Proteomic analysis of stromal and epithelial cell communications in human endometrial cancer using a unique 3D co‐culture Model
Epithelial and stromal communications are essential for normal uterine functions and their
dysregulation contributes to the pathogenesis of many diseases including infertility …
dysregulation contributes to the pathogenesis of many diseases including infertility …
Spectrin and its interacting partners in nuclear structure and function
MW Lambert - Experimental Biology and Medicine, 2018 - journals.sagepub.com
Nonerythroid αII-spectrin is a structural protein whose roles in the nucleus have just begun
to be explored. αII-spectrin is an important component of the nucleoskelelton and has both …
to be explored. αII-spectrin is an important component of the nucleoskelelton and has both …
NEDD4 protects vascular endothelial cells against Angiotensin II-induced cell death via enhancement of XPO1-mediated nuclear export
J Xu, Z Sheng, F Li, S Wang, Y Yuan, M Wang… - Experimental Cell …, 2019 - Elsevier
NEDD4 is an E3 ubiquitin ligase containing the HECT domain, which regulates various
cellular processes, but its role in vascular endothelial cells is unknown. In the present study …
cellular processes, but its role in vascular endothelial cells is unknown. In the present study …
Ubiquitin-proteasome signaling in lung injury
Cell homeostasis requires precise coordination of cellular proteins function. Ubiquitination is
a post-translational modification that modulates protein half-life and function and is tightly …
a post-translational modification that modulates protein half-life and function and is tightly …
[HTML][HTML] Ubiquitin and ubiquitin-like proteins are essential regulators of DNA damage bypass
NA Wilkinson, KS Mnuskin, NW Ashton, R Woodgate - Cancers, 2020 - mdpi.com
Simple Summary Ubiquitin and ubiquitin-like proteins are conjugated to many other proteins
within the cell, to regulate their stability, localization, and activity. These modifications are …
within the cell, to regulate their stability, localization, and activity. These modifications are …
[HTML][HTML] A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning
KF Ketosugbo, HL Bushnell, RI Johnson - PloS one, 2017 - journals.plos.org
Ubiquitination is a crucial post-translational modification that can target proteins for
degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for …
degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for …
[HTML][HTML] Proteasomal degradation of Zn-dependent Hdacs: The E3-ligases implicated and the designed protacs that enable degradation
L Márquez-Cantudo, A Ramos, C Coderch… - Molecules, 2021 - mdpi.com
Protein degradation by the Ubiquitin-Proteasome System is one of the main mechanisms of
the regulation of cellular proteostasis, and the E3 ligases are the key effectors for the protein …
the regulation of cellular proteostasis, and the E3 ligases are the key effectors for the protein …
Introduction to Cancer Epigenetics
EE Gökalp, S Işık, S Artan - Cancer Epigenetics, 2023 - Springer
In recent years, many studies have focused on understanding the effects of genetic and
epigenetic mechanisms on carcinogenesis, diagnosing the disease at an early stage, and …
epigenetic mechanisms on carcinogenesis, diagnosing the disease at an early stage, and …
[HTML][HTML] Regulation of germ cell development by ARI1 family ubiquitin ligases in C. elegans
Abstract RING-between-RING (RBR) E3 ubiquitin ligases are implicated in various
developmental processes, and mutations in genes encoding RBR proteins HHARI/ARIH1 …
developmental processes, and mutations in genes encoding RBR proteins HHARI/ARIH1 …
RNF8 的亚细胞定位及其在胃癌中的表达与凋亡调控
刘健， 雷箴， 袁雯， 赵枚， 黄常志 - 肿瘤防治研究, 2017 - zlfzyj.com
RNF8的亚细胞定位及其在胃癌中的表达与凋亡调控 Page 1 肿瘤防治研究2017年第44卷第9期
Cancer Res Prev Treat,2017,Vol.44,No.9 ·575· doi:10.3971/j.issn.1000-8578.2017.17.0091 …
Cancer Res Prev Treat,2017,Vol.44,No.9 ·575· doi:10.3971/j.issn.1000-8578.2017.17.0091 …