Minxi Rong¹, Yong Li^1,*, Xiaoli Guo^1,*, Tao Zong², Zhiyuan Ma², Penglei Li²

Oncologie, Vol.24, No.2, pp. 309-327, 2022, DOI:10.32604/oncologie.2022.021256 - 29 June 2022

Abstract Objectives: The ERα biological activity prediction model is constructed by the compound molecular data of the anti-breast cancer therapeutic target ERα and its biological activity data, which improves the screening efficiency of anti-breast cancer drug candidates and saves the time and cost of drug development. Methods: In this paper, Ridge model is used to screen out molecular descriptors with a high degree of influence on the biological activity of Erα and divide datasets with different numbers of the molecular descriptors by screening results. Random Forest (RF) is trained by Root Mean Square Error (RMSE) and Coefficient of… More >

MIN TANG^1,#, XUELING HE^1,2,#, XINGHONG YAO¹, JIRUI WEN¹, MINGYUE BAO¹, LIANG LI^1,*

BIOCELL, Vol.46, No.6, pp. 1465-1472, 2022, DOI:10.32604/biocell.2022.018967 - 07 February 2022

Abstract The present study was designed to investigate the role of estrogen receptor α (ERα) in biaxial tensile strain (BTS) regulated osteogenic differentiation of rat bone marrow-derived mesenchymal stem cells (rBMSCs). rBMSCs were derived from rats and overexpressed ERα. The rBMSCs were subjected to BTS at 1 Hz with a strain of 2% for 4 h per day, 3 days, with or without ERα inhibitor ICI 182,780 (ICI). Then, bone mineralization was performed by Alizarin Red Staining. The markers of osteogenic differentiation and downstream Wnt3a/β-catenin signaling were detected by western blotting. Results showed that BTS enhanced More >

JUN ZHANG, YEHONG HUANG, WENZHUO LIU, LULU LI, LIMING CHEN^*

BIOCELL, Vol.44, No.4, pp. 591-595, 2020, DOI:10.32604/biocell.2020.011642 - 24 December 2020

Abstract Estrogen receptor alpha (ERα/ESR1) is overexpressed in over half of all breast cancers and is considered a valuable therapeutic target in ERα positive breast cancer. Here, we designed a membrane-permeant Chaperonemediated Autophagy Targeting Chimeras (CMATAC) peptide to knockdown endogenous ERα protein through chaperone-mediated autophagy. The peptide contains a cell membrane-penetrating peptide (TAT) that allows the peptide to by-pass the plasma membrane, an αI peptide as a protein-binding peptide (PBD) that binds specifically to ERα, and CMA-targeting peptide (CTM) that targeting chaperone-mediated autophagy. We validated that ERα targeting peptide was able to target and degrade ERα More >