Doppel: More rival than double to prion

@article{Qin2006DoppelMR,
  title={Doppel: More rival than double to prion},
  author={Kang Qin and M. E. O'donnell and Richard Y. Zhao},
  journal={Neuroscience},
  year={2006},
  volume={141},
  pages={1-8}
}
Conversion of normal cellular prion protein to the diseased form plays an essential role in transmissible spongiform encephalopathies such as mad cow disease and Creutzfeldt-Jakob disease. However, the normal physiological function of prion protein remains elusive. Doppel, a German synonym of double, was initially identified as a prion-like protein due to its structural and biochemical similarities. However, emerging evidence suggests that function of prion protein is more antagonistic to… Expand
Prion disease.
  • L. M. Buono
  • Medicine
  • International ophthalmology clinics
  • 2007
TLDR
This work has confirmed that the agent responsible for the transmission of scrapie, a spongiform encephalopathy that affects sheep, is a transmissible particle comprised primarily of protein, and called the specific protein in the prion PrP for protease-resistant protein. Expand
Dividing roles of prion protein in staurosporine-mediated apoptosis.
TLDR
It is demonstrated here that down-regulation of PrPC sensitizes N2a cells to STS-induced cytotoxicity and apoptosis, suggesting that physiological level of endogenous PrPC plays a protective role againstSTS-mediated cellular stress. Expand
Prion diseases - animal health and zoonotic concern: a review
TLDR
Research in last few decades add more to the understanding regarding causative agent, mode of transmission, diagnosis of TSEs, but still there is much more required to be known for appropriate diagnosis and specific treatment of prion diseases. Expand
Coevolution of expression of prion-protein and doppel genes
TLDR
A model of PrP/Dpl coregulation is proposed that includes recruitment of BPTF by USF1, phosphorylation of retinoblastoma protein Rb induced by FAC 1/BPTF followed by E2F1 derepression leading to activation of the PRND promoter. Expand
Prion proteins with pathogenic and protective mutations show similar structure and dynamics.
TLDR
These findings raise the possibility that the pathogenic or dominant negative mutations exert their effects on some non-native intermediate form such as PrP* after conversion of cellular PrP (PrP(C)) into the Pathogenic isoform PrP(Sc) has been initiated. Expand
Characterization of the genomic region containing the Shadow of Prion Protein (SPRN) gene in sheep
TLDR
Annotation of a mini-contig including SPRN suggests conserved linkage between Oari22q24 and Hsap10q26, and the ovine SPRN sequence, described for the first time, shows a high level of homology with the bovine, and to a lesser extent with the human SPRn sequence. Expand
Rodent models for prion diseases.
TLDR
Until today most prion strains can only be propagated and the infectivity content assayed by experimentally challenging conventional or transgenic animals, but the pathogenesis of different transmissible spongiform encephalopathies (TSE) can be analysed systematically by using experimentally infected animals. Expand
Did the first virus self-assemble from self-replicating prion proteins and RNA?
TLDR
The hypothesis that prions are a possible relic of an early stage of peptide evolution is supported, because a capsid originating from prion proteins would be a versatile and effective protection to RNA and could also explain some characteristics of virus self-assembly that are not well understood. Expand
Differential Responses of Neuronal and Spermatogenic Cells to the Doppel Cytotoxicity
Although structurally and biochemically similar to the cellular prion (PrPC), doppel (Dpl) is unique in its biological functions. There are no reports about any neurodegenerative diseases induced byExpand
A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein.
TLDR
The synthesis of the human Dpl peptide fragment hDpl(122-139) (Ac-KPDNKLHQQVLWRLVQEL-NH(2)) and its copper(II) complex species are reported and the significant role played by the aspartic residue in addressing the peptide conformation towards a helical structure is revealed. Expand
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