Ubiquitylation is an essential post-translational modification that regulates intracellular
signalling networks by triggering proteasomal substrate degradation, changing the activity of …

The mitogen-activated protein kinase (MAPK) signaling pathway is the primary regulatory
module of various cellular processes such as cell proliferation, differentiation, and stress …

Protein ubiquitination has become one of the most extensively studied post-translational
modifications. Originally discovered as a critical element in highly regulated proteolysis …

A harmonized balance between positive and negative regulation of pattern recognition
receptor (PRR)-initiated immune responses is required to achieve the most favorable …

The E3 ubiquitin ligase (E3)-mediated ubiquitination and deubiquitinase (DUB)-mediated
deubiquitination processes are closely associated with the occurrence and development of …

Rationale: Understanding the molecular mechanisms of deleterious cardiac remodeling is
important for the development of treatments for heart failure. Recent studies have …

Ubiquitylation is one of the most common post-translational modifications (PTMs) of proteins
that frequently targets substrates for proteasomal degradation. However it can also result in …

Deubiquitylating enzymes (DUBs) maintain relative homeostasis of the cellular ubiquitome
by removing the post‐translational modification ubiquitin moiety from substrates. Numerous …

Innate antiviral immunity is the first line of host defense against invading viral pathogens.
Immunity activation primarily relies on the recognition of pathogen‐associated molecular …

Deubiquitination plays an important role in the regulation of the crosstalk between
macroautophagy/autophagy and innate immune signaling, yet its regulatory mechanisms …