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http://purl.uniprot.org/citations/25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25605922http://www.w3.org/2000/01/rdf-schema#comment"The cytoplasmic peptide:N-glycanase (PNGase; Ngly1 in mice) is a deglycosylating enzyme involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) process. The precise role of Ngly1 in the ERAD process, however, remains unclear in mammals. The findings reported herein, using mouse embryonic fibroblast (MEF) cells, that the ablation of Ngly1 causes dysregulation of the ERAD process. Interestingly, not only delayed degradation but also the deglycosylation of a misfolded glycoprotein was observed in Ngly1(-/-) MEF cells. The unconventional deglycosylation reaction was found to be catalyzed by the cytosolic endo-β-N-acetylglucosaminidase (ENGase), generating aggregation-prone N-GlcNAc proteins. The ERAD dysregulation in cells lacking Ngly1 was restored by the additional knockout of ENGase gene. Thus, our study underscores the functional importance of Ngly1 in the ERAD process and provides a potential mechanism underlying the phenotypic consequences of a newly emerging genetic disorder caused by mutation of the human NGLY1 gene."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1414593112"xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Huang C."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Dohmae N."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Hosomi A."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Suzuki T.'"xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Harada Y."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Seino J."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Funakoshi Y."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Masahara-Negishi Y."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/author"Fujihira H."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/pages"1398-1403"xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/title"Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells."xsd:string
http://purl.uniprot.org/citations/25605922http://purl.uniprot.org/core/volume"112"xsd:string
http://purl.uniprot.org/citations/25605922http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25605922
http://purl.uniprot.org/citations/25605922http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25605922
http://purl.uniprot.org/uniprot/#_A0A286YCZ7-mappedCitation-25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25605922
http://purl.uniprot.org/uniprot/#_A0A286YDI5-mappedCitation-25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25605922
http://purl.uniprot.org/uniprot/#_E9Q017-mappedCitation-25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25605922
http://purl.uniprot.org/uniprot/#_A0A286YCI0-mappedCitation-25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25605922
http://purl.uniprot.org/uniprot/#_F7CXI4-mappedCitation-25605922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25605922