Results 11 to 20 of about 248,165 (360)
Structural Diversity of Ubiquitin E3 Ligase [PDF]
Molecules, 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 ...
Sachiko Toma-Fukai, Toshiyuki Shimizu
doaj +4 more sources
A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders
Frontiers in Genetics, 2018 Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George +4 more
doaj +2 more sources
Identification of E3 Ubiquitin Ligase Substrates Using Biotin Ligase-Based Proximity Labeling Approaches [PDF]
BiomedicinesUbiquitylation is a post-translational modification originally identified as the first step in protein degradation by the ubiquitin–proteasome system. Ubiquitylation is also known to regulate many cellular processes without degrading the ubiquitylated ...
Koji Matsuhisa +2 more
doaj +2 more sources
Ub-POD: A Ubiquitin-Specific Proximity-Dependent Labeling Technique to Identify E3 Ubiquitin Ligase Substrates in Human Cells [PDF]
Bio-ProtocolUbiquitination is a post-translational protein modification that regulates a vast majority of processes during protein homeostasis. The covalent attachment of ubiquitin is a highly regulated process carried out by the sequential action of the three ...
Urbi Mukhopadhyay +3 more
doaj +2 more sources
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Nature, 2015 Protein aggregates and damaged organelles are tagged with ubiquitin chains to trigger selective autophagy. To initiate mitophagy, the ubiquitin kinase PINK1 phosphorylates ubiquitin to activate the ubiquitin ligase parkin, which builds ubiquitin chains ...
Michael Lazarou +2 more
exaly +2 more sources
HERC Ubiquitin Ligases in Cancer [PDF]
Cancers, 2020 HERC proteins are ubiquitin E3 ligases of the HECT family. The HERC subfamily is composed of six members classified by size into large (HERC1 and HERC2) and small (HERC3–HERC6). HERC family ubiquitin ligases regulate important cellular processes, such as neurodevelopment, DNA damage response, cell proliferation, cell migration, and immune responses ...
Joan Sala-Gaston +7 more
openaire +4 more sources
Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer
Pathology 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
Ubiquitin ligases and beyond [PDF]
BMC Biology, 2012 In a review published in 2004 [1] and that still repays reading today, Cecile Pickart traced the evolution of research on ubiquitination from its origins in the proteasomal degradation of proteins through the revelation that it has a central role in cell cycle regulation and the recognition of regulatory roles for ubiquitin in intracellular membrane ...
Đikić, Ivan, Robertson, Miranda
openaire +6 more sources
Ubiquitin-protein ligases [PDF]
Journal of Cell Science, 2004 Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
Philip A. Robinson, H. C. Ardley
openaire +3 more sources
Biomolecules, 2021 Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome ...
Rebeca Ibarra +4 more
doaj +1 more source