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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:

HOIL‐1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation
Ian R. Kelsall, Elisha H. McCrory, Yingqi Xu, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 96

Showing 1-25 of 96 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: 225
Mechanisms underlying ubiquitin-driven selective mitochondrial and bacterial autophagy
Ellen A. Goodall, Felix Kraus, J. Wade Harper
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1501-1513
Open Access | Times Cited: 77
Protein neddylation and its role in health and diseases
Shizhen Zhang, Qing Yu, Zhijian Li, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 36
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access | Times Cited: 3
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Kang Zhu, Marcin J. Suskiewicz, Andrea Hloušek-Kasun, et al.
Science Advances (2022) Vol. 8, Iss. 40
Open Access | Times Cited: 67
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
Ubiquitination of phosphatidylethanolamine in organellar membranes
Jun-Ichi Sakamaki, Koji L. Ode, Yoshitaka Kurikawa, et al.
Molecular Cell (2022) Vol. 82, Iss. 19, pp. 3677-3692.e11
Open Access | Times Cited: 55
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
Xiangyi S. Wang, Thomas R. Cotton, Sarah J. Trevelyan, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 40
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: 26
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
Kang Zhu, Marcin J. Suskiewicz, Chatrin Chatrin, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. 2, pp. 801-815
Open Access | Times Cited: 24
Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity
Magdalena Szczesna, Yizhou Huang, Rachel E. Lacoursiere, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 6, pp. 913-924.e7
Open Access | Times Cited: 13
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
Discovery and characterization of noncanonical E2-conjugating enzymes
S.A. Abdul Rehman, Chiara Cazzaniga, Elena Di Nisio, et al.
Science Advances (2024) Vol. 10, Iss. 13
Open Access | Times Cited: 10
Structure of the extracellular region of the adhesion GPCR CELSR1 reveals a compact module which regulates G protein-coupling
Sumit J. Bandekar, Krassimira Garbett, Szymon P. Kordon, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 9
Biallelic human SHARPIN loss of function induces autoinflammation and immunodeficiency
Hirotsugu Oda, Kalpana Manthiram, Pallavi Pimpale Chavan, et al.
Nature Immunology (2024) Vol. 25, Iss. 5, pp. 764-777
Closed Access | Times Cited: 9
Linear ubiquitination at damaged lysosomes induces local NFKB activation and controls cell survival
Laura Zein, Marvin Dietrich, Denise Balta, et al.
Autophagy (2025), pp. 1-21
Open Access | Times Cited: 1
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
DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids
Emily L Dearlove, Chatrin Chatrin, Lori Buetow, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 8
Sugar-mediated non-canonical ubiquitination impairs Nrf1/NFE2L1 activation
Yasuko Yoshida, Tsuyoshi Takahashi, Nozomi Ishii, et al.
Molecular Cell (2024) Vol. 84, Iss. 16, pp. 3115-3127.e11
Closed Access | Times Cited: 8
Just how big is the ubiquitin system?
Bernhard C. Lechtenberg, David Komander
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 210-213
Closed Access | Times Cited: 7
The role of ubiquitination in health and disease
Yan Liao, Wangzheqi Zhang, Yang Liu, et al.
MedComm (2024) Vol. 5, Iss. 10
Open Access | Times Cited: 7
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