Results 91 to 100 of about 29,730 (229)
British Journal of Pharmacology, EarlyView.Created in BioRender. Schiavone, S. (2026). https://BioRender.com/cy0xq6z. Abstract Background and Purpose Autism spectrum disorders (ASD) are multifactorial neurodevelopmental conditions associated with oxidative stress and neuroinflammation across critical developmental periods.
Vladyslav Sikora +8 more
wiley +1 more source
, 2016 International audienceUbiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
Ewa Blaszczak +5 more
core +1 more source
ELISA Based Protein Ubiquitylation Measurement
Bio-Protocol, 2019 Ubiquitylation is a common post-translational modification of cellular proteins that results in proteasomal and lysosomal degradations. Ubiquitylation is generally measured by methods such as immunoblotting using anti-ubiquitin antibodies after isolating
Yuka Kamada +2 more
doaj +1 more source
From hepatic to hematopoietic: LRH‐1's expanding cellular repertoire to the immune system
The FEBS Journal, EarlyView.The nuclear receptor LRH‐1 is a well‐characterized regulator of endodermal tissue. Yet, increasing evidence indicates that LRH‐1, although expressed at low levels, is also a critical regulator of the hematopoietic system. LRH‐1 regulates the immune system by contributing to immune cell‐specific functions.
Lukas Meisinger +3 more
wiley +1 more source
Phosphorylation of BigH1 regulates its expression pattern and promotes embryonic development
The FEBS Journal, EarlyView.Phosphorylation is a key regulator of the linker histone variant BigH1 during Drosophila embryogenesis. We reveal that N‐terminal phosphorylation promotes the timely removal of BigH1 from chromatin. In contrast, C‐terminal phosphorylation supports early nuclear divisions and embryonic viability.
Ramóna Pék +9 more
wiley +1 more source
Advances in characterizing ubiquitylation sites by mass spectrometry
, 2013 The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell ...
Sylvestersen, K.B. +2 more
core +1 more source
Dimerization of human PARP15 is required for NAD+ binding and automodification
The FEBS Journal, EarlyView.This study provides an integrated structural model of human PARP15. Biophysical, enzymatic, and cell‐based analyses identify the dimer as the active oligomeric state capable of binding the substrate NAD+. A co‐crystal structure with a non‐hydrolyzable substrate analog BAD reveals the molecular basis for the dimerization requirement.
Anna Tuovinen +9 more
wiley +1 more source
Nedd4-2-dependent ubiquitylation and regulation of the cardiac potassium channel hERG1
, 2011 The voltage-gated cardiac potassium channel hERG1 (human ether-à-gogo-related gene 1) plays a key role in the repolarization phase of the cardiac action potential (AP).
Albesa, Maxime +11 more
core +1 more source
Multiple Mechanisms Confining RNA Polymerase II Ubiquitylation to Polymerases Undergoing Transcriptional Arrest [PDF]
, 2005 SummaryIn order to study mechanisms and regulation of RNA polymerase II (RNAPII) ubiquitylation and degradation, highly purified factors were used to reconstitute RNAPII ubiquitylation in vitro.
Jesper Q. Svejstrup +13 more
core +1 more source
Histone ubiquitylation and chromatin dynamics
Frontiers in Bioscience, 2012 Histones are subject to several post-translational modifications, which act to regulate gene expression and other processes on the DNA template. One such modification is the addition of a single ubiquitin moiety, which has been reported to influence chromatin dynamics and exhibit cross-talk with other histone modifications.
Duncan Edward, Wright +2 more
openaire +2 more sources