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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:

Emerging functions of branched ubiquitin chains
Michael French, Chad F. Koehler, Tony Hunter
Cell Discovery (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 152

Showing 1-25 of 152 citing articles:

Deubiquitinase-targeting chimeras for targeted protein stabilization
Nathaniel J. Henning, Lydia Boike, Jessica N. Spradlin, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 4, pp. 412-421
Open Access | Times Cited: 215
Decoding Post-Translational Modification Crosstalk With Proteomics
Mario Leutert, Samuel W. Entwisle, Judit Villén
Molecular & Cellular Proteomics (2021) Vol. 20, pp. 100129-100129
Open Access | Times Cited: 160
Ubiquitin ligases: guardians of mammalian development
David A. Cruz Walma, Zhuoyao Chen, Alex N. Bullock, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 5, pp. 350-367
Open Access | Times Cited: 119
E3 ligases and deubiquitinating enzymes regulating the MAPK signaling pathway in cancers
Hong‐Beom Park, Kwang‐Hyun Baek
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2022) Vol. 1877, Iss. 3, pp. 188736-188736
Closed Access | Times Cited: 99
Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory
Angus D. Cowan, Alessio Ciulli
Annual Review of Biochemistry (2022) Vol. 91, Iss. 1, pp. 295-319
Open Access | Times Cited: 83
Disorders of ubiquitylation: unchained inflammation
David B. Beck, Achim Werner, Daniel L. Kastner, et al.
Nature Reviews Rheumatology (2022) Vol. 18, Iss. 8, pp. 435-447
Open Access | Times Cited: 76
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
The proteasome and its role in the nervous system
Fulya Türker, Emily K. Cook, Seth S. Margolis
Cell chemical biology (2021) Vol. 28, Iss. 7, pp. 903-917
Open Access | Times Cited: 62
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
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: 39
The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer
Nicole E. Pellegrino, Arcan Güven, Kayleigh Gray, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3480-3480
Open Access | Times Cited: 38
Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5
Laura A. Hehl, Daniel Horn‐Ghetko, J. Rajan Prabu, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 2, pp. 190-200
Open Access | Times Cited: 36
Speaking the host language: how Salmonella effector proteins manipulate the host
Timesh D Pillay, Sahampath U. Hettiarachchi, Jiyao Gan, et al.
Microbiology (2023) Vol. 169, Iss. 6
Open Access | Times Cited: 29
An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes
Haithem Barbour, Nadine Sen Nkwe, Benjamin Estavoyer, et al.
iScience (2023) Vol. 26, Iss. 5, pp. 106276-106276
Open Access | Times Cited: 26
USP30 inhibition induces mitophagy and reduces oxidative stress in parkin-deficient human neurons
Justyna Okarmus, Jette Bach Agergaard, Tina C. Stummann, et al.
Cell Death and Disease (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 11
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
Exploration of Degrons and Their Ability to Mediate Targeted Protein Degradation
Timothy J. Harris, Darci J. Trader
RSC Medicinal Chemistry (2025)
Closed Access | Times Cited: 1
Distinct Stress Regulators in the CRL Family: Emerging Roles of F‐Box Proteins
Jiwon Hwang, Linda Lauinger, Peter Kaiser
BioEssays (2025)
Closed Access | Times Cited: 1
Atypical Ubiquitination and Parkinson’s Disease
О.А. Бунеева, A. E. Medvedev
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3705-3705
Open Access | Times Cited: 34
Acetylation, Phosphorylation, Ubiquitination (Oh My!): Following Post-Translational Modifications on the Ubiquitin Road
Rachel E. Lacoursiere, Dania Hadi, Gary S. Shaw
Biomolecules (2022) Vol. 12, Iss. 3, pp. 467-467
Open Access | Times Cited: 32
USP15 antagonizes CRL4 CRBN -mediated ubiquitylation of glutamine synthetase and neosubstrates
Thang Van Nguyen
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 40
Open Access | Times Cited: 35
USP1 modulates hepatocellular carcinoma progression via the Hippo/TAZ axis
Dongyi Liu, Quanhui Li, Yifeng Zang, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 4
Open Access | Times Cited: 14
TRIM21 promotes ubiquitination of SARS‐CoV‐2 nucleocapsid protein to regulate innate immunity
Shenglan Mao, Xue-Fei Cai, Siqiang Niu, et al.
Journal of Medical Virology (2023) Vol. 95, Iss. 4
Closed Access | Times Cited: 14
Current and future directions of USP7 interactome in cancer study
Hong‐Beom Park, Kwang‐Hyun Baek
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2023) Vol. 1878, Iss. 6, pp. 188992-188992
Closed Access | Times Cited: 13
In the moonlight: non-catalytic functions of ubiquitin and ubiquitin-like proteases
Marta Campos Alonso, Klaus‐Peter Knobeloch
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access | Times Cited: 5
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