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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:

Enzymatic Assembly of Ubiquitin Chains
Martin A. Michel, David Komander, P.R. Elliott
Methods in molecular biology (2018), pp. 73-84
Closed Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

Mechanism and inhibition of the papain‐like protease, PLpro, of SARS‐CoV‐2
Theresa Klemm, Gregor Ebert, Dale J. Calleja, et al.
The EMBO Journal (2020) Vol. 39, Iss. 18
Open Access | Times Cited: 436
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: 41
Identification and characterization of diverse OTU deubiquitinases in bacteria
Alexander F. Schubert, Justine Nguyen, Tyler G. Franklin, et al.
The EMBO Journal (2020) Vol. 39, Iss. 15
Open Access | Times Cited: 63
Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity
Malte Gersch, Jane L. Wagstaff, Angela V. Toms, et al.
Molecular Cell (2019) Vol. 74, Iss. 3, pp. 436-451.e7
Open Access | Times Cited: 62
Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
Shuang Wang, Xiaoyan Lv, Jialin Zhang, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 4, pp. 2308-2308
Open Access | Times Cited: 33
K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors
Anita Waltho, Oliver Popp, Christopher Lenz, et al.
Life Science Alliance (2024) Vol. 7, Iss. 8, pp. e202402740-e202402740
Open Access | Times Cited: 7
High-throughput matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry–based deubiquitylating enzyme assay for drug discovery
Virginia De Cesare, Jennifer L. Moran, Ryan Traynor, et al.
Nature Protocols (2020) Vol. 15, Iss. 12, pp. 4034-4057
Open Access | Times Cited: 40
The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63‐branched ubiquitin chains
Lukas Pluska, Ernst Jarosch, Henrik Zauber, et al.
The EMBO Journal (2021) Vol. 40, Iss. 6
Open Access | Times Cited: 38
Chemical methods for protein site-specific ubiquitination
Weijun Gui, Gregory A. Davidson, Zhihao Zhuang
RSC Chemical Biology (2021) Vol. 2, Iss. 2, pp. 450-467
Open Access | Times Cited: 35
Structural basis of K63-ubiquitin chain formation by the Gordon-Holmes syndrome RBR E3 ubiquitin ligase RNF216
Thomas R. Cotton, Simon A. Cobbold, Jonathan P. Bernardini, et al.
Molecular Cell (2022) Vol. 82, Iss. 3, pp. 598-615.e8
Open Access | Times Cited: 25
Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, et al.
Molecular Cell (2022) Vol. 83, Iss. 1, pp. 105-120.e5
Open Access | Times Cited: 19
Sortase mediated protein ubiquitination with defined chain length and topology
Nicole R. Raniszewski, Jenna N. Beyer, M. Noël, et al.
RSC Chemical Biology (2024) Vol. 5, Iss. 4, pp. 321-327
Open Access | Times Cited: 4
The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro
Xiangyi S. Wang, Jenny Jiou, Anthony Cerra, et al.
Life Science Alliance (2025) Vol. 8, Iss. 6, pp. e202503243-e202503243
Open Access
Site-directed multivalent conjugation of antibodies to ubiquitinated payloads
Angela F. El Hebieshy, Zacharias Wijfjes, Camille M. Le Gall, et al.
Nature Biomedical Engineering (2025)
Open Access
Branched Ubiquitination: Detection Methods, Biological Functions and Chemical Synthesis
Yane‐Shih Wang, Kuen‐Phon Wu, Han-Kai Jiang, et al.
Molecules (2020) Vol. 25, Iss. 21, pp. 5200-5200
Open Access | Times Cited: 25
DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability
Benjamin M. Foster, Zijuan Wang, Christine K. Schmidt
Biochemical Journal (2024) Vol. 481, Iss. 7, pp. 515-545
Open Access | Times Cited: 3
Evaluating enzyme activities and structures of DUBs
Jonathan N. Pruneda, David Komander
Methods in enzymology on CD-ROM/Methods in enzymology (2019), pp. 321-341
Open Access | Times Cited: 24
Reading and Writing the Ubiquitin Code Using Genetic Code Expansion
Rishi Patel, Nipuni M. Pannala, Chittaranjan Das
ChemBioChem (2024) Vol. 25, Iss. 11
Open Access | Times Cited: 2
Secondary interactions in ubiquitin-binding domains achieve linkage or substrate specificity
Martin A. Michel, Simon R. Scutts, David Komander
Cell Reports (2024) Vol. 43, Iss. 8, pp. 114545-114545
Closed Access | Times Cited: 2
Caspase-2 is a condensate-mediated deubiquitinase in protein quality control
Yingwei Ge, Lijie Zhou, Yesheng Fu, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 11, pp. 1943-1957
Open Access | Times Cited: 2
Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53
Kim Wendrich, Kai Gallant, Sarah Recknagel, et al.
Nature Chemical Biology (2024)
Open Access | Times Cited: 2
Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy
Xiaohui Zhao, Maite Mißun, Tobias Schneider, et al.
ChemBioChem (2019) Vol. 20, Iss. 14, pp. 1772-1777
Open Access | Times Cited: 16
Mechanism and inhibition of SARS-CoV-2 PLpro
Theresa Klemm, Gregor Ebert, Dale J. Calleja, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 15
Synthesis of Branched Triubiquitin Active-Site Directed Probes
Jiaan Liu, Yanfeng Li, Kirandeep K. Deol, et al.
Organic Letters (2019) Vol. 21, Iss. 17, pp. 6790-6794
Open Access | Times Cited: 14
Ubiquitination and De-Ubiquitination in the Synthesis of Cow Milk Fat: Reality and Prospects
Rui Gao, Yanni Wu, Yuhao Wang, et al.
Molecules (2024) Vol. 29, Iss. 17, pp. 4093-4093
Open Access | Times Cited: 1
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