Results 21 to 30 of about 308,731 (375)

Ubiquitination of SARS-CoV-2 ORF7a promotes antagonism of interferon response

Cellular & Molecular Immunology, 2021
Understanding interactions between the host and SARS-CoV-2 is essential for developing effective vaccines and therapeutics. Here, we report that SARS-CoV-2 usurps the host ubiquitin system to polyubiquitinate accessory protein ORF7a at Lys119.
Zengguo Cao, Hongjie Xia, Ricardo Rajsbaum, X. Xia, Hualei Wang, P. Shi   +5 more
semanticscholar   +1 more source

A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]

Cell, 2008
Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Saifee, Nabiha Huq, Zheng, Ning
openaire   +2 more sources

Proteomic Analysis of Ubiquitinated Proteins in Rice (Oryza sativa) After Treatment With Pathogen-Associated Molecular Pattern (PAMP) Elicitors

Frontiers in Plant Science, 2018
Reversible protein ubiquitination plays essential roles in regulating cellular processes. Although many reports have described the functions of ubiquitination in plant defense responses, few have focused on global changes in the ubiquitome.
Xiao-Lin Chen, Xiao-Lin Chen, Xin Xie, Liye Wu, Caiyun Liu, Lirong Zeng, Xueping Zhou, Feng Luo, Guo-Liang Wang, Guo-Liang Wang, Wende Liu   +10 more
doaj   +1 more source

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica, Bustos, Daisy, COSCOY, Laurent, Kirkpatrick, Donald, Lill, Jennie   +4 more
core   +3 more sources

Bypassing ubiquitination enables LAT recycling to the cell surface and enhanced signaling in T cells.

PLoS ONE, 2020
LAT molecules defective in ubiquitination have an increased half-life and induce enhanced signaling when expressed in T cells. In this study, we have examined the role of ubiquitination in regulating LAT endocytosis, recycling, and degradation in resting
Lakshmi Balagopalan, Hiba Malik, Katherine M McIntire, Joseph A Garvey, Tiffany Nguyen, Ana B Rodriguez-Peña, Lawrence E Samelson   +6 more
doaj   +1 more source

Quantitative Ubiquitylomic Analysis of the Dynamic Changes and Extensive Modulation of Ubiquitylation in Papaya During the Fruit Ripening Process

Frontiers in Plant Science, 2022
Lysine ubiquitination is a highly conserved post-translational modification with diverse biological functions. However, there is little available information on lysine ubiquitination of non-histone proteins in papaya (Carica papaya L.).
Yuxing Mo, Bian Jiang, Jingxin Huo, Jiayi Lu, Xiaoyue Zeng, Yan Zhou, Tao Zhang, Min Yang, Yuerong Wei, Kaidong Liu   +9 more
doaj   +1 more source

Proteomic Analysis of Protein Ubiquitination Events in Human Primary and Metastatic Colon Adenocarcinoma Tissues

Frontiers in Oncology, 2020
Protein ubiquitination is essential for multiple physiological processes through regulating the stability or function of target proteins and has been found to play critical roles in human cancers.
Yi Zhang, Cong Chen, Tingting Yu, Tao Chen   +3 more
doaj   +1 more source

Global Screening of LUBAC and OTULIN Interacting Proteins by Human Proteome Microarray

Frontiers in Cell and Developmental Biology, 2021
Linear ubiquitination is a reversible posttranslational modification, which plays key roles in multiple biological processes. Linear ubiquitin chain assembly complex (LUBAC) catalyzes linear ubiquitination, while the deubiquitinase OTULIN (OTU ...
Lijie Zhou, Lijie Zhou, Yingwei Ge, Yesheng Fu, Bo Wu, Yong Zhang, Lei Li, Chun-Ping Cui, Siying Wang, Lingqiang Zhang   +9 more
doaj   +1 more source

Generation and physiological roles of linear ubiquitin chains [PDF]

, 2012
Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational modifications of proteins with broad regulatory roles across all of biology.
A Ciechanover, A Degterev, A Hershko, A Hershko, A Hershko, A Varshavsky, B Eisenhaber, B Gerlach, C Tokunaga, CK Ea, CM Pickart, CY Ni, DM Wenzel, DW Abbott, EW Doss-Pepe, F Ikeda, F Ikeda, F Ikeda, F Tokunaga, F Tokunaga, F Van Herreweghe, H HogenEsch, H Walczak, H Zhou, Henning Walczak, I Marin, I Marin, Ivan Dikic, J Peng, JN Dynek, JW Harper, Kazuhiro Iwai, KL Lim, M Karin, O Micheau, P Cohen, P de Bie, P Xu, S Hatakeyama, S Rahighi, T Hunter, T Kirisako, TL Haas, V Nagy, VK Chaugule, Y Sato, Y Ye, YC Lo   +47 more
core   +4 more sources

K48-Linked Ubiquitination Contributes to Nicotine-Augmented Bone Marrow-Derived Dendritic-Cell-Mediated Adaptive Immunity

Vaccines, 2021
K48-linked ubiquitination determining antigen degradation and the endosomal recruitments of p97 and Sec61 plays vital roles in dendritic cell (DC) cross-presentation.
Chun Fang Hu, Xiao Yan Liao, Dan Dan Xu, Yi Bin Ruan, Feng Guang Gao   +4 more
doaj   +1 more source