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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

N-glycanase 1

N-glycanase, PNGase, peptide:N-glycanase
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.[provided by RefSeq, Feb 2009] (from NCBI)
Top mentioned proteins: fibrillin-1, CD45, ACID, CAN, Endo
Papers using N-glycanase antibodies
Metabolic labeling of glycans with azido sugars for visualization and glycoproteomics
Bertozzi Carolyn R. et al., In ACS Chemical Biology, 2005
... -glycosidase F (PNGase F) was obtained from New England Biolabs.
DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis.
Abraham Edathara, In PLoS ONE, 2001
... Restriction enzymes and PNGase F were purchased from New England Biolabs (Ipswich, MA) ...
GRP94 (gp96) and GRP94 N-Terminal Geldanamycin Binding Domain Elicit Tissue Nonrestricted Tumor Suppression
Nicchitta Christopher V. et al., In The Journal of Experimental Medicine, 2000
... -glycosidase F (PNGase-F) was purchased from New England Biolabs, Inc ...
Pregnancy-associated changes in the glycosylation of tamm-horsfall glycoprotein: expression of sialyl lewis sequences on core 2 type o-glycans derived from uromodulin
Hsu Jue-Liang et al., In Journal of Biomedicine and Biotechnology, 1999
... PNGase F was purchased from New England BioLabs (MA, USA) ...
An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database.
Aebersold Ruedi et al., In Genome Biology, 1993
... PNGase F was purchased from New England Biolabs (Beverly, MA, USA) and ...
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Papers on N-glycanase
The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.
Fujihira et al., Wako, Japan. In Gene, Mar 2016
NGLY1/Ngly1 is a cytosolic peptide:N-glycanase, i.e. de-N-glycosylating enzyme acting on N-glycoproteins in mammals, generating free, unconjugated N-glycans and deglycosylated peptides in which the N-glycosylated asparagine residues are converted to aspartates.
Combined albumin and bicarbonate adversely affects equine sperm-oviduct binding.
Van Soom et al., Utrecht, Netherlands. In Reproduction, Feb 2016
Furthermore, N-glycosidase F (PNGase) pretreatment of oviduct explants and APM did not alter sperm-oviduct binding density.
Coupling Effect of Water and Proteoglycans on the In Situ Toughness of Bone.
Jiang et al., San Antonio, United States. In J Bone Miner Res, Jan 2016
To test the hypothesis, we used a novel nanoscratch test to measure the in situ toughness of human cadaveric bone treated with and without PNGase F, an enzyme that specifically removes the N-linked oligosaccharides of GAGs from core proteins.
Novel O-linked methylated glycan antigens decorate secreted immunodominant glycoproteins from the intestinal nematode Heligmosomoides polygyrus.
Hokke et al., Leiden, Netherlands. In Int J Parasitol, Jan 2016
We used MALDI-TOF-MS and LC-MS/MS to analyse the repertoire of N- and O-linked glycans released from Heligmosomoides polygyrus excretory-secretory products by PNGase A and F, β-elimination and hydrazinolysis revealing a broad range of structures including novel methylhexose- and methylfucose-containing glycans.
Rapid Sample Preparation Methodology for Plant N-Glycan Analysis Using Acid-Stable PNGase H(.).
Liu et al., Nanjing, China. In J Agric Food Chem, Jan 2016
The need to analyze N-glycan moieties in a highly parallel manner inspired us to develop a quick N-glycan analysis method based on a recently discovered bacterial protein N-glycanase (PNGase H(+)).
N-Glycosylation analysis of formalin fixed paraffin embedded samples by capillary electrophoresis.
Guttman et al., Debrecen, Hungary. In Electrophoresis, Dec 2015
FFPE samples were first deparaffinized, followed by solubilization in RIPA buffer and treated with PNGase F for N-glycan release.
Gold nanoparticles immobilized hydrophilic monoliths with variable functional modification for highly selective enrichment and on-line deglycosylation of glycopeptides.
