The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation.
about
Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry.Computational re-engineering of Amylin sequence with reduced amyloidogenic potential.Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formationNMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG.Amyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactionsIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Toxicity of imine-iminium dyes and pigments: electron transfer, radicals, oxidative stress and other physiological effects.A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates.New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity.Implications of peptide assemblies in amyloid diseases.Amylin uncovered: a review on the polypeptide responsible for type II diabetes.Foldamer-mediated manipulation of a pre-amyloid toxinPeptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.Partial peptide of α-synuclein modified with small-molecule inhibitors specifically inhibits amyloid fibrillation of α-synuclein.Folded small molecule manipulation of islet amyloid polypeptide.An in vivo platform for identifying inhibitors of protein aggregation.A direct fluorescence-based technique for cellular localization of amylin.Peptide Conjugates of Benzene Carboxylic Acids as Agonists and Antagonists of Amylin Aggregation.Development of proteolytically stable N-methylated peptide inhibitors of aggregation of the amylin peptide implicated in type 2 diabetes.Teaching an old scaffold new recognition tricks: oligopyrrolamide antagonists of IAPP aggregation.Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms
P2860
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P2860
The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
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2010年學術文章
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name
The sulfated triphenyl methane ...... effects of amyloid formation.
@en
The sulfated triphenyl methane ...... effects of amyloid formation.
@nl
type
label
The sulfated triphenyl methane ...... effects of amyloid formation.
@en
The sulfated triphenyl methane ...... effects of amyloid formation.
@nl
prefLabel
The sulfated triphenyl methane ...... effects of amyloid formation.
@en
The sulfated triphenyl methane ...... effects of amyloid formation.
@nl
P2093
P2860
P50
P1476
The sulfated triphenyl methane ...... effects of amyloid formation.
@en
P2093
Annette Plesner
C Bruce Verchere
Fanling Meng
Kathryn J Potter
Martin T Zanni
P2860
P304
P356
10.1016/J.JMB.2010.05.001
P407
P577
2010-05-07T00:00:00Z