Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.
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Branched polyamines cure prion-infected neuroblastoma cellsConversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteinsPrionsTreatment of Prion Disease with Heterologous Prion ProteinsSheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solutionStrain-specified relative conformational stability of the scrapie prion proteinA family of cellular proteins related to snake venom disintegrinsTwo amyloid States of the prion protein display significantly different folding patternsCopper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation.Mapping the prion protein using recombinant antibodies.Mapping of possible prion protein self-interaction domains using peptide arraysConversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo.Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoformPrions and blood products.Cerebral amyloidosis in prion diseases.Structural studies of the scrapie prion protein by electron crystallography.Ultrastructural studies on scrapie prion protein crystals obtained from reverse micellar solutions.Amyloid structure: conformational diversity and consequences.Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignmentsInfluence of Mabs on PrP(Sc) formation using in vitro and cell-free systemsA family of dynein genes in Drosophila melanogaster.Scrapie prions selectively modify the stress response in neuroblastoma cellsEffect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra.Prion protein misfolding.Recombinant thyroid hormone receptor and retinoid X receptor stimulate ligand-dependent transcription in vitro.Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.Fibril formation of the rabbit/human/bovine prion proteinsProposed three-dimensional structure for the cellular prion proteinEndogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues.Etiology and pathogenesis of prion diseases.Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity.Prion protein PrPc interacts with molecular chaperones of the Hsp60 familyScrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.Chemical chaperones interfere with the formation of scrapie prion protein.Copper and Zinc Interactions with Cellular Prion Proteins Change Solubility of Full-Length Glycosylated Isoforms and Induce the Occurrence of Heterogeneous PhenotypesStructural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.Attempts to restore scrapie prion infectivity after exposure to protein denaturantsPrion protein expression in different species: analysis with a panel of new mAbsNucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein.
P2860
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P2860
Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Perturbation of the secondary ...... itions that alter infectivity.
@ast
Perturbation of the secondary ...... itions that alter infectivity.
@en
type
label
Perturbation of the secondary ...... itions that alter infectivity.
@ast
Perturbation of the secondary ...... itions that alter infectivity.
@en
prefLabel
Perturbation of the secondary ...... itions that alter infectivity.
@ast
Perturbation of the secondary ...... itions that alter infectivity.
@en
P2093
P2860
P356
P1476
Perturbation of the secondary ...... itions that alter infectivity.
@en
P2093
M A Baldwin
R J Fletterick
P2860
P356
10.1073/PNAS.90.1.1
P407
P577
1993-01-01T00:00:00Z