Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible
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Molecular features of the copper binding sites in the octarepeat domain of the prion proteinNovel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and scrapieA database of macromolecular motionsPrionsHot spots in prion protein for pathogenic conversionNMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domainThe Cellular Prion Protein: A Player in Immunological QuiescenceProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsNMR 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 diseasesTwo different neurodegenerative diseases caused by proteins with similar structuresSheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solutionUnique quadruplex structure and interaction of an RNA aptamer against bovine prion proteinStructure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated GlycanUnique Structural Characteristics of the Rabbit Prion ProteinSolution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinN-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion ProteinsPost-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivoRapid folding of the prion protein captured by pressure-jumpInsight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variantsChanging a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers.Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion proteinThe octarepeat region of the prion protein is conformationally altered in PrP(Sc)Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragmentNMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clustersFormation of amyloid fibrils from β-amylaseCellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseasesTetracysteine-tagged prion protein allows discrimination between the native and converted formsA large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMRNatively unfolded proteins: a point where biology waits for physicsAmyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system.Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins.The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.Copper binding to the prion protein: structural implications of four identical cooperative binding sitesDetermination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
P2860
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P2860
Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Structure of the recombinant f ...... N terminus is highly flexible
@ast
Structure of the recombinant f ...... N terminus is highly flexible
@en
type
label
Structure of the recombinant f ...... N terminus is highly flexible
@ast
Structure of the recombinant f ...... N terminus is highly flexible
@en
prefLabel
Structure of the recombinant f ...... N terminus is highly flexible
@ast
Structure of the recombinant f ...... N terminus is highly flexible
@en
P2093
P2860
P50
P356
P1476
Structure of the recombinant f ...... N terminus is highly flexible
@en
P2093
P2860
P304
13452-13457
P356
10.1073/PNAS.94.25.13452
P407
P577
1997-12-01T00:00:00Z