Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration
The endoplasmic reticulum (ER) is a dynamic intracellular organelle with multiple functions
essential for cellular homeostasis, development, and stress responsiveness. In response to …
essential for cellular homeostasis, development, and stress responsiveness. In response to …
The mammalian endoplasmic reticulum-associated degradation system
JA Olzmann, RR Kopito… - Cold Spring Harbor …, 2013 - cshperspectives.cshlp.org
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic
proteome and is accordingly endowed with specialized machinery to ensure that proteins …
proteome and is accordingly endowed with specialized machinery to ensure that proteins …
Protein folding and quality control in the ER
K Araki, K Nagata - Cold Spring Harbor perspectives in …, 2011 - cshperspectives.cshlp.org
The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER
quality control (ERQC) system. The ERQC facilitates folding and modification of secretory …
quality control (ERQC) system. The ERQC facilitates folding and modification of secretory …
Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants
The endoplasmic reticulum (ER) has a sophisticated quality control (QC) system to eliminate
improperly folded proteins from the secretory pathway. Given that protein folding is such a …
improperly folded proteins from the secretory pathway. Given that protein folding is such a …
In and out of the ER: protein folding, quality control, degradation, and related human diseases
DN Hebert, M Molinari - Physiological reviews, 2007 - journals.physiology.org
A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …
N-glycan structures: recognition and processing in the ER
M Aebi, R Bernasconi, S Clerc, M Molinari - Trends in biochemical …, 2010 - cell.com
The processing of N-linked glycans determines secretory protein homeostasis in the
eukaryotic cell. Folding and degradation of glycoproteins in the endoplasmic reticulum (ER) …
eukaryotic cell. Folding and degradation of glycoproteins in the endoplasmic reticulum (ER) …
N-linked sugar-regulated protein folding and quality control in the ER
A Tannous, GB Pisoni, DN Hebert, M Molinari - Seminars in cell & …, 2015 - Elsevier
Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized
in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the …
in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the …
The proteasomal system
T Jung, B Catalgol, T Grune - Molecular aspects of medicine, 2009 - Elsevier
Rising interest in the mechanism and function of the proteasomes and the ubiquitin system
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …
The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation
GM Preston, JL Brodsky - Biochemical Journal, 2017 - portlandpress.com
The endoplasmic reticulum (ER) serves as a warehouse for factors that augment and control
the biogenesis of nascent proteins entering the secretory pathway. In turn, this compartment …
the biogenesis of nascent proteins entering the secretory pathway. In turn, this compartment …
The ubiquitylation machinery of the endoplasmic reticulum
C Hirsch, R Gauss, SC Horn, O Neuber, T Sommer - Nature, 2009 - nature.com
As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains
newly synthesized polypeptides and supports their maturation. Only properly folded proteins …
newly synthesized polypeptides and supports their maturation. Only properly folded proteins …