Phosphorylation of prion protein at serine 43 induces prion protein conformational change
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Post-translational modifications induce significant yet not extreme changes to protein structure.Baking a mass-spectrometry data PIE with McMC and simulated annealing: predicting protein post-translational modifications from integrated top-down and bottom-up data.The N-terminal sequence of prion protein consists an epitope specific to the abnormal isoform of prion protein (PrP(Sc))Cyclin-dependent kinase 5 phosphorylation of familial prion protein mutants exacerbates conversion into amyloid structure.Cdk5 at crossroads of protein oligomerization in neurodegenerative diseases: facts and hypotheses.
P2860
Phosphorylation of prion protein at serine 43 induces prion protein conformational change
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on July 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Phosphorylation of prion protein at serine 43 induces prion protein conformational change
@en
Phosphorylation of prion prote ...... protein conformational change.
@nl
type
label
Phosphorylation of prion protein at serine 43 induces prion protein conformational change
@en
Phosphorylation of prion prote ...... protein conformational change.
@nl
prefLabel
Phosphorylation of prion protein at serine 43 induces prion protein conformational change
@en
Phosphorylation of prion prote ...... protein conformational change.
@nl
P2093
P2860
P1476
Phosphorylation of prion protein at serine 43 induces prion protein conformational change
@en
P2093
Andrea C LeBlanc
Catherine Robertson
Hemant Paudel
Julie Jodoin
Paresa N Giannopoulos
Stephanie A Booth
P2860
P304
P356
10.1523/JNEUROSCI.2294-09.2009
P407
P577
2009-07-01T00:00:00Z