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PubMed:11087738 JSONTXT 27 Projects

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Id Subject Object Predicate Lexical cue
T1 0-181 Sentence denotes A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.
T2 182-318 Sentence denotes Gerstmann-Sträussler-Scheinker disease (GSS) is a cerebral amyloidosis associated with mutations in the prion protein (PrP) gene (PRNP).
T3 319-537 Sentence denotes The aim of this study was to characterize amyloid peptides purified from brain tissue of a patient with the A117V mutation who was Met/Val heterozygous at codon 129, Val(129) being in coupling phase with mutant Val117.
T4 538-626 Sentence denotes The major peptide extracted from amyloid fibrils was a approximately 7-kDa PrP fragment.
T5 627-798 Sentence denotes Sequence analysis and mass spectrometry showed that this fragment had ragged N and C termini, starting mainly at Gly88 and Gly90 and ending with Arg148, Glu152, or Asn153.
T6 799-919 Sentence denotes Only Val was present at positions 117 and 129, indicating that the amyloid protein originated from mutant PrP molecules.
T7 920-1086 Sentence denotes In addition to the approximately 7-kDa peptides, the amyloid fraction contained N- and C-terminal PrP fragments corresponding to residues 23-41, 191-205, and 217-228.
T8 1087-1267 Sentence denotes Fibrillogenesis in vitro with synthetic peptides corresponding to PrP fragments extracted from brain tissue showed that peptide PrP-(85-148) readily assembled into amyloid fibrils.
T9 1268-1415 Sentence denotes Peptide PrP-(191-205) also formed fibrillary structures although with different morphology, whereas peptides PrP-(23-41) and PrP-(217-228) did not.
T10 1416-1563 Sentence denotes These findings suggest that the processing of mutant PrP isoforms associated with Gerstmann-Sträussler-Scheinker disease may occur extracellularly.
T11 1564-1867 Sentence denotes It is conceivable that full-length PrP and/or large PrP peptides are deposited in the extracellular compartment, partially degraded by proteases and further digested by tissue endopeptidases, originating a approximately 7-kDa protease-resistant core that is similar in patients with different mutations.
T12 1868-1976 Sentence denotes Furthermore, the present data suggest that C-terminal fragments of PrP may participate in amyloid formation.