Results 51 to 60 of about 232,488 (209)

Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation [PDF]

Seminars in Cell & Developmental Biology, 2007
Endoplasmic reticulum-associated degradation (ERAD) represents the primary means of quality control within the secretory pathway. Critical to this process are ubiquitin protein ligases (E3s) which, together with ubiquitin conjugating enzymes (E2s), mediate the ubiquitylation of proteins targeted for degradation from the ER.
Zlatka, Kostova, Yien Che, Tsai, Allan M, Weissman   +2 more
openaire   +2 more sources

Regulated Inositol‐Requiring Protein 1‐Dependent Decay as a Mechanism of Corin RNA and Protein Deficiency in Advanced Human Systolic Heart Failure [PDF]

, 2014
BACKGROUND: The compensatory actions of the endogenous natriuretic peptide system require adequate processing of natriuretic peptide pro‐hormones into biologically active, carboxyl‐terminal fragments.
Barton, P, Dries, DL, Felkin, LE, Lee, R, Rame, JE, Xu, B   +5 more
core   +1 more source

Endoplasmic Reticulum-Associated Degradation (ERAD)

, 2019
يتم الاحتفاظ بالبروتينات المصنعة حديثًا في الشبكة الإندوبلازمية (ER) حتى اكتمال نضجها. يعد طي البروتين الدقيق أمرًا حيويًا لتحقيق التوازن، ولكن هذه العملية عرضة للخطأ لأنها معقدة كيميائيًا. قد يؤدي الطي الخفيف إلى وجود تكتسب الركام وظيفة سامة أو قد يؤدي إلى فقدان وظيفة البروتين ؛ لذلك، يمكن أن يؤدي طي البروتين إلى العديد من الأمراض.
Burcu Erbaykent Tepedelen, Petek Ballar
openaire   +3 more sources

Ethanol Induced Disordering of Pancreatic Acinar Cell Endoplasmic Reticulum: An ER Stress/Defective Unfolded Protein Response Model. [PDF]

, 2018
Background & aimsHeavy alcohol drinking is associated with pancreatitis, whereas moderate intake lowers the risk. Mice fed ethanol long term show no pancreas damage unless adaptive/protective responses mediating proteostasis are disrupted. Pancreatic
Abrol, Ravinder, Capri, Joseph, Cohn, Whitaker, Faull, Kym F, Freeman, Michael R, Lugea, Aurelia, Pandol, Stephen J, Piplani, Honit, Sakkiah, Sugunadevi, Su, Hsin-Yuan, Waldron, Richard T, Whitelegge, Julian P, Yang, Wei, Zhou, Bo   +13 more
core   +3 more sources

Polycystin-2 is regulated by endoplasmic reticulum-associated degradation [PDF]

Human Molecular Genetics, 2008
Endoplasmic reticulum(ER)-associated degradation (ERAD) is an essential process for cell homeostasis and remains not well understood. During ERAD, misfolded proteins are recognized, ubiquitinated on ER and subsequently retro-translocated/dislocated from ER to the 26S proteasome in the cytosol for proteolytic elimination. Polycystin-2 (PC2), a member of
Genqing, Liang, Qiang, Li, Yan, Tang, Koichi, Kokame, Tadashi, Kikuchi, Guanqing, Wu, Xing-Zhen, Chen   +6 more
openaire   +2 more sources

Obesity Induces Hypothalamic Endoplasmic Reticulum Stress and Impairs Proopiomelanocortin (POMC) Post-translational Processing [PDF]

, 2013
It was shown previously that abnormal prohormone processing or inactive proconverting enzymes that are responsible for this processing cause profound obesity.
Cakir, Isin, Cyr, Nicole E., Litvinov, Bogdan Patedakis, Nillni, Eduardo A., Perello, Mario, Romero, Amparo, Stuart, Ronald C.   +6 more
core   +1 more source

Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation [PDF]

Molecular Cell, 2018
Misfolded proteins in the endoplasmic reticulum (ER) are destroyed by ER-associated degradation (ERAD). Although the retrotranslocation of misfolded proteins from the ER has been reconstituted, how a polypeptide is initially selected for ERAD remains poorly defined.
G Michael, Preston, Christopher J, Guerriero, Meredith B, Metzger, Susan, Michaelis, Jeffrey L, Brodsky   +4 more
openaire   +2 more sources

The AAA-ATPase p97 facilitates degradation of apolipoprotein B by the ubiquitin-proteasome pathways⃞

Journal of Lipid Research, 2008
The ATPase associated with various cellular activities (AAA-ATPase) p97 (p97) has been implicated in the retrotranslocation of target proteins for delivery to the cytosolic proteasome during endoplasmic reticulum-associated degradation (ERAD ...
Eric A. Fisher, Louis R. Lapierre, Robert D. Junkins, Roger S. McLeod   +3 more
doaj   +1 more source

Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery [PDF]

Journal of Biological Chemistry, 2008
Protein misfolding is monitored by a variety of cellular "quality control" systems. Endoplasmic reticulum (ER) quality control handles misfolded secretory and membrane proteins and is well characterized. However, less is known about the quality control of misfolded cytosolic proteins (CytoQC).
Meredith Boyle, Metzger, Matthew J, Maurer, Beverley M, Dancy, Susan, Michaelis   +3 more
openaire   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source