Zhang et al., Dalian, China. In Anal Chim Acta, Dec 2015
The poly (glycidyl methacrylate-co-poly (ethylene glycol) diacrylate) monoliths modified with gold nanoparticles, with advantages of enhanced reactive sites, good hydrophilicity and facile modification, were prepared as the matrix, followed by variable functionalization with cysteine and PNGase F for glycopeptide enrichment and on-line deglycosylation respectively.
Structural characterization and biological implications of sulfated N-glycans in a serine protease from the neotropical moth Hylesia metabus (Cramer [1775]) (Lepidoptera: Saturniidae).
González et al., Havana, Cuba. In Glycobiology, Dec 2015
Deglycosylation with PNGase F in the presence of a buffer prepared with 40% H2 (18)O allowed the assignment of an N-glycosylation site.
Highly Efficient Release of Glycopeptides from Hydrazide Beads by Hydroxylamine Assisted PNGase F Deglycosylation for N-Glycoproteome Analysis.
Zou et al., Shanghai, China. In Anal Chem, Nov 2015
Selective enrichment of glycopeptides from complex sample followed by cleavage of N-glycans by PNGase F to expose an easily detectable mark on the former glycosylation sites has become the popular protocol for comprehensive glycoproteome analysis.
Less is More: Membrane Protein Digestion Beyond Urea-Trypsin Solution for Next-level Proteomics.
Zhang, Boston, United States. In Mol Cell Proteomics, Sep 2015
Beyond denaturation, the recent discovery of structure/proteomics omni-compatible detergent n-dodecyl-β-d-maltopyranoside, combined with pepsin and PNGase F columns, enabled breakthroughs in membrane protein digestion: a 2010 DDM-low-TCEP (DLT) method for H/D-exchange (HDX) using human G protein-coupled receptor, and a 2015 flow/detergent-facilitated protease and de-PTM digestions (FDD) for integrative deep sequencing and quantitation using full-length human ion channel complex.
Physiological and molecular functions of the cytosolic peptide:N-glycanase.
Suzuki et al., Japan. In Semin Cell Dev Biol, May 2015
Peptide:N-glycanase (PNGase) is a deglycosylating enzyme that acts on N-glycoproteins.
The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.
Suzuki, Wako, Japan. In J Biochem, 2015
Peptide:N-glycanase (PNGase) is a de-N-glycosylating enzyme that cleaves intact N-glycans from glycoproteins/glycopeptides.
Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans.
Kimura et al., Okayama, Japan. In Front Plant Sci, 2013
These findings suggest that endo-β-N-acetylglucosaminidase (ENGase) must be involved in the production of GN1 type FNGs, whereas only peptide:N-glycanase (PNGase) is involved in the production of GN2 type FNGs.
NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23.
Kato et al., Okazaki, Japan. In Febs Lett, 2012
PNGase-PUB serves not only as p97-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells.
Moore et al., Paris, France. In Plos One, 2009
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.
Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase.
Schindelin et al., Stony Brook, United States. In Glycobiology, 2009
the crystal structure of yeast PNGase in complex with N,N'-diacetylchitobiose (chitobiose).
N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.
Wang et al., Jinan, China. In Plos One, 2008
Dynamic simulations of the wild type and N-terminal H1 deletion mutant implied that Png1p-DeltaH1 is more flexible than wild type Png1p.
Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe.
Qi et al., Jinan, China. In Biochem Biophys Res Commun, 2008
N-terminal alpha-helix of SpPNGase was responsible for the protein-protein interaction. we suggest that the N-terminal alpha-helices of PNGase are derived from evolutionary motif/peptide fusion.
Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
Aebersold et al., Seattle, United States. In Nat Biotechnol, 2003
It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
Conformation-independent binding of monoglucosylated ribonuclease B to calnexin.
Bergeron et al., Montréal, Canada. In Cell, 1997
Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin.
More papers using N-glycanase antibodies
The human Thy-1 gene: structure and chromosomal location
Liu Alvin Y et al., In Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, 1984
... PNGase F was purchased from New England Biolabs (Beverly, MA) and hydrazide ...
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