Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration.
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The Cellular Prion Protein: A Player in Immunological QuiescencePrion protein paralog doppel protein interacts with alpha-2-macroglobulin: a plausible mechanism for doppel-mediated neurodegenerationFunctionally relevant domains of the prion protein identified in vivoThe N-terminal, polybasic region is critical for prion protein neuroprotective activity.Instability of the octarepeat region of the human prion protein gene.Mouse-hamster chimeric prion protein (PrP) devoid of N-terminal residues 23-88 restores susceptibility to 22L prions, but not to RML prions in PrP-knockout miceAge-dependent impairment of eyeblink conditioning in prion protein-deficient mice.Prion strain-dependent differences in conversion of mutant prion proteins in cell culture.Male infertility and DNA damage in Doppel knockout and prion protein/Doppel double-knockout miceThe cellular prion protein (PrP(C)): its physiological function and role in diseaseCellular prion protein: from physiology to pathology.Transgene-driven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairmentThe prion protein knockout mouse: a phenotype under challenge.Antagonistic roles of the N-terminal domain of prion protein to doppel.Helix 3 is necessary and sufficient for prion protein's anti-Bax function.Dominant-negative effects of the N-terminal half of prion protein on neurotoxicity of prion protein-like protein/doppel in miceGenetic mapping of activity determinants within cellular prion proteins: N-terminal modules in PrPC offset pro-apoptotic activity of the Doppel helix B/B' region.The prion protein and its paralogue Doppel affect calcium signaling in Chinese hamster ovary cells.Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice.The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells.The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
P2860
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P2860
Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Deletion of N-terminal residue ...... pel-induced Neurodegeneration.
@en
Deletion of N-terminal residues 23-88 from prion protein
@nl
type
label
Deletion of N-terminal residue ...... pel-induced Neurodegeneration.
@en
Deletion of N-terminal residues 23-88 from prion protein
@nl
prefLabel
Deletion of N-terminal residue ...... pel-induced Neurodegeneration.
@en
Deletion of N-terminal residues 23-88 from prion protein
@nl
P2093
P2860
P356
P1476
Deletion of N-terminal residue ...... pel-induced Neurodegeneration.
@en
P2093
Kazuto Shigematsu
Noriyuki Nishida
Ryuichiro Atarashi
Shigeru Katamine
Shinji Goto
Suehiro Sakaguchi
Takahito Kondo
P2860
P304
28944-28949
P356
10.1074/JBC.M303655200
P407
P577
2003-05-19T00:00:00Z