Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models.
about
Attachment of pathogenic prion protein to model oxide surfaces.Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversionGetting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pHProbing the conformation of a prion protein fibril with hydrogen exchange.Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding.Influence of pH on the human prion protein: insights into the early steps of misfolding.The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study.Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.The Effects of Ca2+ Concentration and E200K Mutation on the Aggregation Propensity of PrPC: A Computational Study.Prions and the potential transmissibility of protein misfolding diseasesDecrypting Prion Protein Conversion into a β-Rich Conformer by Molecular DynamicsGeneric cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126.Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure.Characterization of cell-surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane-bound human prion protein.The consequences of pathogenic mutations to the human prion protein.Prion protein misfolding and disease.Natural and synthetic prion structure from X-ray fiber diffractionPrion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.Fate of prions in soil: a review.Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science.Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Left handed beta helix models for mammalian prion fibrils.Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules.Parameters that affect macromolecular self-assembly of prion protein.
P2860
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P2860
Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models.
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structural properties of prion ...... l assessment of atomic models.
@ast
Structural properties of prion ...... l assessment of atomic models.
@en
type
label
Structural properties of prion ...... l assessment of atomic models.
@ast
Structural properties of prion ...... l assessment of atomic models.
@en
prefLabel
Structural properties of prion ...... l assessment of atomic models.
@ast
Structural properties of prion ...... l assessment of atomic models.
@en
P356
P1433
P1476
Structural properties of prion ...... l assessment of atomic models.
@en
P2093
Jay Silveira
Mari L DeMarco
P304
15573-15582
P356
10.1021/BI0612723
P407
P577
2006-12-01T00:00:00Z