Endoplasmic reticulum (ER)-associated degradation (ERAD) is a universally important process among eukaryotic cells. ERAD is necessary to preserve cell integrity since the accumulation of defective proteins results in diseases associated with neurological dysfunction, cancer, and infections. This process involves recognition of misfolded or misassembled proteins that have been translated in association with ER membranes. Recognition of ERAD substrates leads to their extraction through the ER membrane (retrotranslocation or dislocation), ubiquitination, and destruction by cytosolic proteasomes. This review focuses on ERAD and its components as well as how viruses use this process to promote their replication and to avoid the immune response
The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER protein homeos...
Protein homeostasis is maintained through a balance among protein synthesis, folding, assembly and d...
In eukaryotic cells terminally misfolded proteins of the secretory pathway are retarded in the endop...
Endoplasmic reticulum-associated degradation (ERAD) is a universally important process among eukaryo...
Endoplasmic reticulum-associated degradation (ERAD) is highly conserved in yeast. Recent studies hav...
The endoplasmic reticulum-associated degradation pathway, ERAD, is an important mechanism for mainta...
Endoplasmic reticulum (ER)-associated protein degradation (ERAD) eliminates misfolded or unassembled...
Introduction: The endoplasmic-reticulum-associated protein degradation (ERAD) pathway plays an impor...
ER-associated degradation (ERAD) is a mechanism by which numerous ER-localized proteins are targeted...
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic prote...
Proteins are co-translationally inserted into the endoplasmic reticulum (ER) where they undergo matu...
In this review, we focus on the ubiquitination process within the endoplasmic reticulum associated p...
Maintaining proteome integrity is essential for long-term viability of all organisms and is overseen...
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic prote...
Proteins that fail to fold properly as well as constitutive or regulated short-lived proteins of the...
The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER protein homeos...
Protein homeostasis is maintained through a balance among protein synthesis, folding, assembly and d...
In eukaryotic cells terminally misfolded proteins of the secretory pathway are retarded in the endop...
Endoplasmic reticulum-associated degradation (ERAD) is a universally important process among eukaryo...
Endoplasmic reticulum-associated degradation (ERAD) is highly conserved in yeast. Recent studies hav...
The endoplasmic reticulum-associated degradation pathway, ERAD, is an important mechanism for mainta...
Endoplasmic reticulum (ER)-associated protein degradation (ERAD) eliminates misfolded or unassembled...
Introduction: The endoplasmic-reticulum-associated protein degradation (ERAD) pathway plays an impor...
ER-associated degradation (ERAD) is a mechanism by which numerous ER-localized proteins are targeted...
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic prote...
Proteins are co-translationally inserted into the endoplasmic reticulum (ER) where they undergo matu...
In this review, we focus on the ubiquitination process within the endoplasmic reticulum associated p...
Maintaining proteome integrity is essential for long-term viability of all organisms and is overseen...
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic prote...
Proteins that fail to fold properly as well as constitutive or regulated short-lived proteins of the...
The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER protein homeos...
Protein homeostasis is maintained through a balance among protein synthesis, folding, assembly and d...
In eukaryotic cells terminally misfolded proteins of the secretory pathway are retarded in the endop...