Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Structure of ‘linkerless’ hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket
Alexa A. Tabackman, Rochelle Frankson, Eric S. Marsan, et al.
Journal of Structural Biology (2016) Vol. 195, Iss. 3, pp. 373-378
Open Access | Times Cited: 59

Showing 1-25 of 59 citing articles:

Characterization of Histone Deacetylase 8 (HDAC8) Selective Inhibition Reveals Specific Active Site Structural and Functional Determinants
Martin Marek, T.B. Shaik, Tino Heimburg, et al.
Journal of Medicinal Chemistry (2018) Vol. 61, Iss. 22, pp. 10000-10016
Open Access | Times Cited: 103
Histone deacetylase 8 (HDAC8) and its inhibitors with selectivity to other isoforms: An overview
Suvankar Banerjee, Nilanjan Adhikari, Sk. Abdul Amin, et al.
European Journal of Medicinal Chemistry (2018) Vol. 164, pp. 214-240
Closed Access | Times Cited: 97
A Genetically Encoded, Phage‐Displayed Cyclic‐Peptide Library
Xiaoshan Shayna Wang, Peng‐Hsun Chase Chen, J. Trae Hampton, et al.
Angewandte Chemie International Edition (2019) Vol. 58, Iss. 44, pp. 15904-15909
Open Access | Times Cited: 91
Homology modeling andin silicodesign of novel and potential dual-acting inhibitors of human histone deacetylases HDAC5 and HDAC9 isozymes
Ammar D. Elmezayen, Kemal Yelekçi
Journal of Biomolecular Structure and Dynamics (2020) Vol. 39, Iss. 17, pp. 6396-6414
Closed Access | Times Cited: 90
Bitter melon (Momordica charantia): a natural healthy vegetable
Farhan Saeed, Muhammad Afzaal, Bushra Niaz, et al.
International Journal of Food Properties (2018) Vol. 21, Iss. 1, pp. 1270-1290
Open Access | Times Cited: 89
Strategies To Design Selective Histone Deacetylase Inhibitors
Jelena Melesina, Conrad V. Simoben, Lucas Praetorius, et al.
ChemMedChem (2021) Vol. 16, Iss. 9, pp. 1336-1359
Closed Access | Times Cited: 84
Is dual inhibition of metalloenzymes HDAC-8 and MMP-2 a potential pharmacological target to combat hematological malignancies?
Sk. Abdul Amin, Nilanjan Adhikari, Tarun Jha
Pharmacological Research (2017) Vol. 122, pp. 8-19
Closed Access | Times Cited: 64
HDAC3 is a potential validated target for cancer: An overview on the benzamide-based selective HDAC3 inhibitors through comparative SAR/QSAR/QAAR approaches
Nilanjan Adhikari, Sk. Abdul Amin, Prakruti Trivedi, et al.
European Journal of Medicinal Chemistry (2018) Vol. 157, pp. 1127-1142
Closed Access | Times Cited: 59
Histone deacetylases as targets for the treatment of neurodegenerative disorders: Challenges and future opportunities
Daniel A. Rodrigues, Pedro de Sena Murteira Pinheiro, Fernanda S. Sagrillo, et al.
Medicinal Research Reviews (2020) Vol. 40, Iss. 6, pp. 2177-2211
Closed Access | Times Cited: 55
A Therapeutic Perspective of HDAC8 in Different Diseases: An Overview of Selective Inhibitors
Anna Fontana, Ilaria Cursaro, Gabriele Carullo, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 17, pp. 10014-10014
Open Access | Times Cited: 29
Are inhibitors of histone deacetylase 8 (HDAC8) effective in hematological cancers especially acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL)?
Sk. Abdul Amin, Samima Khatun, Shovanlal Gayen, et al.
European Journal of Medicinal Chemistry (2023) Vol. 258, pp. 115594-115594
Closed Access | Times Cited: 18
Intrinsic structural dynamics dictate enzymatic activity and inhibition
