
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:
Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector
Anıl Aktürk, David J. Wasilko, Xiaochun Wu, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 729-733
Open Access | Times Cited: 87
Anıl Aktürk, David J. Wasilko, Xiaochun Wu, et al.
Nature (2018) Vol. 557, Iss. 7707, pp. 729-733
Open Access | Times Cited: 87
Showing 51-75 of 87 citing articles:
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
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
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
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
Development of ADPribosyl Ubiquitin Analogues to Study Enzymes Involved in Legionella Infection
Robbert Q. Kim, Mohit Misra, Alexis González, et al.
Chemistry - A European Journal (2020) Vol. 27, Iss. 7, pp. 2506-2512
Open Access | Times Cited: 11
Robbert Q. Kim, Mohit Misra, Alexis González, et al.
Chemistry - A European Journal (2020) Vol. 27, Iss. 7, pp. 2506-2512
Open Access | Times Cited: 11
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
INHAT subunit SET/TAF-Iβ regulates PRC1-independent H2AK119 mono-ubiquitination via E3 ligase MIB1 in colon cancer
Junyoung Park, Jiyoung Kim, Jin Woo Park, et al.
NAR Cancer (2023) Vol. 5, Iss. 3
Open Access | Times Cited: 3
Junyoung Park, Jiyoung Kim, Jin Woo Park, et al.
NAR Cancer (2023) Vol. 5, Iss. 3
Open Access | Times Cited: 3
Synthesis of Stable NAD+ Mimics as Inhibitors for the Legionella pneumophila Phosphoribosyl Ubiquitylating Enzyme SdeC
Jerre M. Madern, Robbert Q. Kim, Mohit Misra, et al.
ChemBioChem (2020) Vol. 21, Iss. 20, pp. 2903-2907
Open Access | Times Cited: 8
Jerre M. Madern, Robbert Q. Kim, Mohit Misra, et al.
ChemBioChem (2020) Vol. 21, Iss. 20, pp. 2903-2907
Open Access | Times Cited: 8
A toolbox of diverse arginine N-glycosylated peptides and specific antibodies
Yanan Jiang, Zhaoxi Cheng, Si Chen, et al.
Bioorganic Chemistry (2022) Vol. 130, pp. 106267-106267
Closed Access | Times Cited: 5
Yanan Jiang, Zhaoxi Cheng, Si Chen, et al.
Bioorganic Chemistry (2022) Vol. 130, pp. 106267-106267
Closed Access | Times Cited: 5
Structural biology of the invasion arsenal of Gram‐negative bacterial pathogens
Andrey M. Grishin, Kevin Voth, Alla Gagarinova, et al.
FEBS Journal (2021) Vol. 289, Iss. 6, pp. 1385-1427
Open Access | Times Cited: 7
Andrey M. Grishin, Kevin Voth, Alla Gagarinova, et al.
FEBS Journal (2021) Vol. 289, Iss. 6, pp. 1385-1427
Open Access | Times Cited: 7
VibrioMARTX toxin processing and degradation of cellular Rab GTPases by the cytotoxic effector Makes Caterpillars Floppy
Alfa Herrera, Megan M. Packer, Mónica Rosas‐Lemus, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Alfa Herrera, Megan M. Packer, Mónica Rosas‐Lemus, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Structural insights into caspase ADPR deacylization catalyzed by a bacterial effector and host calmodulin
Kuo Zhang, Ting Peng, Xinyuan Tao, et al.
Molecular Cell (2022) Vol. 82, Iss. 24, pp. 4712-4726.e7
Open Access | Times Cited: 4
Kuo Zhang, Ting Peng, Xinyuan Tao, et al.
Molecular Cell (2022) Vol. 82, Iss. 24, pp. 4712-4726.e7
Open Access | Times Cited: 4
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
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
Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis
Xiu Yin, Qingbin Liu, Fen Liu, et al.
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 3
Xiu Yin, Qingbin Liu, Fen Liu, et al.
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 3
A survey of ADP-ribosyltransferase families in the pathogenicLegionella
Marianna Krysińska, Marcin Gradowski, Bartosz Baranowski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Marianna Krysińska, Marcin Gradowski, Bartosz Baranowski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Legionella pneumophila , a Rosetta stone to understanding bacterial pathogenesis
Katerina A. Romanov, Tamara J. O’Connor
Journal of Bacteriology (2024)
Closed Access
Katerina A. Romanov, Tamara J. O’Connor
Journal of Bacteriology (2024)
Closed Access
Protein polyglutamylation catalyzed by the bacterial Calmodulin-dependent pseudokinase SidJ
Alan Sulpizio, Marena E. Minelli, Min Wan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 3
Alan Sulpizio, Marena E. Minelli, Min Wan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 3
Deubiquitination of phosphoribosyl-ubiquitin conjugates by PDE domain-containingLegionellaeffectors
Min Wan, Alan Sulpizio, Anıl Aktürk, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 3
Min Wan, Alan Sulpizio, Anıl Aktürk, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 3
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
Deciphering the catalytic mechanism of bacterial ubiquitination
Kathy Wong, Kalle Gehring
Nature (2018) Vol. 557, Iss. 7707, pp. 644-645
Closed Access | Times Cited: 2
Kathy Wong, Kalle Gehring
Nature (2018) Vol. 557, Iss. 7707, pp. 644-645
Closed Access | Times Cited: 2
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
Yaobin Liu, Rukmini Mukherjee, Florian Bonn, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 2
Yaobin Liu, Rukmini Mukherjee, Florian Bonn, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 2
Diverse ubiquitin codes in the regulation of inflammatory signaling
Fumiyo Ikeda
Proceedings of the Japan Academy Series B (2020) Vol. 96, Iss. 9, pp. 431-439
Open Access | Times Cited: 2
Fumiyo Ikeda
Proceedings of the Japan Academy Series B (2020) Vol. 96, Iss. 9, pp. 431-439
Open Access | Times Cited: 2