The elongation of yeast prion fibers involves separable steps of association and conversion.
about
Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteinsMechanism of prion propagation: amyloid growth occurs by monomer additionHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Recognition of 27-class protein folds by adding the interaction of segments and motif information.The recognition of multi-class protein folds by adding average chemical shifts of secondary structure elementsElongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Monitoring dynamics of single-cell gene expression over multiple cell cyclesMechanistic and environmental control of the prevalence and lifetime of amyloid oligomersA synergistic small-molecule combination directly eradicates diverse prion strain structuresRole of small oligomers on the amyloidogenic aggregation free-energy landscapeDescribing sequence-ensemble relationships for intrinsically disordered proteins.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansStructural insights into a yeast prion illuminate nucleation and strain diversityAmyloid-like fibril elongation follows michaelis-menten kineticsFusion of Epstein-Barr virus with epithelial cells can be triggered by αvβ5 in addition to αvβ6 and αvβ8, and integrin binding triggers a conformational change in glycoproteins gHgL.A three-stage kinetic model of amyloid fibrillation.Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.Folding versus aggregation: polypeptide conformations on competing pathwaysOrdering recombinant silk-elastin-like nanofibers on the microscale.Emergence and natural selection of drug-resistant prions.The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.Dynamics of heteromolecular filament formation.Molecular mechanisms of protein aggregation from global fitting of kinetic models.Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism.Human beta-synuclein rendered fibrillogenic by designed mutations.Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NMRole of elongation and secondary pathways in S6 amyloid fibril growth.Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding.Scaling behaviour and rate-determining steps in filamentous self-assembly.Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation.Engineering aqueous fiber assembly into silk-elastin-like protein polymersFrequency Factors in a Landscape Model of Filamentous Protein AggregationInfluence of Solution Parameters on Phase Diagram of Recombinant Spider Silk-Like Block CopolymersAmyloid assembly and disassembly
P2860
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P2860
The elongation of yeast prion fibers involves separable steps of association and conversion.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The elongation of yeast prion ...... of association and conversion.
@ast
The elongation of yeast prion ...... of association and conversion.
@en
type
label
The elongation of yeast prion ...... of association and conversion.
@ast
The elongation of yeast prion ...... of association and conversion.
@en
prefLabel
The elongation of yeast prion ...... of association and conversion.
@ast
The elongation of yeast prion ...... of association and conversion.
@en
P2860
P50
P356
P1476
The elongation of yeast prion ...... of association and conversion.
@en
P2860
P304
P356
10.1073/PNAS.0308754101
P407
P577
2004-02-01T00:00:00Z