Vaibhav Kumar Shukla, Lucas Siemons, D. Flemming Hansen
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 41
Open Access | Times Cited: 18
Entropy as a Driver of Selectivity for Inhibitor Binding to Histone Deacetylase 6
N.J. Porter, Florence F. Wagner, D.W. Christianson
Biochemistry (2018) Vol. 57, Iss. 26, pp. 3916-3924
Open Access | Times Cited: 47
The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture
Jason K. K. Low, Ana P. G. Silva, Mehdi Sharifi Tabar, et al.
Cell Reports (2020) Vol. 33, Iss. 9, pp. 108450-108450
Open Access | Times Cited: 44
Discovery of novel N-substituted thiazolidinediones (TZDs) as HDAC8 inhibitors: in-silico studies, synthesis, and biological evaluation
Neha Upadhyay, Kalpana Tilekar, Niklas Jänsch, et al.
Bioorganic Chemistry (2020) Vol. 100, pp. 103934-103934
Open Access | Times Cited: 43
Structure-Based Inhibitor Discovery of Class I Histone Deacetylases (HDACs)
Yuxiang Luo, Huilin Li
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 22, pp. 8828-8828
Open Access | Times Cited: 39
Discovery of PPAR Alpha Lipid Pathway Modulators That Do Not Bind Directly to the Receptor as Potential Anti-Cancer Compounds
Arwa Al Subait, Raghad Alghamdi, Rizwan Ali, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 2, pp. 736-736
Open Access
HDAC inhibitor suppresses proliferation and invasion of breast cancer cells through regulation of miR-200c targeting CRKL
Xuehai Bian, Zhongxing Liang, Amber Feng, et al.
Biochemical Pharmacology (2017) Vol. 147, pp. 30-37
Open Access | Times Cited: 47
1-Arylsulfonyl indoline-benzamides as a new antitubulin agents, with inhibition of histone deacetylase
Mei-Jung Lai, Ritu Ojha, Mei-Hsiang Lin, et al.
European Journal of Medicinal Chemistry (2018) Vol. 162, pp. 612-630
Closed Access | Times Cited: 39
Binding mechanism and distant regulation of histone deacetylase 8 by PCI-34051
Yuxiang Luo, Zhaoyue Yan, Xiakun Chu, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access
Structure–Activity Relationships of Hydroxamate-Based Histone Deacetylase-8 Inhibitors: Reality Behind Anticancer Drug Discovery
Sk. Abdul Amin, Nilanjan Adhikari, Tarun Jha
Future Medicinal Chemistry (2017) Vol. 9, Iss. 18, pp. 2211-2237
Closed Access | Times Cited: 37
Design, Synthesis, and Biological Evaluation of Tetrahydroisoquinoline-Based Histone Deacetylase 8 Selective Inhibitors
Taha Y. Taha, Shaimaa M. Aboukhatwa, Rachel C. Knopp, et al.
ACS Medicinal Chemistry Letters (2017) Vol. 8, Iss. 8, pp. 824-829
Open Access | Times Cited: 35
In Silico Approaches for Investigating the Binding Propensity of Apigenin and Luteolin Against Class I HDAC Isoforms
Shabir Ahmad Ganai, Zeenat Farooq, Shahid Banday, et al.
Future Medicinal Chemistry (2018) Vol. 10, Iss. 16, pp. 1925-1945
Closed Access | Times Cited: 33
Structures of the Peptidoglycan N-Acetylglucosamine Deacetylase Bc1974 and Its Complexes with Zinc Metalloenzyme Inhibitors.
Petros Giastas, Athena Andreou, Athanasios Papakyriakou, et al.
Biochemistry (2018) Vol. 57, Iss. 5, pp. 753-763
Closed Access | Times Cited: 30
Combined pharmacophore modeling, 3D-QSAR and docking studies to identify novel HDAC inhibitors using drug repurposing
Jian Liu, Yehua Zhu, Yufang He, et al.
Journal of Biomolecular Structure and Dynamics (2019) Vol. 38, Iss. 2, pp. 533-547
Closed Access | Times Cited: 24
Page 1 - Next Page

Scroll to top