Results 11 to 20 of about 9,109,989 (294)

Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. [PDF]

open access: yesPLoS ONE, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Jessica R Blount   +4 more
doaj   +3 more sources

Regulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin [PDF]

open access: yesCells, 2014
Quality control of protein folding inside the endoplasmic reticulum (ER) includes chaperone-mediated assistance in folding and the selective targeting of terminally misfolded species to a pathway called ER-associated protein degradation, or simply ERAD ...
Leticia Lemus, Veit Goder
doaj   +5 more sources

Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.

open access: yesPLoS ONE, 2019
Proteins that misfold in the endoplasmic reticulum (ER) are transported back to the cytosol for ER-associated degradation (ERAD). The Sec61 channel is one of the candidates for the retrograde transport conduit.
Fabio Pereira   +5 more
doaj   +6 more sources

Endoplasmic Reticulum-associated Protein Degradation in Plant Cells

open access: yes, 2006
The endoplasmic reticulum is equipped with a quality control function that retains misfolded and unassembled proteins and allows only structurally mature polypeptides to be transported to their final destination. The retained proteins are eventually retro-translocated to the cytosol and destroyed by a process called endoplasmic reticulum-associated ...
Ceriotti A, Roberts LM
openaire   +4 more sources

Lipid biosynthesis perturbation impairs endoplasmic reticulum-associated degradation. [PDF]

open access: yesJ Biol Chem, 2023
ABSTRACT The relationship between lipid homeostasis and protein homeostasis (proteostasis) is complex and remains incompletely understood. We conducted a screen for genes required for efficient degradation of Deg1 -Sec62, a model aberrant translocon-associated substrate of the ...
Turk SM   +20 more
europepmc   +3 more sources

The kinesin Kar3 is required for endoplasmic reticulum-associated degradation. [PDF]

open access: yesMol Biol Cell
Degradation of aberrant, excess, and regulatory proteins at the endoplasmic reticulum (ER) is a conserved feature of eukaryotic cells, disruption of which contributes to disease. While remarkable progress has been made in recent years, mechanisms and genetic requirements for ER-associated degradation (ERAD) remain incompletely understood.
Akoto E   +16 more
europepmc   +3 more sources

Insights into endoplasmic reticulum‐associated degradation in plants [PDF]

open access: yesNew Phytologist, 2020
SummarySecretory and transmembrane protein synthesis and initial modification are essential processes in protein maturation, and these processes are important for maintaining protein homeostasis in the endoplasmic reticulum (ER). ER homeostasis can be disrupted by the accumulation of misfolded proteins, resulting in ER stress, due to specific intra‐ or
Qian Chen, Feifei Yu, Qi Xie
openaire   +2 more sources

Endoplasmic Reticulum–Associated Degradation and Lipid Homeostasis [PDF]

open access: yesAnnual Review of Nutrition, 2016
The endoplasmic reticulum is the port of entry for proteins into the secretory pathway and the site of synthesis for several important lipids, including cholesterol, triacylglycerol, and phospholipids. Protein production within the endoplasmic reticulum is tightly regulated by a cohort of resident machinery that coordinates the folding, modification ...
Stevenson, Julian   +2 more
openaire   +4 more sources

The Mammalian Endoplasmic Reticulum-Associated Degradation System [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2012
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 deployed to the distal secretory pathway are correctly folded and assembled into native oligomeric complexes.
Olzmann, James A   +2 more
openaire   +4 more sources

Linking chanelopathies with endoplasmic reticulum associated degradation [PDF]

open access: yesChannels, 2017
Bartter syndrome is caused by mutations in several salt-handling channels in the kidney, but the type II variety is particularly severe.
Brighid M, O'Donnell   +2 more
openaire   +2 more sources

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