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:

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

Showing 24 citing articles:

A new dawn beyond lysine ubiquitination
Daniel R. Squair, Satpal Virdee
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 802-811
Closed Access | Times Cited: 60
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
The emerging roles of non-canonical ubiquitination in proteostasis and beyond
Yoshino Akizuki, Stephanie Kaypee, Fumiaki Ohtake, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 5
Open Access | Times Cited: 10
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
Ubiquitination of non-protein substrates
Jun-Ichi Sakamaki, Noboru Mizushima
Trends in Cell Biology (2023) Vol. 33, Iss. 11, pp. 991-1003
Open Access | Times Cited: 20
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
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
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
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
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
Yeast Display Enables Identification of Covalent Single-Domain Antibodies against Botulinum Neurotoxin Light Chain A
Rafael Alcala‐Torano, Mariha Islam, Jaclyn Cika, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 12, pp. 3435-3449
Open Access | Times Cited: 11
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 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
New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts
A. Maxwell Burroughs, L. Aravind
NAR Genomics and Bioinformatics (2023) Vol. 5, Iss. 1
Open Access | Times Cited: 5
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
Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, aLegionella pneumophilaprotein that impinges on a stress response pathway
Dar Hershkovitz, Emy J. Chen, Alexander W. Ensminger, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Decoding the ubiquitin landscape by cutting-edge ubiquitinomic approaches
P T Brindhavanam, Indrajit Sahu
Biochemical Society Transactions (2024) Vol. 52, Iss. 2, pp. 627-637
Closed Access | Times Cited: 1
Mechanism and Modulation of SidE Family Proteins in the Pathogenesis of Legionella pneumophila
Yongchao Xie, Yi Zhang, Yong Wang, et al.
Pathogens (2023) Vol. 12, Iss. 4, pp. 629-629
Open Access | Times Cited: 2
Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, a Legionella pneumophila protein that impinges on a stress response pathway
Dar Hershkovitz, Emy J. Chen, Alexander W. Ensminger, et al.
mSphere (2024) Vol. 9, Iss. 9
Open Access
Insights into mechanisms of ubiquitin ADP-ribosylation reversal
Zhengrui Zhang, Chittaranjan Das
Biochemical Society Transactions (2024)
Closed Access
The Sde phosphoribosyl-linked ubiquitin transferases exploit reticulons to protect the integrity of theLegionella-containing vacuole
Mengyun Zhang, Seongok Kim, Ralph R. Isberg
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Sde Proteins Coordinate Ubiquitin Utilization and Phosphoribosylation to Promote Establishment and Maintenance of the Legionella Replication Vacuole
Ralph R. Isberg, Kristin M. Kotewicz, Mengyun Zheng, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 1
Sde Proteins Coordinate Ubiquitin Utilization and Phosphoribosylation to Establish and Maintain theLegionellaReplication Vacuole
Kristin M. Kotewicz, Mengyun Zhang, Seongok Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Page 1

Scroll to top