Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function.
about
Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain.Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice.
P2860
Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function.
description
2010 nî lūn-bûn
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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2010年论文
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2010年论文
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name
Changing the solvent accessibi ...... g and effect on cell function.
@en
Changing the solvent accessibi ...... g and effect on cell function.
@nl
type
label
Changing the solvent accessibi ...... g and effect on cell function.
@en
Changing the solvent accessibi ...... g and effect on cell function.
@nl
prefLabel
Changing the solvent accessibi ...... g and effect on cell function.
@en
Changing the solvent accessibi ...... g and effect on cell function.
@nl
P2093
P2860
P356
P1433
P1476
Changing the solvent accessibi ...... g and effect on cell function.
@en
P2093
Bryan Schmidt
Catherine A Tabrett
Christopher F Harrison
Philip J Hogg
Shayne A Bellingham
Tristan Hardy
Yves-Henri Sanejouand
P2860
P304
P356
10.1042/BJ20091635
P407
P577
2010-05-13T00:00:00Z