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Our prospective phenotyping expands the clinical spectrum of NGLY1-CDDG, offers prognostic information, and provides baseline data for evaluating therapeutic interventions
The patients with NGLY1 deficiency show developmental delay, seizures, peripheral neuropathy, abnormal liver function and alacrima.
This review summarizes the research history of cytoplasmic PNGase.
NGLY1 mutation causes neuromotor impairment, intellectual disability, and neuropathy
Data indicate that N-glycanase 1 (NGLY1) deficiency is a novel autosomal recessive disorder of the endoplasmic reticulum-associated degradation pathway associated with neurological dysfunction, abnormal tear production, and liver disease.
PNGase-PUB serves not only as p97 (show EIF4G2 Proteins)-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
As the generation of the bulk of fOS is unaffected by co-down regulation of Ngly1p and Engase1p, alternative quantitatively important mechanisms must underlie the liberation of these fOS from either LLO or glycoproteins during protein N-glycosylation.
the PUB domain functions as a p97 (show EIF4G2 Proteins) binding module in human peptide N-glycanase
generation of an HLA-A*0201-associated epitope from tyrosinase (show TYR Proteins) with deamidation of Asn to Asp (show ASIP Proteins) is dependent on glycosylation in the endoplasmic reticulum (ER), and subsequent deglycosylation by peptide-N-glycanase in the cytosol
Describes the function of Yeast PNG1 and identifies similar proteins in mouse, human, D. melanogaster, C. elegans, and S. pombe.
These observations strongly suggest that the Ngly1- or Ngly1/Engase (show ENGASE Proteins)-deficient mice could serve as a valuable animal model for studies related to the pathogenesis of the NGLY1-deficiency, and that cytoplasmic ENGase (show ENGASE Proteins) represents one of the potential therapeutic targets for this genetic disorder.
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
Data show that both the yeast PNG1 enzyme and its mammalian homolog display N-glycanase activity towards intact glycoproteins.
results suggested two possible pathways for the interaction between mPNGase and the proteasome; in one, mHR23B (show RAD23B Proteins) mediates the interaction between mPNGase and the proteasome; in an alternative pathway, mPNGase directly binds to the proteasome subunit, mS4
The crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B (show RAD23B Proteins) is described; the results suggest a co-evolution of ER-associated degradation and DNA repair pathways.
cytoplasmic protein (show BLZF1 Proteins) mouse p97 (show EIF4G2 Proteins)(mp97) participates in the formation of a ternary complex containing mouse autocrine motility factor receptor (show AMFR Proteins) (mAMFR), mp97, and peptide N-glycanase
enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins
crystal structure of the N-terminal domain of PNGase in complex with this motif provides detailed insight into the interaction between p97 (show EIF4G2 Proteins) and its substrate-processing cofactors
The plant PNGase facilitates ERAD through its deglycosylation activity, while the catalytic mutant of AtPNG1 impair glycoprotein ERAD by binding to N-glycans on the ERAD substrates.
the AtPng1p gene product acts as a transglutaminase; the first reported plant protein, characterized at molecular level showing TGase (show TGM1 Proteins) activity. [AtPng1p]
AtPng1p, the first plant transglutaminase sequenced shows undetectable sequence homology to the animal enzymes, except for the catalytic triad. It is, however, endowed with a calcium-dependent activity that allowed us to build a three-dimensional model.
Caenorhabditis elegans PNG-1 exhibits dual enzyme functions, not only as PNGase but also as an oxidoreductase (show HSD17B6 Proteins) (thioredoxin).
Authors show a developmental role for a PNGase and Rad-23 in the regulation of neuronal branching during organ innervation.
This gene encodes an enzyme that catalyzes hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl) asparagine residue to N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. The encoded enzyme may play a role in the proteasome-mediated degradation of misfolded glycoproteins. Multiple transcript variants encoding different isoforms have been found for this gene.
peptide-N(4)-(N-acetyl-beta-glucosaminyl) asparagine amidase
, N-glycanase 1
, Peptide-N4-N-acetyl-beta-glucosaminylasparagine amidase
, peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
, peptide N-glycanase homolog
, potential de-N-glycosylation enzyme