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OpenAlex Citation Counts

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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:

Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB
Dong Hyuk Shin, Rukmini Mukherjee, Yaobin Liu, et al.
Molecular Cell (2019) Vol. 77, Iss. 1, pp. 164-179.e6
Open Access | Times Cited: 120

Showing 1-25 of 120 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
ER remodeling via ER-phagy
Andrea Gubaš, Ivan Đikić
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1492-1500
Open Access | Times Cited: 82
A lysosome membrane regeneration pathway depends on TBC1D15 and autophagic lysosomal reformation proteins
Anshu Bhattacharya, Rukmini Mukherjee, Santosh Kumar Kuncha, et al.
Nature Cell Biology (2023) Vol. 25, Iss. 5, pp. 685-698
Closed Access | Times Cited: 41
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Outer membrane vesicles containing OmpA induce mitochondrial fragmentation to promote pathogenesis of Acinetobacter baumannii
Varnesh Tiku, Eric M. Kofoed, Donghong Yan, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 71
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
Legionella pneumophila modulates host energy metabolism by ADP-ribosylation of ADP/ATP translocases
Jiaqi Fu, Mowei Zhou, Marina Gritsenko, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 44
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
Non-proteolytic ubiquitylation in cellular signaling and human disease
Yongrong Liao, Izabela Sumara, Evanthia Pangou
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 40
The ubiquitin codes in cellular stress responses
Xiangpeng Sheng, Zhixiong Xia, Hanting Yang, et al.
Protein & Cell (2023) Vol. 15, Iss. 3, pp. 157-190
Open Access | Times Cited: 37
Targeting the Ubiquitin–Proteasome System and Recent Advances in Cancer Therapy
Daniela Spano, Giuliana Catara
Cells (2023) Vol. 13, Iss. 1, pp. 29-29
Open Access | Times Cited: 25
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
Legionella effector LnaB is a phosphoryl-AMPylase that impairs phosphosignalling
Ting Wang, Xiaonan Song, Jiaxing Tan, et al.
Nature (2024) Vol. 631, Iss. 8020, pp. 393-401
Closed Access | Times Cited: 9
Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms
Jiaqi Fu, Siying Li, Hongxin Guan, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9
Molecular Mimicry: a Paradigm of Host-Microbe Coevolution Illustrated by Legionella
Sonia Mondino, Silke Schmidt, Carmen Buchrieser
mBio (2020) Vol. 11, Iss. 5
Open Access | Times Cited: 66
Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes
Shuxin Liu, Jiwei Luo, Xiangkai Zhen, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 51
ADP-ribosylation systems in bacteria and viruses
Petra Mikolčević, Andrea Hloušek-Kasun, Ivan Ahel, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 2366-2383
Open Access | Times Cited: 48
The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains
Alan Rodriguez Carvajal, Irina Grishkovskaya, Carlos Gómez-Díaz, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 48
The Ubiquitination System within Bacterial Host–Pathogen Interactions
Vera Vozandychova, Pavla Stojková, Kamil Hercík, et al.
Microorganisms (2021) Vol. 9, Iss. 3, pp. 638-638
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
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
Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Bacterial ubiquitin ligases hijack the host deubiquitinase OTUB1 to inhibit MTORC1 signaling and promote autophagy
Kelong Ma, Wei Xian, Hongtao Liu, et al.
Autophagy (2024) Vol. 20, Iss. 9, pp. 1968-1983
Closed Access | Times Cited: 6
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