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 Chemical Biology of Reversible Lysine Post-translational Modifications
Zhipeng A. Wang, Philip A. Cole
Cell chemical biology (2020) Vol. 27, Iss. 8, pp. 953-969
Open Access | Times Cited: 130

Showing 1-25 of 130 citing articles:

Deciphering protein post-translational modifications using chemical biology tools
Anne C. Conibear
Nature Reviews Chemistry (2020) Vol. 4, Iss. 12, pp. 674-695
Closed Access | Times Cited: 182

YY1 lactylation in microglia promotes angiogenesis through transcription activation-mediated upregulation of FGF2
Xiaotang Wang, Wei Fan, Na Li, et al.
Genome biology (2023) Vol. 24, Iss. 1
Open Access | Times Cited: 121

Recombinant protein expression: Challenges in production and folding related matters
Azadeh Beygmoradi, Ahmad Homaei, Roohullah Hemmati, et al.
International Journal of Biological Macromolecules (2023) Vol. 233, pp. 123407-123407
Closed Access | Times Cited: 48

Histone lactylation inhibits RARγ expression in macrophages to promote colorectal tumorigenesis through activation of TRAF6-IL-6-STAT3 signaling
Xiu-Ming Li, Yun Yang, Fuquan Jiang, et al.
Cell Reports (2024) Vol. 43, Iss. 2, pp. 113688-113688
Open Access | Times Cited: 33

Noncanonical Amino Acids in Biocatalysis
Zachary Birch-Price, Florence J. Hardy, Thomas M. Lister, et al.
Chemical Reviews (2024) Vol. 124, Iss. 14, pp. 8740-8786
Open Access | Times Cited: 22

Histone lysine acetyltransferase inhibitors: an emerging class of drugs for cancer therapy
Jeffrey D. White, Frederick A. Derheimer, Kristen Jensen-Pergakes, et al.
Trends in Pharmacological Sciences (2024) Vol. 45, Iss. 3, pp. 243-254
Open Access | Times Cited: 19

Coenzyme A biosynthesis: mechanisms of regulation, function and disease
Samuel A. Barritt, Sarah DuBois-Coyne, Christian C. Dibble
Nature Metabolism (2024) Vol. 6, Iss. 6, pp. 1008-1023
Closed Access | Times Cited: 18

Formaldehyde-Mediated Hydride Liberation of Alkylamines for Intermolecular Reactions in Hexafluoroisopropanol
Shaokun Cai, Hong Tang, Bo Li, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 9, pp. 5952-5963
Closed Access | Times Cited: 17

Lactate and lactylation in cancer
Jie Chen, Ziyue Huang, Ya Chen, et al.
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access | Times Cited: 9

CBP/p300: Critical Co-Activators for Nuclear Steroid Hormone Receptors and Emerging Therapeutic Targets in Prostate and Breast Cancers
Aaron Waddell, Haojie Huang, Daiqing Liao
Cancers (2021) Vol. 13, Iss. 12, pp. 2872-2872
Open Access | Times Cited: 72

STALLION: a stacking-based ensemble learning framework for prokaryotic lysine acetylation site prediction
Shaherin Basith, Gwang Lee, Balachandran Manavalan
Briefings in Bioinformatics (2021) Vol. 23, Iss. 1
Open Access | Times Cited: 72

Histone H2B Deacylation Selectivity: Exploring Chromatin’s Dark Matter with an Engineered Sortase
Zhipeng A. Wang, Samuel D. Whedon, Mingxuan Wu, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 8, pp. 3360-3364
Open Access | Times Cited: 47

Structural Basis of Sirtuin 6-Catalyzed Nucleosome Deacetylation
Zhipeng A. Wang, Jonathan Markert, Samuel D. Whedon, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 12, pp. 6811-6822
Closed Access | Times Cited: 39

Beyond metabolic waste: lysine lactylation and its potential roles in cancer progression and cell fate determination
Jun‐Han Wang, Ling Mao, Jun Wang, et al.
Cellular Oncology (2023) Vol. 46, Iss. 3, pp. 465-480
Closed Access | Times Cited: 36

Biological importance of arginine: A comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins
Munishwar N. Gupta, Vladimir N. Uversky
International Journal of Biological Macromolecules (2023) Vol. 257, pp. 128646-128646
Open Access | Times Cited: 33

Functional analysis of protein post‐translational modifications using genetic codon expansion
Tao Peng, Tandrila Das, Ke Ding, et al.
Protein Science (2023) Vol. 32, Iss. 4
Open Access | Times Cited: 28

HDAC inhibitors as pharmacological treatment for Duchenne muscular dystrophy: a discovery journey from bench to patients
Chiara Mozzetta, Vittorio Sartorelli, Prem Puri
Trends in Molecular Medicine (2024) Vol. 30, Iss. 3, pp. 278-294
Closed Access | Times Cited: 15

Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids
Cosimo Jann, Sabrina Giofrè, Rajanya Bhattacharjee, et al.
Chemical Reviews (2024) Vol. 124, Iss. 18, pp. 10281-10362
Closed Access | Times Cited: 15

Astrocyte-derived lactate aggravates brain injury of ischemic stroke in mice by promoting the formation of protein lactylation
Xiao‐Yi Xiong, Xinru Pan, Xia-Xia Luo, et al.
Theranostics (2024) Vol. 14, Iss. 11, pp. 4297-4317
Open Access | Times Cited: 14

Proteomics of the heart
Oleg A. Karpov, Aleksandr Stotland, Koen Raedschelders, et al.
Physiological Reviews (2024) Vol. 104, Iss. 3, pp. 931-982
Open Access | Times Cited: 13

Acetyl-methyllysine marks chromatin at active transcription start sites
William J. Lu-Culligan, Leah J. Connor, Yixuan Xie, et al.
Nature (2023) Vol. 622, Iss. 7981, pp. 173-179
Open Access | Times Cited: 19

Site-Specific Acetylation of the Transcription Factor Protein Max Modulates Its DNA Binding Activity
Raj V. Nithun, Yumi Minyi Yao, Omer Harel, et al.
ACS Central Science (2024) Vol. 10, Iss. 6, pp. 1295-1303
Open Access | Times Cited: 6

Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1
Kwangwoon Lee, Marco Barone, Amanda L. Waterbury, et al.
Nature Chemical Biology (2024)
Closed Access | Times Cited: 6

KATs off: Biomedical insights from lysine acetyltransferase inhibitors
Samuel D. Whedon, Philip A. Cole
Current Opinion in Chemical Biology (2022) Vol. 72, pp. 102255-102255
Open Access | Times Cited: 23

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