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:
Computational Dissection of the Role of Trp305 in the Regulation of the Death-Associated Protein Kinase–Calmodulin Interaction
Yu-Ping Zhu, Xinyi Gao, Guo-Hui Xu, et al.
Biomolecules (2022) Vol. 12, Iss. 10, pp. 1395-1395
Open Access | Times Cited: 8
Yu-Ping Zhu, Xinyi Gao, Guo-Hui Xu, et al.
Biomolecules (2022) Vol. 12, Iss. 10, pp. 1395-1395
Open Access | Times Cited: 8
Showing 8 citing articles:
Predictive identification and design of potent inhibitors targeting resistance-inducing candidate genes from E. coli whole-genome sequences
Abdullahi Tunde Aborode, Neeraj Kumar, Christopher Busayo Olowosoke, et al.
Frontiers in Bioinformatics (2024) Vol. 4
Open Access | Times Cited: 2
Abdullahi Tunde Aborode, Neeraj Kumar, Christopher Busayo Olowosoke, et al.
Frontiers in Bioinformatics (2024) Vol. 4
Open Access | Times Cited: 2
The effect of phosphorylation on the conformational dynamics and allostery of the association of death-associated protein kinase with calmodulin
Xiaolong Li, Canglong Hou, Mingyuan Yang, et al.
Journal of Biomolecular Structure and Dynamics (2024), pp. 1-9
Closed Access | Times Cited: 1
Xiaolong Li, Canglong Hou, Mingyuan Yang, et al.
Journal of Biomolecular Structure and Dynamics (2024), pp. 1-9
Closed Access | Times Cited: 1
Mechanistic insights into the allosteric inactivation mechanism of ZAP-70 induced by the hot spot W165C mutation
Mingtai Hu, Wencong Ma, Jinghan Wang, et al.
Journal of Biomolecular Structure and Dynamics (2023) Vol. 42, Iss. 14, pp. 7600-7609
Closed Access | Times Cited: 4
Mingtai Hu, Wencong Ma, Jinghan Wang, et al.
Journal of Biomolecular Structure and Dynamics (2023) Vol. 42, Iss. 14, pp. 7600-7609
Closed Access | Times Cited: 4
Decoding the deactivation mechanism of R192W mutation of ZAP-70 using molecular dynamics simulations and binding free energy calculations
Xuehua Zhang, Wenqi Liang, Guodong Zheng, et al.
Journal of Molecular Modeling (2023) Vol. 29, Iss. 12
Closed Access | Times Cited: 3
Xuehua Zhang, Wenqi Liang, Guodong Zheng, et al.
Journal of Molecular Modeling (2023) Vol. 29, Iss. 12
Closed Access | Times Cited: 3
Mechanistic insights into the role of calcium in the allosteric regulation of the calmodulin-regulated death-associated protein kinase
Xiaolong Li, Bo Li, Jun Li, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 4
Xiaolong Li, Bo Li, Jun Li, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 4
Experimental and Computational Insights into Gangronema latifolium Leaf Compounds as GLP-1 Receptor Agonists
Ijeoma Akunna Duru, Uchechi E. Enenebeaku, Lynda Chioma Ngozi-Olehi, et al.
Chemistry Africa (2024) Vol. 7, Iss. 5, pp. 2581-2597
Closed Access
Ijeoma Akunna Duru, Uchechi E. Enenebeaku, Lynda Chioma Ngozi-Olehi, et al.
Chemistry Africa (2024) Vol. 7, Iss. 5, pp. 2581-2597
Closed Access
Advances in Computational Intelligence-Based Methods of Structure and Function Prediction of Proteins
Jian Zhang, Jingjing Qian
Biomolecules (2024) Vol. 14, Iss. 9, pp. 1083-1083
Open Access
Jian Zhang, Jingjing Qian
Biomolecules (2024) Vol. 14, Iss. 9, pp. 1083-1083
Open Access
Stereo-selectivity of enantiomeric inhibitors to ubiquitin-specific protease 7 (USP7) dissected by molecular docking, molecular dynamics simulations, and binding free energy calculations
Yusheng Zhang, Wenwen Dou, Ziqi Zhao, et al.
Molecular Diversity (2024)
Closed Access
Yusheng Zhang, Wenwen Dou, Ziqi Zhao, et al.
Molecular Diversity (2024)
Closed Access
