CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
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Unique Structural Characteristics of the Rabbit Prion ProteinStructural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulationsSimilar folds with different stabilization mechanisms: the cases of Prion and Doppel proteins.The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study.Prion protein misfolding.The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPScInsight into Early-Stage Unfolding of GPI-Anchored Human Prion Protein.Rare large scale subdomain motions in prion protein can initiate aggregation.Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations.Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein.Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transitionFrom conversion to aggregation: protofibril formation of the prion protein.The reconstitution of mammalian prion infectivity de novo.Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain.Factors governing helix formation in peptides confined to carbon nanotubes.Conformational properties of beta-PrP.Probing the instabilities in the dynamics of helical fragments from mouse PrPC.Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Misfolding pathways of the prion protein probed by molecular dynamics simulations.Structural and hydration properties of the partially unfolded states of the prion protein.Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment.The therapeutically anti-prion active antibody-fragment scFv-W226: paramagnetic relaxation-enhanced NMR spectroscopy aided structure elucidation of the paratope-epitope interface.The role of electrostatic interaction in triggering the unraveling of stable helix 1 in normal prion protein. A molecular dynamics simulation investigation.Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules.Putative aggregation initiation sites in prion protein.Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.
P2860
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P2860
CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
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2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
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2003年學術文章
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name
CD and NMR studies of prion pr ...... PC-->PrPSc conversion process.
@en
CD and NMR studies of prion protein
@nl
type
label
CD and NMR studies of prion pr ...... PC-->PrPSc conversion process.
@en
CD and NMR studies of prion protein
@nl
prefLabel
CD and NMR studies of prion pr ...... PC-->PrPSc conversion process.
@en
CD and NMR studies of prion protein
@nl
P2093
P2860
P356
P1476
CD and NMR studies of prion pr ...... PC-->PrPSc conversion process.
@en
P2093
Jan Ziegler
Paul Rösch
Stephan Schwarzinger
Ute C Marx
Wolfgang Müller
P2860
P304
50175-50181
P356
10.1074/JBC.M305234200
P407
P577
2003-09-02T00:00:00Z