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Article

Removal of the glycosylation of prion protein provokes apoptosis in SF126.

Journal of biochemistry and molecular biology - 30 Sept 2007

Chen Lan, Yang Yang, Han Jun, Zhang Bao-Yun, Zhao Lin, Nie Kai, Wang Xiao-Fan, Li Feng, Gao Chen, Dong Xiao-Ping, Xu Cai-Min

Abstract excerpt

Although the function of cellular prion protein (PrPc) and the pathogenesis of prion diseases have been widely described, the mechanisms are not fully clarified. In this study, increases of the portion of non-glycosylated prion protein deposited in the hamster brains infected with scrapie strain 263K were described. To elucidate the pathological role of glycosylation profile of PrP, wild type human PrP (HuPrP)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17927898
DOI: 10.5483/bmbrep.2007.40.5.662

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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