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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:

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: 34

Showing 1-25 of 34 citing articles:

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
Chemical and Enzymatic Methods for Post-Translational Protein–Protein Conjugation
Ross Taylor, Michael B. Geeson, Toby Journeaux, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 32, pp. 14404-14419
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
D‐Peptide and D‐Protein Technology: Recent Advances, Challenges, and Opportunities**
Alexander J. Lander, Yi Jin, Louis Y. P. Luk
ChemBioChem (2022) Vol. 24, Iss. 4
Open Access | Times Cited: 42
Structure-guided engineering enables E3 ligase-free and versatile protein ubiquitination via UBE2E1
Xiangwei Wu, Yunxiang Du, Lu-Jun Liang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 12
Decoding Chromatin Ubiquitylation: A Chemical Biology Perspective
Pauline Franz, Beat Fierz
Journal of Molecular Biology (2024) Vol. 436, Iss. 7, pp. 168442-168442
Open Access | Times Cited: 6
Native Semisynthesis of Isopeptide-Linked Substrates for Specificity Analysis of Deubiquitinases and Ubl Proteases
Zhou Zhao, Rachel O’Dea, Kim Wendrich, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 38, pp. 20801-20812
Open Access | Times Cited: 11
Deubiquitinase processing of a non-natural linkage of ubiquitinated-PTEN
Reina Iwase, Isabella Jaen Maisonet, Kwangwoon Lee, et al.
Bioorganic Chemistry (2025), pp. 108223-108223
Closed Access
Thioether-mediated protein ubiquitination in constructing affinity- and activity-based ubiquitinated protein probes
Gregory A. Davidson, Zeinab Moafian, Amanda R. Sensi, et al.
Nature Protocols (2025)
Closed Access
Site-specific ubiquitination: Deconstructing the degradation tag
Emma C. Carroll, Susan Marqusee
Current Opinion in Structural Biology (2022) Vol. 73, pp. 102345-102345
Open Access | Times Cited: 17
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: 3
Posttranslational Chemical Mutagenesis Methods to Insert Posttranslational Modifications into Recombinant Proteins
Omer Harel, Muhammad Jbara
Molecules (2022) Vol. 27, Iss. 14, pp. 4389-4389
Open Access | Times Cited: 15
NEDD4 and NEDD4L: Ubiquitin Ligases Closely Related to Digestive Diseases
Jiafan Xu, Jiang Wang, Tian Hu, et al.
Biomolecules (2024) Vol. 14, Iss. 5, pp. 577-577
Open Access | Times Cited: 2
Stable ubiquitin conjugation for biological interrogation of ubiquitinated tau repeat domain
Giovanna Viola, Daniele Trivellato, Lorenzo Meulli, et al.
Bioorganic Chemistry (2024) Vol. 150, pp. 107549-107549
Open Access | Times Cited: 2
Untangling the complexity and impact of tau protein ubiquitination
Daniele Trivellato, Francesca Munari, Michael Assfalg, et al.
ChemBioChem (2024) Vol. 25, Iss. 22
Open Access | Times Cited: 2
Genetic Code Expansion Approaches to Decipher the Ubiquitin Code
Vera Wanka, Maximilian Fottner, Marko Cigler, et al.
Chemical Reviews (2024) Vol. 124, Iss. 20, pp. 11544-11584
Open Access | Times Cited: 2
Nature-inspired and medicinally relevant short peptides
Maria Gessica Ciulla, Monica Civera, Sara Sattin, et al.
(2023), pp. 140-171
Open Access | Times Cited: 6
Synthesis of ubiquitinated proteins for biochemical and functional analysis
Julia Kriegesmann, Ashraf Brik
Chemical Science (2023) Vol. 14, Iss. 37, pp. 10025-10040
Open Access | Times Cited: 6
Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins
Dominik P. Vogl, Anne C. Conibear, Christian F. W. Becker
RSC Chemical Biology (2021) Vol. 2, Iss. 5, pp. 1441-1461
Open Access | Times Cited: 14
Cell‐Permeable Ubiquitin and Histone Tools for Studying Post‐translational Modifications
Jiahui Tang, Qingyao Shu, Yanyan Guo, et al.
ChemBioChem (2023) Vol. 24, Iss. 16
Closed Access | Times Cited: 4
N-tert-Butoxycarbonyl-N-(2-(tritylthio)ethoxy)glycine as a Building Block for Peptide Ubiquitination
Lingling Peng, Elizabeth Helgason, Rafael de Souza Miranda, et al.
Bioconjugate Chemistry (2024) Vol. 35, Iss. 2, pp. 245-253
Open Access | Times Cited: 1
Chemical Diversification of Enzymatically Assembled Polyubiquitin Chains to Decipher the Ubiquitin Codes Programmed on the Branch Structure
Takafumi Furuhata, Bumkyu Choi, Taiki Uno, et al.
Journal of the American Chemical Society (2024)
Closed Access | Times Cited: 1
A Site‐Specific Click Chemistry Approach to Di‐ubiquitylate H1 Variants Reveals Position‐dependent Stimulation of the DNA Repair Protein RNF168
Pauline Franz, Charlotte M. Delvaux de Fenffe, Beat Fierz
Angewandte Chemie International Edition (2024)
Open Access | Times Cited: 1
RAD18-catalysed formation of ubiquitination intermediate mimic of proliferating cell nuclear antigen PCNA
Liying Zhang, Zhiheng Deng, Yunxiang Du, et al.
Bioorganic & Medicinal Chemistry (2024) Vol. 117, pp. 118016-118016
Closed Access | Times Cited: 1
In vivo synthetic chemistry of proteolysis targeting chimeras (PROTACs)
Shusuke Tomoshige, Minoru Ishikawa
Bioorganic & Medicinal Chemistry (2021) Vol. 41, pp. 116221-116221
Closed Access | Times Cited: 10
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