Phosphorylation of Tyrosine-182 decreases the ubiquitin binding ability and Rad23-mediated protein degradation
碩士 === 國立中興大學 === 生物醫學研究所 === 96 === Rad23 is evolutionarily conserved for involving in DNA nuclear excision repair (NER) and ubiquitin-proteasome system (UPS) from yeast to human. However, the signaling regulation of Rad23 function is still unknown. To investigate the signaling control for Rad23...
Main Authors: | Bo-RongChen, 陳柏蓉 |
---|---|
Other Authors: | 莊秀美 |
Format: | Others |
Language: | en_US |
Online Access: | http://ndltd.ncl.edu.tw/handle/26586077287142432865 |
Similar Items
-
Phosphorylation of Serine 47 on Rad23 protein reduces the 26S proteasome binding ability and Rad23-mediated protein degradation in Saccharomyces cerevisiae
by: Bo-Ting Ko, et al.
Published: (99) -
Phosphorylation of Serine-73 decreases the association of yeast Rad23 with the 26S proteasome and Rad23-mediated protein degradation
by: Ruei-Yue Liang, et al.
Published: (99) -
Characterization of the Rad23T354 phosphorylation site in the regulation of Rad23 functions
by: Bo-Chu Kuo, et al.
Published: (2006) -
Regulation of Inter-Protein Interactions Between Ubiquitin and Ubiquitin-Associated Domains in Rad23A/Ubiquilin-1 by Phosphorylation
by: RAN Meng-lin, et al.
Published: (2019-03-01) -
Analysis of the role of B23 phosphorylation at Thr199 on B23 protein ubiquitination/degradation and its localization.
by: Huang Yuan-Chun, et al.
Published: (2007)