PNG1/YPL096W Literature Guide Help

Other names published for PNG1: YPL096W

PNG1 - Function/Process (21)

ReferenceOther Genes Addressed
Wang S, et al.  (2012) Development of a method for the efficient release of N-glycans from glycoproteins generating native deglycosylated proteins. Enzyme Microb Technol 51(3):139-42
Kario E, et al.  (2011) A New Autophagy-related Checkpoint in the Degradation of an ERAD-M Target. J Biol Chem 286(13):11479-91
Hosomi A, et al.  (2010) Identification of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) Pathway in Saccharomyces cerevisiae: APPLICATION OF A NOVEL ASSAY FOR GLYCOPROTEIN ERAD. J Biol Chem 285(32):24324-34
Wang S, et al.  (2009) N-terminal deletion of Peptide:N-glycanase results in enhanced deglycosylation activity. PLoS One 4(12):e8335
Zhao G, et al.  (2009) Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase. Glycobiology 19(2):118-125
Wang S, et al.  (2007) Influence of Substrate Conformation on the Deglycosylation of Ribonuclease B by Recombinant Yeast Peptide:N-glycanase. Acta Biochim Biophys Sin (Shanghai) 39(1):8-14
Witte MD, et al.  (2007) Bodipy-VAD-Fmk, a useful tool to study yeast peptide N-glycanase activity. Org Biomol Chem 5(22):3690-7
Kim I, et al.  (2006) The Png1-Rad23 complex regulates glycoprotein turnover. J Cell Biol 172(2):211-9
Suzuki T, et al.  (2006) Site-specific labeling of cytoplasmic peptide:N-glycanase by N,N'-diacetylchitobiose-related compounds. J Biol Chem 281(31):22152-60
Joshi S, et al.  (2005) Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase mediated deglycosylation. FEBS Lett 579(3):823-6
Suzuki T  (2005) A simple, sensitive in vitro assay for cytoplasmic deglycosylation by peptide: N-glycanase. Methods 35(4):360-5
Biswas S, et al.  (2004) The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23. Biochem Biophys Res Commun 323(1):149-55
Hirsch C, et al.  (2004) Yeast N-glycanase distinguishes between native and non-native glycoproteins. EMBO Rep 5(2):201-6
Misaghi S, et al.  (2004) Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem Biol 11(12):1677-87
Chantret I, et al.  (2003) Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Biochem J 373(Pt 3):901-8
Hirsch C, et al.  (2003) A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J 22(5):1036-46
Katiyar S, et al.  (2002) Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation. J Biol Chem 277(15):12953-9
van Laar T, et al.  (2002) A role for Rad23 proteins in 26S proteasome-dependent protein degradation? Mutat Res 499(1):53-61
Suzuki T, et al.  (2001) Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast. J Biol Chem 276(24):21601-7
Suzuki T, et al.  (2000) PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. J Cell Biol 149(5):1039-52
Suzuki T, et al.  (1998) Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J Biol Chem 273(34):21526-30