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Article

Characterization of spontaneously generated prion-like conformers in cultured cells.

Aging - 1 Oct 2011

Zou Roger S, Fujioka Hisashi, Guo Jian-Ping, Xiao Xiangzhu, Shimoji Miyuki, Kong Crystal, Chen Cecilia, Tasnadi Megan, Voma Chesinta, Yuan Jue, Moudjou Mohammed, Laude Hubert, Petersen Robert B, Zou Wen-Quan

Abstract excerpt

A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form characterized by the formation of insoluble aggregates and protease-resistant PrP species termed insoluble...

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Share to Electrophoresis, Gel, Two-Dimensional
Share to Endopeptidase K

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase

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Share to Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase

Share to Prions

Share to Protein Structure, Secondary

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Identifiers

PMID: 21990137
DOI: 10.18632/aging.100370
PMCID: PMC3229973

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