Direct conversion of an oligopeptide from a beta-sheet to an alpha-helix: a model for amyloid formation.
about
Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone proteinEnvironmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin.Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulationsConformational behavior of ionic self-complementary peptides.Concentration effect on the aggregation of a self-assembling oligopeptide.Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Abeta1-40 fibrillogenesis.De novo amyloid proteins from designed combinatorial librariesIncreasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallelSolvent-induced beta-hairpin to helix conformational transition in a designed peptide.Structural dynamic of a self-assembling peptide d-EAK16 made of only D-amino acidsInoculation of scrapie with the self-assembling RADA-peptide disrupts prion accumulation and extends hamster survival.Metal and complementary molecular bioimaging in Alzheimer's disease.De novo designed peptide-based amyloid fibrils.Large scale conformational transitions in β-structural motif of gramicidin A: kinetic analysis based on CD and FT-IR data.Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.Folding a protein with equal probability of being helix or hairpin.Biopolymers and supramolecular polymers as biomaterials for biomedical applications.Design and preparation of polymeric scaffolds for tissue engineering.Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1.Solid-state NMR evidence for β-hairpin structure within MAX8 designer peptide nanofibers.FTIR spectroscopic imaging of protein aggregation in living cells.Mechanisms of amyloid fibril formation--focus on domain-swapping.Self-assembly of amphipathic β-sheet peptides: insights and applications.Soft materials based on designed self-assembling peptides: from design to application.DNA and RNA-controlled switching of protein kinase activity.Structure-mechanical property correlations of hydrogel forming β-sheet peptides.The effect of self-assembling peptide RADA16-I on the growth of human leukemia cells in vitro and in nude miceDesign of 11-residue peptides with unusual biophysical properties: induced secondary structure in the absence of water.Early tissue patterning recreated by mouse embryonic fibroblasts in a three-dimensional environment.Solvent effects on the conformational transition of a model polyalanine peptide.A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins.Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides.The role of hydrophobic interactions in amyloidogenesis: example of prion-related polypeptides.Peptide binding landscapes: Specificity and homophilicity across sequence space in a lattice model.Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation.Photo-switched self-assembly of a gemini α-helical peptide into supramolecular architectures.Design Principles of Peptide Based Self-Assembled Nanomaterials.Stimuli responsive fibrous hydrogels from hierarchical self-assembly of a triblock copolypeptide.Metal-triggered Nanofiber Formation of His-containing β-Sheet Peptide
P2860
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P2860
Direct conversion of an oligopeptide from a beta-sheet to an alpha-helix: a model for amyloid formation.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Direct conversion of an oligop ...... a model for amyloid formation.
@ast
Direct conversion of an oligop ...... a model for amyloid formation.
@en
type
label
Direct conversion of an oligop ...... a model for amyloid formation.
@ast
Direct conversion of an oligop ...... a model for amyloid formation.
@en
prefLabel
Direct conversion of an oligop ...... a model for amyloid formation.
@ast
Direct conversion of an oligop ...... a model for amyloid formation.
@en
P2860
P356
P1476
Direct conversion of an oligop ...... a model for amyloid formation.
@en
P2860
P356
10.1073/PNAS.94.1.23
P407
P577
1997-01-01T00:00:00Z