Solution structure of Syrian hamster prion protein rPrP(90-231).
about
Conformational diversity in prion protein variants influences intermolecular beta-sheet formationProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsTrans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactorNMR solution structure of the human prion proteinNMR structure of the bovine prion proteinNMR structures of three single-residue variants of the human prion proteinSolution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseasesSheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solutionSolution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinPrion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrPA brief history of prionsRapid folding of the prion protein captured by pressure-jumpInsight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variantsCorrelation analysis for the incubation period of prion diseaseEarly onset prion disease from octarepeat expansion correlates with copper binding propertiesEnhanced stability of human prion proteins with two disulfide bridges.Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.Mapping the early steps in the pH-induced conformational conversion of the prion protein.Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion.The role of disulfide bridge in the folding and stability of the recombinant human prion protein.High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility.Probing structural differences in prion protein isoforms by tyrosine nitrationCharacteristics of 263K scrapie agent in multiple hamster speciesTransmission barriers for bovine, ovine, and human prions in transgenic mice.Prion protein NMR structures of elk and of mouse/elk hybridsIdentification of two prion protein regions that modify scrapie incubation time.Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice.A molecular switch controls interspecies prion disease transmission in mice.Structural studies of the scrapie prion protein by electron crystallography.The origin of cellular life.Familial conformational diseases and dementias.A plausible function of the prion protein: conjectures and a hypothesis.The ZIP5 ectodomain co-localizes with PrP and may acquire a PrP-like fold that assembles into a dimer.Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteinsEmerging therapeutic agents for transmissible spongiform encephalopathies: a review.Copper binding in the prion proteinEffect of the E200K mutation on prion protein metabolism. Comparative study of a cell model and human brain.Mimicking dominant negative inhibition of prion replication through structure-based drug design.
P2860
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P2860
Solution structure of Syrian hamster prion protein rPrP(90-231).
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Solution structure of Syrian hamster prion protein rPrP(90-231).
@ast
Solution structure of Syrian hamster prion protein rPrP(90-231).
@en
type
label
Solution structure of Syrian hamster prion protein rPrP(90-231).
@ast
Solution structure of Syrian hamster prion protein rPrP(90-231).
@en
prefLabel
Solution structure of Syrian hamster prion protein rPrP(90-231).
@ast
Solution structure of Syrian hamster prion protein rPrP(90-231).
@en
P2093
P356
P1433
P1476
Solution structure of Syrian hamster prion protein rPrP(90-231).
@en
P2093
Farr-Jones S
Marqusee S
Ulyanov NB
P304
P356
10.1021/BI982878X
P407
P577
1999-04-01T00:00:00Z