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:

Histone deacetylase-10 liberates spermidine to support polyamine homeostasis and tumor cell growth
Tracy Murray Stewart, Jackson R. Foley, Cassandra E. Holbert, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 10, pp. 102407-102407
Open Access | Times Cited: 14

Showing 14 citing articles:

Chemical Versatility in Catalysis and Inhibition of the Class IIb Histone Deacetylases
D.W. Christianson
Accounts of Chemical Research (2024) Vol. 57, Iss. 8, pp. 1135-1148
Closed Access | Times Cited: 11

Polyamine metabolism and anti-tumor immunity
Jingyi Wu, Yan Zeng, Yu-Yang You, et al.
Frontiers in Immunology (2025) Vol. 16
Open Access | Times Cited: 1

Acylspermidines are conserved mitochondrial sirtuin-dependent metabolites
Bingsen Zhang, James Mullmann, Andreas H. Ludewig, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 7, pp. 812-822
Closed Access | Times Cited: 8

Technologies of targeting histone deacetylase in drug discovery: Current progress and emerging prospects
Jinxiao Ru, Yuxi Wang, Zijia Li, et al.
European Journal of Medicinal Chemistry (2023) Vol. 261, pp. 115800-115800
Closed Access | Times Cited: 10

An enhanced method for the determination of polyamine content in biological samples by dansyl chloride derivatization and HPLC
Ashley Nwafor, Tracy Murray Stewart, Robert A. Casero
Methods in enzymology on CD-ROM/Methods in enzymology (2025)
Closed Access

Cell-based determination of HDAC10-mediated polyamine deacetylase activity
I.D. Gupta, Ashley Nwafor, Robert A. Casero, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2025)
Closed Access

Polyamine quantitation by LC-MS using isobutyl chloroformate derivatives
Christine Isaguirre, Megan Gendjar, Kelsie M. Nauta, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2025)
Closed Access

Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors
Chiara Lambona, Clemens Zwergel, Rossella Fioravanti, et al.
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102668-102668
Open Access | Times Cited: 9

Design, Synthesis, and Structural Evaluation of Acetylated Phenylthioketone Inhibitors of HDAC10
Juana Goulart Stollmaier, P. R. Watson, D.W. Christianson
ACS Medicinal Chemistry Letters (2024) Vol. 15, Iss. 10, pp. 1715-1723
Closed Access | Times Cited: 3

HDAC10 switches NLRP3 modification from acetylation to ubiquitination and attenuates acute inflammatory diseases
Min Yang, Zhenzhi Qin, Yueke Lin, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 3

Knockdown of HDAC10 inhibits POLE2-mediated DNA damage repair in NSCLC cells by increasing SP1 acetylation levels
Hua Guo, Hui Ren, Kun Han, et al.
Pulmonary Pharmacology & Therapeutics (2023) Vol. 83, pp. 102250-102250
Closed Access | Times Cited: 5

A Structurally Diverse Compound Screening Library to Identify Substrates for Diamine, Polyamine, and Related Acetyltransferases
Hazel Leiva, P. Silva, Robert B. Painter, et al.
ACS Omega (2024) Vol. 9, Iss. 50, pp. 49887-49898
Open Access | Times Cited: 1

Distribution and diversity of classical deacylases in bacteria
Leonie G. Graf, Carlos Moreno–Yruela, Chuan Qin, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

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