
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:
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
Yaobin Liu, Rukmini Mukherjee, Florian Bonn, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 10, pp. 2957-2969
Open Access | Times Cited: 29
Yaobin Liu, Rukmini Mukherjee, Florian Bonn, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 10, pp. 2957-2969
Open Access | Times Cited: 29
Showing 1-25 of 29 citing articles:
An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 223
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 223
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
Regulation of Host-Pathogen Interactions via the Ubiquitin System
Rukmini Mukherjee, Ivan Đikić
Annual Review of Microbiology (2022) Vol. 76, Iss. 1, pp. 211-233
Open Access | Times Cited: 32
Rukmini Mukherjee, Ivan Đikić
Annual Review of Microbiology (2022) Vol. 76, Iss. 1, pp. 211-233
Open Access | Times Cited: 32
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
Daniel C. Lockwood, Himani Amin, Tiago R. D. Costa, et al.
Microbiology (2022) Vol. 168, Iss. 5
Open Access | Times Cited: 31
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
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
Seongok Kim, Ralph R. Isberg
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 33
Open Access | Times Cited: 13
Arginine ADP-Ribosylation: Chemical Synthesis of Post-Translationally Modified Ubiquitin Proteins
Jim Voorneveld, Max S. Kloet, Sven Wijngaarden, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 45, pp. 20582-20589
Open Access | Times Cited: 20
Jim Voorneveld, Max S. Kloet, Sven Wijngaarden, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 45, pp. 20582-20589
Open Access | Times Cited: 20
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
Jinli Ge, Ying Wang, Xindi Chen, et al.
Cell Reports (2023) Vol. 42, Iss. 8, pp. 112817-112817
Open Access | Times Cited: 11
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
Kristin M. Kotewicz, Mengyun Zhang, Seongok Kim, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Comparison of Phosphoribosyl Ubiquitin Probes Targeting Legionella Dup Enzymes
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Bioconjugate Chemistry (2025)
Closed Access
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Bioconjugate Chemistry (2025)
Closed Access
Deciphering non-canonical ubiquitin signaling: biology and methodology
Nila van Overbeek, Tim Aguirre, Gerbrand J. van der Heden van Noort, et al.
Frontiers in Molecular Biosciences (2024) Vol. 10
Open Access | Times Cited: 2
Nila van Overbeek, Tim Aguirre, Gerbrand J. van der Heden van Noort, et al.
Frontiers in Molecular Biosciences (2024) Vol. 10
Open Access | Times Cited: 2
Ceramide-1-phosphate is a regulator of Golgi structure and is co-opted by the obligate intracellular bacterial pathogen Anaplasma phagocytophilum
Curtis B. Read, Anika N. Ali, Daniel Stephenson, et al.
mBio (2024) Vol. 15, Iss. 4
Open Access | Times Cited: 2
Curtis B. Read, Anika N. Ali, Daniel Stephenson, et al.
mBio (2024) Vol. 15, Iss. 4
Open Access | Times Cited: 2
The DarT/DarG Toxin–Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies
Giuliana Catara, Rocco Caggiano, Luca Palazzo
Pathogens (2023) Vol. 12, Iss. 2, pp. 240-240
Open Access | Times Cited: 6
Giuliana Catara, Rocco Caggiano, Luca Palazzo
Pathogens (2023) Vol. 12, Iss. 2, pp. 240-240
Open Access | Times Cited: 6
Ubiquitin-mediated degradation at the Golgi apparatus
Lana Buzuk, Doris Hellerschmied
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 6
Lana Buzuk, Doris Hellerschmied
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 6
Atypical Legionella GTPase effector hijacks host vesicular transport factor p115 to regulate host lipid droplet
Tao-Tao Chen, Yanling Lin, Shijun Zhang, et al.
Science Advances (2022) Vol. 8, Iss. 50
Open Access | Times Cited: 8
Tao-Tao Chen, Yanling Lin, Shijun Zhang, et al.
Science Advances (2022) Vol. 8, Iss. 50
Open Access | Times Cited: 8
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
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
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
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
Max S. Kloet, Rishov Mukhopadhyay, Rukmini Mukherjee, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1
Serine ubiquitination of SQSTM1 regulates NFE2L2-dependent redox homeostasis
Rukmini Mukherjee, Anshu Bhattacharya, João Mello-Vieira, et al.
Autophagy (2024)
Closed Access | Times Cited: 1
Rukmini Mukherjee, Anshu Bhattacharya, João Mello-Vieira, et al.
Autophagy (2024)
Closed Access | Times Cited: 1
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
Minwoo Jeong, Hayoung Jeon, Dong Hyuk Shin
BMB Reports (2022) Vol. 55, Iss. 7, pp. 316-322
Open Access | Times Cited: 7
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
Yongchao Xie, Yi Zhang, Yong Wang, et al.
Pathogens (2023) Vol. 12, Iss. 4, pp. 629-629
Open Access | Times Cited: 2
Transcriptomic Defense Mechanism of Japanese Eel (Anguilla Japonica) Against Edwardsiella Anguillarum Infection after Bath Immunization with Bacillus Subtilis Spores Displaying Ompa of E. Anguillarum
Minxia Chen, Zihao Chen, Guanghua Sun, et al.
(2024)
Closed Access
Minxia Chen, Zihao Chen, Guanghua Sun, et al.
(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
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
Ralph R. Isberg, Kristin M. Kotewicz, Mengyun Zheng, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 1