Results 21 to 30 of about 232,488 (209)

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

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

Translational balancing questioned: Unaltered glycosylation during disulfiram treatment in mannosyl‐oligosaccharide alpha‐1,2‐mannnosidase‐congenital disorders of glycosylation (MAN1B1‐CDG)

open access: yesJIMD Reports, 2021
MAN1B1‐CDG is a multisystem disorder caused by mutations in MAN1B1, encoding the endoplasmic reticulum mannosyl‐oligosaccharide alpha‐1,2‐mannnosidase. A defect leads to dysfunction within the degradation of misfolded glycoproteins.
Lisa Kemme   +8 more
doaj   +1 more source

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

Membrane-associated RING ubiquitin ligase RNF-121 and advancement of cancer [PDF]

open access: yesCellular, Molecular and Biomedical Reports
Exploration of E3 ubiquitin ligases as potential therapeutic targets has been ongoing for two to three decades. Various chemicals and drugs have been developed to either upregulate or inhibit the activity of E3 ligases, aiming to mitigate several ...
Somesh Roy
doaj   +1 more source

Identification of endoplasmic reticulum stress response genes in homologous vs. heterologous asf infections in vitro

open access: yesActa Veterinaria, 2023
The endoplasmic reticulum (ER) is crucial for the production, processing and transport of proteins. Infection with pathogens activates Unfolded Protein Response (UPR), which can lead to their survival/replication or elimination from the body.
Kholod Natalia   +3 more
doaj   +1 more source

Ricin trafficking in plant and mammalian cells [PDF]

open access: yes, 2011
Ricin is a heterodimeric plant protein that is potently toxic to mammalian and many other eukaryotic cells. It is synthesized and stored in the endosperm cells of maturing Ricinus communis seeds (castor beans).
Lord, Mike, Spooner, Robert A.
core   +2 more sources

Novel Functions of Ubiquitin Ligase HRD1 With Transmembrane and Proline-Rich Domains

open access: yesJournal of Pharmacological Sciences, 2008
Human ubiquitin ligase HRD1 is involved in endoplasmic reticulum-associated degradation (ERAD). We recently reported that HRD1 interacts with Parkin-associated endothelin receptor-like receptor (Pael-R), a substrate of Parkin, and promotes Pael-R ...
Tomohiro Omura   +7 more
doaj   +1 more source

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

open access: yes, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica   +4 more
core   +3 more sources

Amino acid sequences within the β1 domain of human apolipoprotein B can mediate rapid intracellular degradation

open access: yesJournal of Lipid Research, 2004
Apolipoprotein B (apoB)-48 contains a region termed the β1 domain that is predicted to be composed of extensive amphipathic β-strands. Analysis of truncated apoB variants revealed that sequences between the carboxyl termini of apoB-37 and apoB-42 ...
Louis R. Lapierre   +4 more
doaj   +1 more source

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