ERp57 in neurodegeneration and regeneration
Leslie Bargsted
Claudio Hetz
Soledad Matus
摘要：The protein disulfide isomerases (PDIs) family has a central function in the folding of proteins synthetized through the secretory pathway.ERp57,also known as Grp58 or PDIA3,is one of the main studied members of this family.ERp57 catalyzes the formation,disruption and isomerization of disulfide bonds of glycoproteins mediated by a cooperative interaction with the endoplasmic reticulum (ER) chaperones calnexin and calreticulin (Turano et al.,2002) (Figure 1A,B).In the past years,several studies have linked ERp57 and its closest homologue PDI (also known as PDIA1) to diseases affecting the central nervous system,including amyotrophic lateral sclerosis (ALS),Parkinson's disease (PD),Alzheimer's disease (AD),among others (Andreu et al.,2012).These neurodegenerative conditions are characterized by the presence of abnormal protein aggregates containing specific proteins,which are now classified as protein misfolding disorders (PMDs) (Hetz and Mollereau,2014).
机标关键词：amyotrophic lateral sclerosiscentral nervous systemendoplasmic reticulumsecretory pathway
资助基金：Millennium Institute (No.P09-015-F,Fondo de Financiamiento de Centros de Investigación en (A)reas Prioritarias (FONDAP) 15150012)the Frick Foundation (No.20014-15,ALS Therapy Alliance 2014-F-059,Muscular Dystrophy Association 382453,Comisión Nacional de Investigación Científica y Tecnológica (CONICYT)CONICYTUSA2013-0003,the Michael J.Fox Foundation for Parkinson's Research No.9277,Fundación Copec-Univer)
论文发表日期：2016-01-01
在线出版日期：2025-08-15（本平台首次上网日期，不代表文献的发表时间）
页数：2( 232-233 )
英文信息