Results 81 to 90 of about 63,885 (332)

Put a RING on it: Regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites.

Frontiers in Genetics, 2013
RING domain containing E3 ubiquitin ligases comprise a large family of enzymes that in combination with an E2 ubiquitin-conjugating enzyme, modify target proteins by attaching ubiquitin moieties.
Cristina eBartocci, Eros eLazzerini Denchi   +1 more
doaj   +1 more source

The E2 Ubiquitin-conjugating Enzymes Direct Polyubiquitination to Preferred Lysines

Journal of Biological Chemistry, 2010
The ubiquitin-proteasome pathway plays a crucial role in many cellular processes by degrading substrates tagged by polyubiquitin chains, linked mostly through lysine 48 of ubiquitin.
Yael David, T. Ziv, A. Admon, A. Navon
semanticscholar   +1 more source

Acod1 Promotes PAD4 Ubiquitination via UBR5 Alkylation to Modulate NETosis and Exert Protective Effects in Sepsis

Advanced Science, EarlyView.
In this study, Acod1 knockout in CLP mice significantly increases peripheral blood NET levels, exacerbating inflammation, organ damage, and reducing survival. Further research shows that UBR5 interacts with PAD4, a key NET formation protein. Acod1/itaconate (ITA) enhances the enzymatic activity of UBR5 by alkylating the Cys2768 site, promoting the K48 ...
Huifan Liu, Guoqing Jing, Shujuan Wu, Min Yuan, Yingyue Dong, Xue Chen, Huimin Zhou, Hailong Gong, Jing Zuo, Xiaojing Wu, Xuemin Song   +10 more
wiley   +1 more source

Proteasome inhibitors: new class of antitumor agents

Biomolecules & Biomedicine, 2003
The ubiquitin-proteasome pathway is the principal pathway for intracellular protein degradation1,2 (Fig 1). This pathway selectively degrades an extensive number of short-lived regulatory proteins involved in the control of normal cellular processes. In
Gordan Srkalović
doaj   +1 more source

Decoding the ubiquitin-mediated pathway of arthropod disease vectors. [PDF]

PLoS ONE, 2013
Protein regulation by ubiquitin has been extensively described in model organisms. However, characterization of the ubiquitin machinery in disease vectors remains mostly unknown.
Anthony Choy, Maiara S Severo, Ruobai Sun, Thomas Girke, Joseph J Gillespie, Joao H F Pedra   +5 more
doaj   +1 more source

The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes.

Proceedings of the National Academy of Sciences of the United States of America, 2005
Bacteria of Shigella spp. are responsible for shigellosis in humans. They use a type III secretion system to inject effector proteins into host cells and induce their entry into epithelial cells or trigger apoptosis in macrophages.
D. W. Kim, G. Lenzen, A. Page, P. Legrain, P. Sansonetti, C. Parsot   +5 more
semanticscholar   +1 more source

USP10 Inhibits Ferroptosis via Deubiquinating POLR2A in Head and Neck Squamous Cell Carcinoma

Advanced Science, EarlyView.
This study identifies USP10 as a novel deubiquitinase that antagonizes ferroptosis in head and neck squamous cell carcinoma (HNSCC). Mechanistically, USP10 directly stabilizes POLR2A protein through post‐translational deubiquitination, enabling POLR2A‐mediated transcriptional activation of SLC7A11, a key ferroptosis inhibitor.
Diekuo Zhang, Xueying Wang, Shanhong Lu, Yan Gao, Gangcai Zhu, Guo Li, Zongnan Yu, Junwei Hou, Helei Yan, Wenhui Yuan, Xin Zhang, Mien‐Chie Hung, Zhifeng Liu, Yong Liu   +13 more
wiley   +1 more source

PSMD14 Stabilizes SLC7A11 to Ameliorate Glucocorticoid‐Induced Osteoporosis by Suppressing Osteocyte Ferroptosis

Advanced Science, EarlyView.
Glucocorticoid‐induced osteoporosis (GIOP) triggers osteocyte ferroptosis via SLC7A11 degradation. PSMD14 stabilizes SLC7A11 by counteracting glucocorticoid‐driven ubiquitination, preserving cystine uptake and glutathione synthesis. AAV‐mediated PSMD14 delivery or its agonist Pantethine rescues osteocyte survival and bone loss in GIOP mice.
Yifeng Shi, Qian Tang, Sunren Sheng, Hongyi Jiang, Chen Jin, Chencheng Zhou, Chenglong Xie, Lin Zheng, Di Zhang, Hui Xu, Cong Xu, Haiwei Ma, Guangheng Xiang, Wenfei Ni, Xiaoyun Pan, Lei Yang, Huazi Xu, Yu Qian, Aimin Wu, Xiangyang Wang, Gang Zheng   +20 more
wiley   +1 more source

Following Ariadne's thread: a new perspective on RBR ubiquitin ligases

BMC Biology, 2012
Ubiquitin signaling pathways rely on E3 ligases for effecting the final transfer of ubiquitin from E2 ubiquitin conjugating enzymes to a protein target. Here we re-evaluate the hybrid RING/HECT mechanism used by the E3 family RING-between-RINGs (RBRs) to
Wenzel Dawn M, Klevit Rachel E
doaj   +1 more source

Lysine 63-linked Polyubiquitination of the Dopamine Transporter Requires WW3 and WW4 Domains of Nedd4-2 and UBE2D Ubiquitin-conjugating Enzymes*

Journal of Biological Chemistry, 2010
RNA interference screen previously revealed that a HECT-domain E3 ubiquitin ligase, neuronal precursor cell expressed, developmentally down-regulated 4-2 (Nedd4-2), is necessary for ubiquitination and endocytosis of the dopamine transporter (DAT) induced
Arnau Vina-Vilaseca, A. Sorkin
semanticscholar   +1 more source