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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:

Recent progress in dissecting ubiquitin signals with chemical biology tools
Qingyun Zheng, Zhen Su, Yuanyuan Yu, et al.
Current Opinion in Chemical Biology (2022) Vol. 70, pp. 102187-102187
Closed Access | Times Cited: 12

Showing 12 citing articles:

Recent advances in chemical protein synthesis: method developments and biological applications
Suwei Dong, Ji‐Shen Zheng, Yiming Li, et al.
Science China Chemistry (2024) Vol. 67, Iss. 4, pp. 1060-1096
Closed Access | Times Cited: 60
Chemical Synthesis of Human Proteoforms and Application in Biomedicine
Huasong Ai, Man Pan, Lei Liu
ACS Central Science (2024) Vol. 10, Iss. 8, pp. 1442-1459
Open Access | Times Cited: 11
Advances in the chemical synthesis of human proteoforms
Ziyi Yang, Yingqi Xiao, Yang Shi, et al.
Science China Life Sciences (2025)
Closed Access
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
Revealing the extracellular function of HMGB1 N-terminal region acetylation assisted by a protein semi-synthesis approach
Tongyao Wei, Jiamei Liu, Can Li, et al.
Chemical Science (2023) Vol. 14, Iss. 37, pp. 10297-10307
Open Access | Times Cited: 5
Rapid reconstitution of ubiquitinated nucleosome using a non-denatured histone octamer ubiquitylation approach
Weijie Li, Peirong Cao, Pengqi Xu, et al.
Cell & Bioscience (2024) Vol. 14, Iss. 1
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
Activity-based profiling of cullin-RING ligase networks by conformation-specific probes
Lukas T. Henneberg, Jaspal Singh, David M. Duda, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Chemical mechanisms of nucleosomal histone ubiquitination by RING-type E3 enzymes
Qiang Shi, Zebin Tong, Zhiheng Deng, et al.
Scientia Sinica Chimica (2023) Vol. 53, Iss. 8, pp. 1455-1471
Closed Access | Times Cited: 2
Development and applications of enzymatic peptide and protein ligation
Yan Cui, Dongyang Han, Xinfeng Bai, et al.
Journal of Peptide Science (2024)
Closed Access
Capturing Covalent Catalytic Intermediates by Enzyme Mutants: Recent Advances in Methodologies and Applications
Yongchao Wang, Shan Tang
ChemBioChem (2023) Vol. 24, Iss. 10
Closed Access | Times Cited: 1
Methods of the enzymatic production of Ub-based tools
Rujing Yuan, Yu Wang, Guo‐Chao Chu, et al.
Current Research in Chemical Biology (2023) Vol. 3, pp. 100044-100044
Open Access
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