Results 31 to 40 of about 525,256 (308)

SUMO conjugation regulates immune signalling

open access: yesFly, 2020
Post-translational modifications (PTMs) are critical drivers and attenuators for proteins that regulate immune signalling cascades in host defence. In this review, we explore functional roles for one such PTM, the small ubiquitin-like modifier (SUMO ...
Sushmitha Hegde   +3 more
doaj   +1 more source

Processing of the ribosomal ubiquitin-like fusion protein FUBI-eS30/FAU is required for 40S maturation and depends on USP36

open access: yeseLife, 2021
In humans and other holozoan organisms, the ribosomal protein eS30 is synthesized as a fusion protein with the ubiquitin-like protein FUBI. However, FUBI is not part of the mature 40S ribosomal subunit and cleaved off by an as-of-yet unidentified ...
Jasmin van den Heuvel   +6 more
doaj   +1 more source

Dss1 is a 26S proteasome ubiquitin receptor [PDF]

open access: yes, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Arrigoni   +35 more
core   +5 more sources

Solo or in Concert: SUMOylation in Pathogenic Fungi [PDF]

open access: yesThe Plant Pathology Journal
SUMOylation plays a pivotal role in DNA replication and repair, transcriptional stability, and stress response. Although SUMOylation is a conserved post-translational modification (PTM) in eukaryotes, the number, type, and function of SUMOylation ...
You-Jin Lim, Yong-Hwan Lee
doaj   +1 more source

Triad3a induces the degradation of early necrosome to limit RipK1-dependent cytokine production and necroptosis. [PDF]

open access: yes, 2018
Understanding the molecular signaling in programmed cell death is vital to a practical understanding of inflammation and immune cell function. Here we identify a previously unrecognized mechanism that functions to downregulate the necrosome, a central ...
A Degterev   +67 more
core   +2 more sources

Ubiquitin Carboxyl-Terminal Hydrolase L1 of Cardiomyocytes Promotes Macroautophagy and Proteostasis and Protects Against Post-myocardial Infarction Cardiac Remodeling and Heart Failure

open access: yesFrontiers in Cardiovascular Medicine, 2022
Ubiquitin carboxyl-terminal hydrolase L1 (UCHL1) is a deubiquitinase known to play essential roles in the nervous tissue. Myocardial upregulation of UCHL1 was observed in human dilated cardiomyopathy and several animal models of heart disease, but the ...
Penglong Wu   +9 more
doaj   +1 more source

Phenotypic Characterization of the Arabidopsis ufm1 (Ubiquitin Fold Modifier) Gene Involved in Seed Development [PDF]

open access: yes, 2016
Background and Objective: With the completion of the Arabidopsis genome sequencing, the next challenge is the determination ofgene function. Post-translational modifications of proteins by small polypeptide are implicated in plant growth and development ...
Cornejo, Paula   +1 more
core   +1 more source

Pathophysiology of Primary Cilia: Signaling and Proteostasis Regulation

open access: yesFrontiers in Cell and Developmental Biology, 2022
Primary cilia are microtubule-based, non-motile sensory organelles present in most types of growth-arrested eukaryotic cells. They are transduction hubs that receive and transmit external signals to the cells in order to control growth, differentiation ...
Emanuela Senatore   +5 more
doaj   +1 more source

The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo [PDF]

open access: yes, 1991
The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however.
Chau, Vincent   +3 more
core  

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

open access: yes, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica   +4 more
core   +3 more sources

Home - About - Disclaimer - Privacy