2009
DOI: 10.1371/annotation/9eb11869-6acb-49b0-978e-abedc3cc545a
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Correction: Interactome Analyses Identify Ties of PrPC and Its Mammalian Paralogs to Oligomannosidic N-Glycans and Endoplasmic Reticulum-Derived Chaperones

Abstract: The physiological environment which hosts the conformational conversion of the cellular prion protein (PrP C ) to diseaseassociated isoforms has remained enigmatic. A quantitative investigation of the PrP C interactome was conducted in a cell culture model permissive to prion replication. To facilitate recognition of relevant interactors, the study was extended to Doppel (Prnd) and Shadoo (Sprn), two mammalian PrP C paralogs. Interestingly, this work not only established a similar physiological environment for… Show more

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Cited by 20 publications
(12 citation statements)
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References 59 publications
(69 reference statements)
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“…The two bands seen here by us could correspond to these two glycosylated forms of Sho, when tagged by EYFP in our N2a cells. The levels of endogenous Sho in N2a cells are known to be below detection limits by Western blot of the cell lysates [21,65] and as also observed by us (data not shown). Contrarily, the endogenous PrP C is well detected in parental N2a (Supplemental Figure S5D) and in transgenic PrP-EGFP (data not shown) cells and appears as multiple bands based on its different glycosylation states ranging between 26 and 42 kDa (Supplemental Figure S5D, lanes 1 and 2), as commonly observed [75,83].…”
Section: Resultssupporting
confidence: 81%
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“…The two bands seen here by us could correspond to these two glycosylated forms of Sho, when tagged by EYFP in our N2a cells. The levels of endogenous Sho in N2a cells are known to be below detection limits by Western blot of the cell lysates [21,65] and as also observed by us (data not shown). Contrarily, the endogenous PrP C is well detected in parental N2a (Supplemental Figure S5D) and in transgenic PrP-EGFP (data not shown) cells and appears as multiple bands based on its different glycosylation states ranging between 26 and 42 kDa (Supplemental Figure S5D, lanes 1 and 2), as commonly observed [75,83].…”
Section: Resultssupporting
confidence: 81%
“…We chose mouse neuroblastoma Neuro-2a (N2a) cells as a model system, since they had widely been used in the past for the study of the biology and conversion of PrP C [79], as well as for mapping the interactome of prion paralogs [21] and, therefore, are bestcharacterized for prion studies. To monitor the two prion family proteins, Shadoo (Sho) and prion protein (PrP), we developed N2a cells stably expressing either of these proteins in fusion with a fluorescent protein tag (EYFP for Sho and EGFP for PrP) at their Ctermini, preceding their GPI-anchor signal peptides (termed Sho-EYFP and PrP-EGFP cells, respectively).…”
Section: Resultsmentioning
confidence: 99%
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“…Notable examples of TSEs include bovine spongiform encephalopathy (BSE), commonly known as mad cow disease; in humans, it is known as new variant Creutzfeldt-Jakob disease (CJD). These disorders are associated with the conversion of the normal cellular prion protein PrP C to its pathogenic isoform PrP Sc (Watts et al, 2009). Prion diseases are characterized by long incubation periods, spongiform changes and the accumulation of misfolded protein deposits.…”
Section: Introductionmentioning
confidence: 99%