Results 31 to 40 of about 933 (165)
NGLY1 deficiency—A rare congenital disorder of deglycosylation
JIMD Reports, 2020 Pathogenic variants in the NGLY1 gene are associated with a Congenital Disorder of Deglycosylation (CDDG) characterized by delays in reaching developmental milestones, complex hyperkinetic movement disorder, transient elevation of transaminases, and ...
Patrícia Lipari Pinto +6 more
doaj +3 more sources
Stem Cell Research, 2019 NGLY1 deficiency is a rare genetic disease caused by mutations in the NGLY1 gene that encodes N-glycanase 1. The disease phenotype in patient cells is unclear.
Rong Li +11 more
doaj +2 more sources
Liver involvement in NGLY1 congenital disorder of deglycosylation [PDF]
Polish Journal of Pathology, 2020 N-glycanase 1 deficiency is a congenital disorder of deglycosylation, which has been diagnosed in 27 patients, including 2 of them from Poland. The most characteristic symptoms include global developmental disability, hyperkinetic movement disorder, hypo-
Patryk Lipiński +3 more
doaj +3 more sources
An Assay System for Plate-based Detection of Endogenous Peptide:N-glycanase/NGLY1 Activity Using A Fluorescence-based Probe [PDF]
Bio-ProtocolCytosolic peptide: N-glycanase (PNGase/NGLY1 in mammals), an amidase classified under EC:3.5.1.52, is a highly conserved enzyme across eukaryotes that catalyzes the removal of N-glycans from glycoproteins, converting N-glycosylated asparagine residues ...
Hiroto Hirayama, Tadashi Suzuki
doaj +2 more sources
NGLY1 mutation causes neuromotor impairment, intellectual disability, and neuropathy [PDF]
European Journal of Medical Genetics, 2015 N-glycanase 1 (NGLY1) is a conserved enzyme that is responsible for the deglycosylation of misfolded N-glycosylated proteins in the cytoplasm prior to their proteasome-mediated degradation.
Dolen, Duygu +14 more
core +5 more sources
Comprehensive Pan-Cancer Analysis of TRNT1 as a Potential Biomarker for Breast Cancer. [PDF]
J Cell Mol MedABSTRACT TRNT1, an RNA nucleotide transferase, plays a critical role in cellular processes and may be involved in cancer. However, its role in cancer has not been fully explored. This study aims to explore the potential significance of TRNT1 in cancer, particularly in breast cancer (BC) progression and prognosis.
Li X, Meng Y, Gu B.
europepmc +2 more sources
NGLY1 deficiency: Novel patient, review of the literature and diagnostic algorithm [PDF]
JIMD Reports, 2020 Objectives Together with the lysosomal storage diseases, NGLY1 deficiency is a congenital disorder of deglycosylation (NGLY1‐CDDG). Since the first report in 2012, 26 patients have been described. All but one were diagnosed by exome or genome sequencing;
Patryk Lipiński +4 more
doaj +3 more sources
Ever-expanding NGLY1 biology [PDF]
The Journal of Biochemistry, 2021 Abstract The cytosolic peptide:N-glycanase (PNGase; NGLY1 in humans) is a deglycosylating enzyme that is widely conserved in eukaryotes. This enzyme is involved in the degradation of misfolded N-glycoproteins that are destined for proteasomal degradation in the cytosol, a process that is called endoplasmic reticulum-associated ...
Tadashi, Suzuki, Yukiko, Yoshida
openaire +2 more sources
Assay for the peptide:N-glycanase/NGLY1 and disease-specific biomarkers for diagnosing NGLY1 deficiency [PDF]
The Journal of Biochemistry, 2021 Abstract Cytosolic peptide:N-glycanase (NGLY1 in mammals), a highly conserved enzyme in eukaryotes, catalyses the deglycosylation of N-glycans that are attached to glycopeptide/glycoproteins. In 2012, an autosomal recessive disorder related to the NGLY1 gene, which was referred to as NGLY1 deficiency, was reported.
Hirayama, Hiroto, Suzuki, Tadashi
openaire +3 more sources
Ferroptosis regulation by the NGLY1/NFE2L1 pathway [PDF]
Proceedings of the National Academy of Sciences, 2021 Significance Ferroptosis is an oxidative form of cell death whose biochemical regulation remains incompletely understood. Cap’n’collar (CNC) transcription factors including nuclear factor erythroid-2–related factor 1 (NFE2L1/NRF1) and NFE2L2/NRF2 can both regulate oxidative stress pathways but are each regulated in a distinct manner ...
Giovanni C. Forcina +6 more
openaire +2 more sources