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Article

Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster.

PloS one - 10 May 2010

Funakoshi Yoko, Negishi Yuki, Gergen J Peter, Seino Junichi, Ishii Kumiko, Lennarz William J, Matsuo Ichiro, Ito Yukishige, Taniguchi Naoyuki, Suzuki Tadashi

Abstract excerpt

BACKGROUND: Peptide:N-glycanase (PNGase) is an enzyme which releases N-linked glycans from glycopeptides/glycoproteins. This enzyme plays a role in the ER-associated degradation (ERAD) pathway in yeast and mice, but the biological importance of this activity remains unknown. PRINCIPAL FINDINGS: In this study, we characterized the ortholog of cytoplasmic PNGases, PNGase-like (Pngl), in Drosophila melanogaster....

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Identifiers

PMID: 20479940
DOI: 10.1371/journal.pone.0010545
PMCID: PMC2866665

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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