
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:
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
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
Showing 26-50 of 39 citing articles:
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
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
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
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
Yunjia Shi, Hongtao Liu, Kelong Ma, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 2
Open Access | Times Cited: 2
Phosphoribosyl modification of poly-ubiquitin chains at the Legionella-containing vacuole prohibiting autophagy adaptor recognition
Yuxin Mao, Min Wan, Marena Minelli, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 2
Yuxin Mao, Min Wan, Marena Minelli, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 2
Global atlas of predicted functional domains in Legionella pneumophila Dot/Icm translocated effectors
D. Patel, P.J. Stogios, Lukasz Jaroszewski, et al.
Molecular Systems Biology (2024)
Closed Access
D. Patel, P.J. Stogios, Lukasz Jaroszewski, et al.
Molecular Systems Biology (2024)
Closed Access
Legionella pneumophila IrsA, a novel, iron-regulated exoprotein that facilitates growth in low-iron conditions and modulates biofilm formation
Alberto E. Lopez, Joshua Mayoral, Huaixin Zheng, et al.
Microbiology Spectrum (2024)
Open Access
Alberto E. Lopez, Joshua Mayoral, Huaixin Zheng, et al.
Microbiology Spectrum (2024)
Open Access
Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection
Dong Hyuk Shin, Anshu Bhattacharya, Yi-Lin Cheng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 3
Dong Hyuk Shin, Anshu Bhattacharya, Yi-Lin Cheng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 3
Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics onLegionellaphagosomes
Shuxin Liu, Jiwei Luo, Xiangkai Zhen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 1
Shuxin Liu, Jiwei Luo, Xiangkai Zhen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 1
Self-stabilization mechanism encoded by a bacterial toxin facilitates reproductive parasitism
Toshiyuki Harumoto
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Toshiyuki Harumoto
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Cocrystallization of ubiquitin–deubiquitinase complexes through disulfide linkage
Kristos I. Negrón Terón, Chittaranjan Das
Acta Crystallographica Section D Structural Biology (2023) Vol. 79, Iss. 11, pp. 1044-1055
Open Access
Kristos I. Negrón Terón, Chittaranjan Das
Acta Crystallographica Section D Structural Biology (2023) Vol. 79, Iss. 11, pp. 1044-1055
Open Access
Phylogenomics of Life Kingdom's Deubiquitinases
A. S. Evpak, Peter V. Evseev, Anna A. Kudriaeva, et al.
(2023), pp. 273-278
Closed Access
A. S. Evpak, Peter V. Evseev, Anna A. Kudriaeva, et al.
(2023), pp. 273-278
Closed Access