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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:

Ubiquitylation at the crossroads of development and disease
Michael Rapé
Nature Reviews Molecular Cell Biology (2017) Vol. 19, Iss. 1, pp. 59-70
Closed Access | Times Cited: 515

Showing 1-25 of 515 citing articles:

Targeting NF-κB pathway for the therapy of diseases: mechanism and clinical study
Hui Yu, Liangbin Lin, Zhiqiang Zhang, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 1303
N-degron and C-degron pathways of protein degradation
Alexander Varshavsky
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 2, pp. 358-366
Open Access | Times Cited: 478
Harnessing the anti-cancer natural product nimbolide for targeted protein degradation
Jessica N. Spradlin, Xirui Hu, Carl C. Ward, et al.
Nature Chemical Biology (2019) Vol. 15, Iss. 7, pp. 747-755
Open Access | Times Cited: 348
Control of protein stability by post-translational modifications
Ji Min Lee, Henrik M. Hammarén, Mikhail M. Savitski, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 304
Principles of Ubiquitin-Dependent Signaling
Eugene Oh, David Akopian, Michael Rapé
Annual Review of Cell and Developmental Biology (2018) Vol. 34, Iss. 1, pp. 137-162
Closed Access | Times Cited: 295
Covalent Ligand Screening Uncovers a RNF4 E3 Ligase Recruiter for Targeted Protein Degradation Applications
Carl C. Ward, Jordan I. Kleinman, Scott M. Brittain, et al.
ACS Chemical Biology (2019) Vol. 14, Iss. 11, pp. 2430-2440
Open Access | Times Cited: 279
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
Richard S. Marshall, Richard D. Vierstra
Frontiers in Molecular Biosciences (2019) Vol. 6
Open Access | Times Cited: 194
USP7 targeting modulates anti-tumor immune response by reprogramming Tumor-associated Macrophages in Lung Cancer
Xiaomeng Dai, Lisen Lu, Suke Deng, et al.
Theranostics (2020) Vol. 10, Iss. 20, pp. 9332-9347
Open Access | Times Cited: 186
It’s all about tau
Cheril Tapia‐Rojas, Fabian Cabezas-Opazo, Carol A. Deaton, et al.
Progress in Neurobiology (2018) Vol. 175, pp. 54-76
Open Access | Times Cited: 162
Emerging functions of branched ubiquitin chains
Michael French, Chad F. Koehler, Tony Hunter
Cell Discovery (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 147
TRIM22 inhibits osteosarcoma progression through destabilizing NRF2 and thus activation of ROS/AMPK/mTOR/autophagy signaling
Wei Liu, Yuechao Zhao, Guangfu Wang, et al.
Redox Biology (2022) Vol. 53, pp. 102344-102344
Open Access | Times Cited: 109
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
Selenium chemistry for spatio-selective peptide and protein functionalization
Zhenguang Zhao, Shay Laps, Jacob S. Gichtin, et al.
Nature Reviews Chemistry (2024) Vol. 8, Iss. 3, pp. 211-229
Closed Access | Times Cited: 18
Branching Out: Improved Signaling by Heterotypic Ubiquitin Chains
Diane L. Haakonsen, Michael Rapé
Trends in Cell Biology (2019) Vol. 29, Iss. 9, pp. 704-716
Closed Access | Times Cited: 137
A Cellular Mechanism to Detect and Alleviate Reductive Stress
Andrew G. Manford, Fernando Rodríguez-Pérez, Karen Y. Shih, et al.
Cell (2020) Vol. 183, Iss. 1, pp. 46-61.e21
Open Access | Times Cited: 131
Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization
Anisha Shakya, Seonyoung Park, Neha Rana, et al.
Biophysical Journal (2019) Vol. 118, Iss. 3, pp. 753-764
Open Access | Times Cited: 130
The Role of Exportin-5 in MicroRNA Biogenesis and Cancer
Ke Wu, Juan He, Wenchen Pu, et al.
Genomics Proteomics & Bioinformatics (2018) Vol. 16, Iss. 2, pp. 120-126
Open Access | Times Cited: 122
Bardoxolone conjugation enables targeted protein degradation of BRD4
Bingqi Tong, Mai Luo, Yi Xie, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 114
Visualizing ubiquitination in mammalian cells
Sjoerd J. L. van Wijk, Simone Fulda, Ivan Đikić, et al.
EMBO Reports (2019) Vol. 20, Iss. 2
Open Access | Times Cited: 108
Epitranscriptomics and epiproteomics in cancer drug resistance: therapeutic implications
Huibin Song, Dongcheng Liu, Shaowei Dong, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 102
NEDD4 E3 ligase: Functions and mechanism in human cancer
Zhiwei Wang, Xiaoli Hu, Miaomiao Ye, et al.
Seminars in Cancer Biology (2020) Vol. 67, pp. 92-101
Closed Access | Times Cited: 101
An E3 ligase guide to the galaxy of small-molecule-induced protein degradation
Predrag Jevtić, Diane L. Haakonsen, Michael Rapé
Cell chemical biology (2021) Vol. 28, Iss. 7, pp. 1000-1013
Open Access | Times Cited: 99
Activity- and reactivity-based proteomics: Recent technological advances and applications in drug discovery
Henry J. Benns, Ceire J. Wincott, Edward W. Tate, et al.
Current Opinion in Chemical Biology (2020) Vol. 60, pp. 20-29
Closed Access | Times Cited: 91
Gene expression and cell identity controlled by anaphase-promoting complex
Eugene Oh, Kevin G. Mark, Annamaria Mocciaro, et al.
Nature (2020) Vol. 579, Iss. 7797, pp. 136-140
Open Access | Times Cited: 83
Protein Modification and Autophagy Activation
Rui Wang, Guanghui Wang
Advances in experimental medicine and biology (2019), pp. 237-259
Closed Access | Times Cited: 82
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