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Structural Diversity of Ubiquitin E3 Ligase [PDF]

open access: yesMolecules, 2021
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes ...
S. Toma-Fukai, Toshiyuki Shimizu
semanticscholar   +4 more sources

Discovery of E3 Ligase Ligands for Target Protein Degradation

open access: yesMolecules, 2022
Target protein degradation has emerged as a promising strategy for the discovery of novel therapeutics during the last decade. Proteolysis-targeting chimera (PROTAC) harnesses a cellular ubiquitin-dependent proteolysis system for the efficient ...
Jaeseok Lee   +5 more
doaj   +2 more sources

Differential PROTAC substrate specificity dictated by orientation of recruited E3 ligase

open access: yesNature Communications, 2019
PROTACs enable targeted protein degradation by recruiting an E3 ligase to a specific substrate but the determinants of selectivity are not fully understood.
Blake E. Smith   +6 more
doaj   +2 more sources

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity [PDF]

open access: yesNature, 2018
Ubiquitination is initiated by transfer of ubiquitin (Ub) from a ubiquitin-activating enzyme (E1) to a ubiquitin-conjugating enzyme (E2), producing a covalently linked intermediate (E2-Ub) 1 . Ubiquitin ligases (E3s) of the 'really interesting new gene' (RING) class recruit E2-Ub via their RING domain and then mediate direct transfer of ubiquitin to ...
Kuan-Chuan Pao   +9 more
semanticscholar   +4 more sources

E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points

open access: yesFrontiers in Chemistry, 2021
Proteolysis-targeting chimeras (PROTACs) have received tremendous attention as a new and exciting class of therapeutic agents that promise to significantly impact drug discovery.
Aleša Bricelj   +4 more
doaj   +2 more sources

Discovery of small molecule ligands for the von Hippel-Lindau (VHL) E3 ligase and their use as inhibitors and PROTAC degraders

open access: yesChemical Society Reviews, 2022
The von Hippel-Lindau (VHL) Cullin RING E3 ligase is an essential enzyme in the ubiquitin-proteasome system that recruits substrates such as the hypoxia inducible factor for ubiquitination and subsequent proteasomal degradation.
Claudia J Diehl, A. Ciulli
semanticscholar   +1 more source

Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer

open access: yesPathology and Oncology Research, 2023
Gastric cancer (GC) is one of the most pernicious gastrointestinal tumors with extraordinarily high incidence and mortality. Ubiquitination modification of cellular signaling proteins has been shown to play important roles in GC tumorigenesis ...
Aiqin Sun   +5 more
doaj   +1 more source

Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory.

open access: yesAnnual Review of Biochemistry, 2022
Methods to direct the degradation of protein targets with proximity-inducing molecules that coopt the cellular degradation machinery are advancing in leaps and bounds, and diverse modalities are emerging.
A. Cowan, A. Ciulli
semanticscholar   +1 more source

A non‐canonical scaffold‐type E3 ligase complex mediates protein UFMylation

open access: yesEMBO Journal, 2022
Protein UFMylation, i.e., post‐translational modification with ubiquitin‐fold modifier 1 (UFM1), is essential for cellular and endoplasmic reticulum homeostasis.
J. Peter   +8 more
semanticscholar   +1 more source

Differential requirement for BRCA1-BARD1 E3 ubiquitin ligase activity in DNA damage repair and meiosis in the Caenorhabditis elegans germ line.

open access: yesPLoS Genetics, 2023
The tumor suppressor BRCA1-BARD1 complex regulates many cellular processes; of critical importance to its tumor suppressor function is its role in genome integrity.
Qianyan Li   +4 more
doaj   +1 more source

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