Results 101 to 110 of about 191,822 (309)

Enzymes of ubiquitination and deubiquitination [PDF]

, 2012
Ubiquitination, the covalent attachment of the small protein modifier ubiquitin to a substrate protein is involved in virtually all cellular processes by mediating the regulated degradation of proteins.
Neutzner, M., Neutzner, A.
core   +1 more source

The role of ubiquitination in health and disease

MedComm
Ubiquitination is an enzymatic process characterized by the covalent attachment of ubiquitin to target proteins, thereby modulating their degradation, transportation, and signal transduction.
Yan Liao, Wangzheqi Zhang, Yang Liu, Chenglong Zhu, Zui Zou   +4 more
doaj   +1 more source

Quantitative Analysis of Ubiquitinated Proteins in Human Pituitary and Pituitary Adenoma Tissues

Frontiers in Endocrinology, 2019
Protein ubiquitination is an important post-translational modification that is associated with multiple diseases, including pituitary adenomas (PAs). Protein ubiquitination profiling in human pituitary and PAs remains unknown.
Shehua Qian, Shehua Qian, Shehua Qian, Xiaohan Zhan, Xiaohan Zhan, Xiaohan Zhan, Miaolong Lu, Miaolong Lu, Miaolong Lu, Na Li, Na Li, Na Li, Ying Long, Ying Long, Ying Long, Xuejun Li, Dominic M. Desiderio, Xianquan Zhan, Xianquan Zhan, Xianquan Zhan, Xianquan Zhan   +20 more
doaj   +1 more source

Unveiling Lactylation: A Novel Frontier in Cancer Stemness and Therapy

Advanced Science, EarlyView.
Tumor metabolism and epigenetic regulation are intrinsically linked. This review highlights lactylation as a pivotal bridge connecting these processes, acting as an active epigenetic effector in cancer stemness. We delineate how lactylation orchestrates the cancer stem cell landscape and evaluate its regulatory networks.
Ting Li, Hongyu Gu, Chang Liu, Yuesheng Lv, Feifei Li, Liang Liang, Jia Yi, Xuanyi Wang, Yi Zhun Zhu, Chuan Xu   +9 more
wiley   +1 more source

Identification of ubiquitination sites in IKKβ. [PDF]

, 2018
As described in Materials and Methods, ubiquitination sites in IKKβ were detected by LC-MS/MS. All Lys residues in the IKKβ primary sequence are indicated on the x-axis.
Alexandre R. Campos (5870912), Thomas C. Whisenant (242995), Asma Siari (5870909), Leandro H. Gallo (502815), April N. Meyer (234448), Daniel J. Donoghue (234454), Juyeon Ko (5870900), Guillermo Cardenas (5870903), Katelyn N. Nelson (5870906)   +8 more
core   +1 more source

Dual Cytoplasmic and Chloroplastic Mechanisms Fine‐Tune Chloroplast Division through ARC3 Protein Stability

Advanced Science, EarlyView.
ARC3 levels are controlled by cytosolic and chloroplast proteolytic systems. PUB52 mediates ARC3 precursor ubiquitination and degradation in the cytosol, while CLPC1 promotes ARC3 degradation in chloroplasts, where ARC2 protects ARC3 from excessive breakdown. Disrupting these components causes chloroplast division defects, placing them upstream of ARC3.
Yang Yuan, Denghao Xiang, Ruiying Li, Zhichuang Yue, Zhipeng Wang, Honghong Hu   +5 more
wiley   +1 more source

Role of SUMO-1 modification in transcriptional activation [PDF]

, 2012
In unstimulated cells, the transcription factor NF-κB is held in the cytoplasm in an inactive state by IκB inhibitor proteins. Activation of NF--KB is mediated by signal induced degradation of IκBα via the ubiquitin proteasome-dependent pathway ...
Pinto Desterro, Maria Joana
core  

EUP: Enhanced cross-species prediction of ubiquitination sites via a conditional variational autoencoder network based on ESM2.

PLoS Computational Biology
Ubiquitination is critical in biomedical research. Predicting ubiquitination sites based on deep learning model have advanced the study of ubiquitination.
Junhao Liu, Zeyu Luo, Rui Wang, Xin Li, Yawen Sun, Zongqing Chen, Yu-Juan Zhang   +6 more
doaj   +1 more source

Ubiquitin and Ubiquitin-Like Modifications of the p53 Family

Neoplasia, 2006
Regulation of p53 by the ubiquitin-proteasomal pathway has been studied considerably. Studies have also demonstrated that the ubiquitin-like proteins SUMO-1 and NEDD8 modify p53. Similarly, p63 and p73 are subject to regulation by ubiquitin and ubiquitin-like modifications, and perturbations of these pathways in the regulation of the p53 family have ...
Ian R. Watson, Meredith S. Irwin
openaire   +3 more sources

FUCA2 Sustains AKT Signaling and Suppresses Senescence by Antagonizing FUT3‐Mediated ErbB3 Fucosylation in Lung Adenocarcinoma

Advanced Science, EarlyView.
ABSTRACT While targeted therapies have improved outcomes in lung adenocarcinoma (LUAD), many patients still lack targetable mutations. Here, we identified alpha‐L‐fucosidase 2 (FUCA2) as a crucial driver of LUAD by preventing cellular senescence. Mechanistically, through the restriction of fucosyltransferase 3 (FUT3)‐mediated α‐1,3‐fucosylation of ...
Lu Chen, Jintao Guo, Fei Li, Mingjie Gao, Runyang Li, Zhaozhang Huang, Yaolin Zheng, Chunyi Gao, Jihuan Hou, Qiang Yu, Bowen Zheng, Xuemei Chen, Wenqing Zhang, Xiaoting Hong, Yali Zheng, Daxuan Wang, Qiyuan Li, Tianhui Hu, Yan‐yan Zhan   +18 more
wiley   +1 more source