A kinetic model for amyloid formation in the prion diseases: importance of seeding.
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Infectivity versus Seeding in Neurodegenerative Diseases Sharing a Prion-Like MechanismLeu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experimentConversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteinsEx vivo mammalian prions are formed of paired double helical prion protein fibrils.Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solutionMolecular mechanisms for protein-encoded inheritanceA brief history of prionsPrion diseases: dynamics of the infection and properties of the bistable transition.Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting diseaseEffects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's diseaseIsolation of proteinase K-sensitive prions using pronase E and phosphotungstic acidAmyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation.High pressure, a tool to switch between soluble and fibrillar prion protein structures.Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.Biophysical characterization of lithostathine. Evidences for a polymeric structure at physiological pH and a proteolysis mechanism leading to the formation of fibrils.Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B.Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation.Prions, amyloids, and RNA: Pieces of a puzzle.Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal modelCellular biology of prion diseases.Neurodegeneration in humans caused by prionsHeat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry.Monoclonal antibody F89/160.1.5 defines a conserved epitope on the ruminant prion protein.Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence.Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked.Quantitative detection and biological propagation of scrapie seeding activity in vitro facilitate use of prions as model pathogens for disinfectionActivation of TRPML1 clears intraneuronal Aβ in preclinical models of HIV infection.Is there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles?Simulations of oligomeric intermediates in prion diseases.The circularization of amyloid fibrils formed by apolipoprotein C-II.Prion strain interactions are highly selective.Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strainA mechanistic model for amorphous protein aggregation of immunoglobulin-like domains.Binary and ternary aggregation within tethered protein constructs.Interaction of the anthracycline 4'-iodo-4'-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesisHeterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain.
P2860
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P2860
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@ast
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@en
type
label
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@ast
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@en
prefLabel
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@ast
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@en
P2093
P2860
P356
P1476
A kinetic model for amyloid formation in the prion diseases: importance of seeding.
@en
P2093
Lansbury PT Jr
P2860
P304
P356
10.1073/PNAS.90.13.5959
P407
P577
1993-07-01T00:00:00Z