Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

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

Showing 26-50 of 81 citing articles:

Sde proteins coordinate ubiquitin utilization and phosphoribosylation to establish and maintain the Legionella replication vacuole
Kristin M. Kotewicz, Mengyun Zhang, Seongok Kim, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
The Legionella pneumophila Metaeffector Lpg2505 (MesI) Regulates SidI-Mediated Translation Inhibition and Novel Glycosyl Hydrolase Activity
Ashley M. Joseph, Adrienne E. Pohl, Theodore J. Ball, et al.
Infection and Immunity (2020) Vol. 88, Iss. 5
Open Access | Times Cited: 30
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
Members of the Legionella pneumophila Sde family target tyrosine residues for phosphoribosyl-linked ubiquitination
Mengyun Zhang, Joseph M. McEwen, Nicole M. Sjoblom, et al.
RSC Chemical Biology (2021) Vol. 2, Iss. 5, pp. 1509-1519
Open Access | Times Cited: 24
Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila
Leehyeon Kim, Do Hoon Kwon, Bong Heon Kim, et al.
Journal of Molecular Biology (2018) Vol. 430, Iss. 17, pp. 2843-2856
Closed Access | Times Cited: 28
Bacterial virulence mediated by orthogonal post-translational modification
Kaitlin A. Chambers, Rebecca A. Scheck
Nature Chemical Biology (2020) Vol. 16, Iss. 10, pp. 1043-1051
Closed Access | Times Cited: 27
Structural and mechanistic basis for protein glutamylation by the kinase fold
Adam Osinski, Miles H. Black, Krzysztof Pawłowski, et al.
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4527-4539.e8
Open Access | Times Cited: 23
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: 21
Ginsenoside Rh2 enhances immune surveillance of natural killer (NK) cells via inhibition of ERp5 in breast cancer
Chunmei Yang, Cheng Qian, Weiwei Zheng, et al.
Phytomedicine (2023) Vol. 123, pp. 155180-155180
Closed Access | Times Cited: 9
Upgraded SSRF BL19U2 beamline for small-angle X-ray scattering of biological macromolecules in solution
Guangfeng Liu, Yiwen Li, Hongjin Wu, et al.
Journal of Applied Crystallography (2018) Vol. 51, Iss. 6, pp. 1633-1640
Closed Access | Times Cited: 24
A Legionella effector ADP-ribosyltransferase inactivates glutamate dehydrogenase
Miles H. Black, Adam Osinski, Gina J. Park, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100301-100301
Open Access | Times Cited: 19
The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis
Shalini Iyer, Chittaranjan Das
Journal of Biological Chemistry (2021) Vol. 297, Iss. 6, pp. 101340-101340
Open Access | Times Cited: 19
Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC
Yajuan Mu, Yue Wang, Yanfei Huang, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 20
Capturing Legionella pneumophila effector enzymes using a ubiquitin derived photo-activatable probe
Max S. Kloet, Gerbrand J. van der Heden van Noort
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 2
Uncovering the Structural Basis of a New Twist in Protein Ubiquitination
Kedar Puvar, Zhao‐Qing Luo, Chittaranjan Das
Trends in Biochemical Sciences (2018) Vol. 44, Iss. 5, pp. 467-477
Open Access | Times Cited: 19
Interesting Biochemistries in the Structure and Function of Bacterial Effectors
Hazel Mak, Teresa L. M. Thurston
Frontiers in Cellular and Infection Microbiology (2021) Vol. 11
Open Access | Times Cited: 15
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
Insights into catalysis and regulation of non-canonical ubiquitination and deubiquitination by bacterial deamidase effectors
Yong Wang, Qi Zhang, Xinlu Wang, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 15
Structural basis for protein glutamylation by the Legionella pseudokinase SidJ
Michael Adams, Rahul Sharma, Thomas Colby, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 13
Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases
Toru Yoshida, Hideaki Tsuge
Toxins (2021) Vol. 13, Iss. 1, pp. 40-40
Open Access | Times Cited: 11
The Sde Phosphoribosyl-Linked Ubiquitin Transferases protect theLegionella pneumophilavacuole from degradation by the host
Seongok Kim, Ralph R. Isberg
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
Development of covalent probes to captureLegionella pneumophilaeffector enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
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
Legionella pneumophila evades host-autophagic clearance using phosphoribosyl-polyubiquitin chains
Minhyeong Choi, Minwoo Jeong, Sangwoo Kang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 1
Covalent Probes To Capture Legionella pneumophila Dup Effector Enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1

Scroll to top