<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">van Ham, Tjakko J</style></author><author><style face="normal" font="default" size="100%">Holmberg, Mats A</style></author><author><style face="normal" font="default" size="100%">van der Goot, Annemieke T</style></author><author><style face="normal" font="default" size="100%">Teuling, Eva</style></author><author><style face="normal" font="default" size="100%">Garcia-Arencibia, Moises</style></author><author><style face="normal" font="default" size="100%">Kim, Hyun-eui</style></author><author><style face="normal" font="default" size="100%">Du, Deguo</style></author><author><style face="normal" font="default" size="100%">Thijssen, Karen L</style></author><author><style face="normal" font="default" size="100%">Wiersma, Marit</style></author><author><style face="normal" font="default" size="100%">Burggraaff, Rogier</style></author><author><style face="normal" font="default" size="100%">van Bergeijk, Petra</style></author><author><style face="normal" font="default" size="100%">van Rheenen, Jeroen</style></author><author><style face="normal" font="default" size="100%">Jerre van Veluw, G</style></author><author><style face="normal" font="default" size="100%">Hofstra, Robert M W</style></author><author><style face="normal" font="default" size="100%">Rubinsztein, David C</style></author><author><style face="normal" font="default" size="100%">Nollen, Ellen A A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity.</style></title><secondary-title><style face="normal" font="default" size="100%">Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">alpha-Synuclein</style></keyword><keyword><style  face="normal" font="default" size="100%">Amyloid beta-Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line, Tumor</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Nerve Tissue Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Neurodegenerative Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">08/2010</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">142</style></volume><pages><style face="normal" font="default" size="100%">601-12</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Fibrillar protein aggregates are the major pathological hallmark of several incurable, age-related, neurodegenerative disorders. These aggregates typically contain aggregation-prone pathogenic proteins, such as amyloid-beta in Alzheimer&#039;s disease and alpha-synuclein in Parkinson&#039;s disease. It is, however, poorly understood how these aggregates are formed during cellular aging. Here we identify an evolutionarily highly conserved modifier of aggregation, MOAG-4, as a positive regulator of aggregate formation in C. elegans models for polyglutamine diseases. Inactivation of MOAG-4 suppresses the formation of compact polyglutamine aggregation intermediates that are required for aggregate formation. The role of MOAG-4 in driving aggregation extends to amyloid-beta and alpha-synuclein and is evolutionarily conserved in its human orthologs SERF1A and SERF2. MOAG-4/SERF appears to act independently from HSF-1-induced molecular chaperones, proteasomal degradation, and autophagy. Our results suggest that MOAG-4/SERF regulates age-related proteotoxicity through a previously unexplored pathway, which will open up new avenues for research on age-related, neurodegenerative diseases.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">&lt;p&gt;http://www.ncbi.nlm.nih.gov/pubmed/20723760?dopt=Abstract&lt;/p&gt;
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