Results 41 to 50 of about 211,577 (291)

An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

Nature Communications, 2017
Protein stability modulation by E3 ubiquitin ligases is an important layer of functional regulation, but screening for E3 ligase-substrate interactions is time-consuming and costly.
Yang Li, Ping Xie, Liang Lu, Jian Wang, Lihong Diao, Zhongyang Liu, Feifei Guo, Yangzhige He, Yuan Liu, Qin Huang, Han Liang, Dong Li, Fuchu He   +12 more
doaj   +1 more source

Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity.

Cell, 2019
The conventional view posits that E3 ligases function primarily through conjugating ubiquitin (Ub) to their substrate molecules. We report here that RIPLET, an essential E3 ligase in antiviral immunity, promotes the antiviral signaling activity of the ...
Cristhian Cadena, Sadeem Ahmad, Audrey Xavier, J. Willemsen, Sehoon Park, Ji Woo Park, Seong-wook Oh, T. Fujita, F. Hou, M. Binder, S. Hur   +10 more
semanticscholar   +1 more source

A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR pathway to regulate neuronal pruning.

PLoS Biology, 2013
Pruning that selectively eliminates unnecessary axons/dendrites is crucial for sculpting the nervous system during development. During Drosophila metamorphosis, dendrite arborization neurons, ddaCs, selectively prune their larval dendrites in response to
Jack Jing Lin Wong, Song Li, Edwin Kok Hao Lim, Yan Wang, Cheng Wang, Heng Zhang, Daniel Kirilly, Chunlai Wu, Yih-Cherng Liou, Hongyan Wang, Fengwei Yu   +10 more
doaj   +1 more source

Prospective discovery of small molecule enhancers of an E3 ligase-substrate interaction

Nature Communications, 2019
Protein–protein interactions (PPIs) governing the recognition of substrates by E3 ubiquitin ligases are critical to cellular function. There is significant therapeutic potential in the development of small molecules that modulate these interactions ...
K. Simonetta, Joshua P. Taygerly, Kathleen A. Boyle, S. Basham, C. Padovani, Yan Lou, T. Cummins, Stephanie L. Yung, Szerenke Kiss von Soly, F. Kayser, J. Kuriyan, M. Rapé, M. Cardozo, M. Gallop, N. Bence, P. Barsanti, Anjanabha Saha   +16 more
semanticscholar   +1 more source

Building ubiquitination machineries: E3 ligase multi-subunit assembly and substrate targeting by PROTACs and molecular glues.

Current Opinion in Structural Biology, 2020
E3 ubiquitin ligase machineries are emerging as attractive therapeutic targets because they confer specificity to substrate ubiquitination and can be hijacked for targeted protein degradation.
S. Ramachandran, A. Ciulli
semanticscholar   +1 more source

Rational Design and Synthesis of HSF1-PROTACs for Anticancer Drug Development

Molecules, 2022
PROTACs employ the proteosome-mediated proteolysis via E3 ligase and recruit the natural protein degradation machinery to selectively degrade the cancerous proteins. Herein, we have designed and synthesized heterobifunctional small molecules that consist
Chiranjeev Sharma, Myeong A Choi, Yoojin Song, Young Ho Seo   +3 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Discovery of Highly Potent and Efficient PROTAC Degraders of Androgen Receptor (AR) by Employing Weak Binding Affinity VHL E3 Ligase Ligands.

Journal of Medicinal Chemistry, 2019
Androgen receptor (AR) is a validated therapeutic target for the treatment of metastatic castration-resistant prostate cancer (mCRPC). We report herein our design, synthesis, and biological characterization of highly potent small-molecule proteolysis ...
Xin-jun Han, Lijie Zhao, Weiguo Xiang, C. Qin, Bukeyan Miao, Tianfeng Xu, Mi Wang, Chao-Yie Yang, Krishnapriya Chinnaswamy, J. Stuckey, Shaomeng Wang   +10 more
semanticscholar   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Novel Inhibitors for MDM2-MDM4 E3 Ligase Potently Induce p53-Indepedent Apoptosis in Drug-Resistant Leukemic Cells

Molecules
MDM2 and MDM4 are major negative regulators of tumor suppressor p53. Beyond regulating p53, MDM2 possesses p53-independent activity in promoting cell cycle progression and tumorigenesis via its RING domain ubiquitin E3 ligase activity. MDM2 and MDM4 form
Rati Lama, Joseph M. Fose, Diana Martín, Inés G. Muñoz, Eunice S. Wang, Pamela J. Sung, Sherry R. Chemler, Xinjiang Wang   +7 more
doaj   +1 more source