iss. 2
Open Access | Times Cited: 38
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
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
Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
Molecular Cell (2022) Vol. 83, Iss. 1, pp. 105-120.e5
Open Access | Times Cited: 19
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
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
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