ArticleProceedings of the National Academy of Sciences of the United States of America2001
Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 101 citations in OpenAlex.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Regulation of PD-L1 Protein Expression by the E3 Ubiquitin Ligase GP78.Current issues in molecular biology · 2025Article
- Article
- Landscape of protein-protein interactions during hepatitis C virus assembly and release.Microbiology spectrum · 2024Article
- RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.bioRxiv : the preprint server for biology · 2023Article
- An in vivo drug repurposing screen and transcriptional analyses reveals the serotonin pathway and GSK3 as major therapeutic targets for NGLY1 deficiency.PLoS genetics · 2022Article
- A method for assaying peptide: N-glycanase/N-glycanase 1 activities in crude extracts using an N-glycosylated cyclopeptide.Glycobiology · 2022Article
- Glycoproteome remodeling in MLL-rearranged B-cell precursor acute lymphoblastic leukemia.Theranostics · 2021Article
- AeLife · 2020Article
- Orthopaedic phenotyping of NGLY1 deficiency using an international, family-led disease registry.Orphanet journal of rare diseases · 2019Article
- Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins.Scientific reports · 2019Article
- Physiological and pathophysiological characteristics of ataxin-3 isoforms.The Journal of biological chemistry · 2019Article
- Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene.PLoS genetics · 2017Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathway.Genetics in medicine : official journal of the American College of Medical Genetics · 2014Article
- ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase.Histochemistry and cell biology · 2014Article
- Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.PloS one · 2012Article
- Importin beta interacts with the endoplasmic reticulum-associated degradation machinery and promotes ubiquitination and degradation of mutant alpha1-antitrypsin.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Peptide:N-glycanase (PNGase) cleaves oligosaccharide chains from glycopeptides and glycoproteins. Recently the deduced amino acid sequence of a cytoplasmic PNGase has been identified in various eukaryotes ranging from yeast to mammals, suggesting that deglycosylation may play a central role in some catabolic process. Several lines of evidence indicate that the cytoplasmic enzyme is involved in the quality control system for newly synthesized glycoproteins. Two-hybrid library screening by using mouse PNGase as the target yielded several PNGase-interacting proteins that previously had been implicated in proteasome-dependent protein degradation: mHR23B, ubiquitin, a regulatory subunit of the 19S proteasome, as well as a protein containing an ubiquitin regulatory motif (UBX) and an ubiquitin-associated motif (UBA). These findings by using the two-hybrid system were further confirmed either by in vitro binding assays or size fractionation assays. These results suggest that PNGase may be required for efficient proteasome-mediated degradation of misfolded glycoproteins in mammalian cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.