Results 41 to 50 of about 232,488 (209)

Endoplasmic Reticulum Quality Control in Immune Cells

Frontiers in Cell and Developmental Biology, 2021
The endoplasmic reticulum quality control (ERQC) system, including endoplasmic reticulum-associated degradation (ERAD), the unfolded protein response (UPR), and autophagy, presides over cellular protein secretion and maintains proteostasis in mammalian ...
Yalan Jiang, Zehua Tao, Hua Chen, Sheng Xia   +3 more
doaj   +1 more source

SGTA regulates the cytosolic quality control of hydrophobic substrates [PDF]

, 2014
Hydrophobic amino acids are normally shielded from the cytosol and their exposure is often used as an indicator of protein misfolding to enable the chaperone-mediated recognition and quality control of aberrant polypeptides.
High, Stephen, Leznicki, Pawel, Payapilly, Aishwarya, Wunderley, Lydia   +3 more
core   +10 more sources

Effects of oxidative stress on the solubility of HRD1, a ubiquitin ligase implicated in Alzheimer's disease.

PLoS ONE, 2014
The E3 ubiquitin ligase HRD1 is found in the endoplasmic reticulum membrane of brain neurons and is involved in endoplasmic reticulum-associated degradation. We previously demonstrated that suppression of HRD1 expression in neurons causes accumulation of
Ryo Saito, Masayuki Kaneko, Yoshihisa Kitamura, Kazuyuki Takata, Koichi Kawada, Yasunobu Okuma, Yasuyuki Nomura   +6 more
doaj   +1 more source

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain [PDF]

, 2013
The plant cytotoxin ricin enters mammalian cells by receptor-mediated endocytosis, undergoing retrograde transport to the endoplasmic reticulum (ER) where its catalytic A chain (RTA) is reductively separated from the holotoxin to enter the cytosol and ...
Afshar, Allen, Argent, Bays, Bellisola, Blum, Braun, Brodsky, Carvalho, Cascio, Craiu, David M. Roberts, Deeks, Elkabetz, Endo, Fiani, Fleming, Fu, Gallastegui, Giodini, Groll, Hartley, Hazes, Heiligenstein, Heinemeyer, Hendil, Holmberg, Hudson, Husnjak, J. Michael Lord, Jarosch, Jin, Jonathan P. Cook, Kohler, Lam, Li, Li, Lipson, Lundgren, Lynne M. Roberts, May, Mayerhofer, Nishi Vasisht, Paola Pietroni, Rabinovich, Rasmus Hartmann-Petersen, Redmann, Robert A. Spooner, Rubin, Sandvig, Schreiner, Sokolowska, Spooner, Spooner, Spooner, Spooner, Strickland, Surjit, Unno, van Nocker, Wesche, Ye   +61 more
core   +2 more sources

The Endoplasmic Reticulum-Associated Degradation Pathways of Budding Yeast [PDF]

Cold Spring Harbor Perspectives in Biology, 2012
Protein misfolding is a common cellular event that can produce intrinsically harmful products. To reduce the risk, quality control mechanisms are deployed to detect and eliminate misfolded, aggregated, and unassembled proteins. In the secretory pathway, it is mainly the endoplasmic reticulum-associated degradation (ERAD) pathways that perform this role.
Guillaume, Thibault, Davis T W, Ng
openaire   +2 more sources

Adapter-mediated Substrate Selection for Endoplasmic Reticulum-associated Degradation [PDF]

Journal of Biological Chemistry, 2009
During endoplasmic reticulum (ER)-associated degradation (ERAD), a relatively small number of ubiquitin ligases (E3) must be capable of ubiquitinating an assortment of substrates diverse in both structure and location (ER lumen, membrane, and/or cytosol).
Kathleen, Corcoran, Xiaoli, Wang, Lonnie, Lybarger   +2 more
openaire   +2 more sources

Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response [PDF]

, 2017
Background: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response (UPR).
Bulleid, Neil J., Cain, Katharine, Chalmers, Fiona, Sweeney, Bernadette, van Lith, Marcel   +4 more
core   +2 more sources

One step at a time: endoplasmic reticulum-associated degradation [PDF]

Nature Reviews Molecular Cell Biology, 2008
Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC) mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the secretory pathway, whereas non-native and unassembled subunits of multimeric proteins are degraded by the ER-associated degradation (ERAD) pathway.
Shruthi S, Vembar, Jeffrey L, Brodsky
openaire   +2 more sources

Regulation of podocyte survival and endoplasmic reticulum stress by fatty acids and its modification by Stearoyl-CoA desaturases and cyclic AMP [PDF]

, 2011
Podocyte apoptosis is a hallmark in the development and progression of diabetic nephropathy (DN). Several factors of the diabetic milieu are known to induce podocyte apoptosis. Currently, the role of free fatty acids (FFAs) for podocytopathy and podocyte
Sieber, Jonas
core   +1 more source

Endoplasmic reticulum-associated degradation: exceptions to the rule

European Journal of Cell Biology, 2004
Quality control mechanisms in the endoplasmic reticulum (ER) ensure that misfolded proteins are recognized and targeted for degradation. According to the current view of ER-associated degradation (ERAD), the degradation does not occur in the ER itself but requires the retrotranslocation of the proteins to the cytosol where they are degraded by ...
Anton, Schmitz, Volker, Herzog
openaire   +2 more sources