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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:

The ‘dark matter’ of ubiquitin-mediated processes: opportunities and challenges in the identification of ubiquitin-binding domains
Elizabeth Radley, Joanna Long, Kevin C. Gough, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1949-1962
Closed Access | Times Cited: 17

Showing 17 citing articles:

Ubiquitomics: An Overview and Future
George Vere, Rachel Kealy, Benedikt M. Kessler, et al.
Biomolecules (2020) Vol. 10, Iss. 10, pp. 1453-1453
Open Access | Times Cited: 102
Membrane Protein Quality Control Mechanisms in the Endo-Lysosome System
Richa Sardana, Scott D. Emr
Trends in Cell Biology (2021) Vol. 31, Iss. 4, pp. 269-283
Open Access | Times Cited: 81
Current methodologies in protein ubiquitination characterization: from ubiquitinated protein to ubiquitin chain architecture
Mingwei Sun, Xiaofei Zhang
Cell & Bioscience (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 41
The role of K63-linked polyubiquitin in several types of autophagy
Anna Dósa, Tamás Csizmadia
Biologia Futura (2022) Vol. 73, Iss. 2, pp. 137-148
Open Access | Times Cited: 29
TNK1 is a ubiquitin-binding and 14-3-3-regulated kinase that can be targeted to block tumor growth
Tsz‐Yin Chan, Christina M. Egbert, Julia E. Maxson, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 29
Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
Barbara Korbei
Essays in Biochemistry (2022) Vol. 66, Iss. 2, pp. 169-177
Open Access | Times Cited: 17
Old and New Concepts in Ubiquitin and NEDD8 Recognition
Elena Santonico
Biomolecules (2020) Vol. 10, Iss. 4, pp. 566-566
Open Access | Times Cited: 27
Identification of ester-linked ubiquitylation sites during TLR7 signalling increases the number of inter-ubiquitin linkages from 8 to 12
Elisha H. McCrory, Vyacheslav Akimov, Philip Cohen, et al.
Biochemical Journal (2022) Vol. 479, Iss. 23, pp. 2419-2431
Open Access | Times Cited: 12
Deciphering the protein ubiquitylation system in plants
Zhihua Hua
Journal of Experimental Botany (2023) Vol. 74, Iss. 21, pp. 6487-6504
Closed Access | Times Cited: 5
Tsg101 mimicry of canonical E2 enzymes underlies its role in ubiquitin signaling
David A. Nyenhuis, Susan M. Watanabe, Nico Tjandra, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 122, Iss. 1
Open Access | Times Cited: 1
Antibody-free approach for ubiquitination profiling by selectively clicking the ubiquitination sites
Mingwei Sun, Qing Zhang, Baofeng Zhao, et al.
Analytica Chimica Acta (2023) Vol. 1246, pp. 340877-340877
Closed Access | Times Cited: 3
Tools for Decoding Ubiquitin Signaling in DNA Repair
Benjamin M. Foster, Martin Attwood, Ian Gibbs‐Seymour
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 5
Bacterial mimicry of eukaryotic HECT ubiquitin ligation
Tyler G. Franklin, Peter S. Brzović, Jonathan N. Pruneda
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Bacterial ligases reveal fundamental principles of polyubiquitin specificity
Tyler G. Franklin, Peter S. Brzović, Jonathan N. Pruneda
Molecular Cell (2023) Vol. 83, Iss. 24, pp. 4538-4554.e4
Open Access | Times Cited: 1
Functional characterisation of DHX proteins in the regulation of RNA metabolism and genome stability
Rebecca Rossen Falk
(2023)
Open Access
Ester-linked ubiquitin sites formed by HOIL-1 in TLR7 signaling include four novel ubiquitin dimers
Elisha H. McCrory, Vyacheslav Akimov, Philip Cohen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
The Lambda Display Technology: A Useful Tool for the Identification of Ubiquitin-and Ubiquitin-Like-Binding Domains
Elena Santonico
Methods in molecular biology (2022), pp. 163-175
Closed Access
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