The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors.
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Porcine islet amyloid polypeptide fragments are refractory to amyloid formationBlockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAASMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusResidue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsRationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubilityStructural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitorsShort Peptides as Inhibitors of Amyloid AggregationAnalysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced ToxicityInduction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's diseaseIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Cyclic N-terminal loop of amylin forms non amyloid fibers.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Advances in electrochemical detection for study of neurodegenerative disorders.Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation.Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Fiber-dependent and -independent toxicity of islet amyloid polypeptide.Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers.Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitorRole of aromatic interactions in amyloid formation by islet amyloid polypeptide.Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids.
P2860
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P2860
The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
The ability of rodent islet am ...... and the design of inhibitors.
@en
type
label
The ability of rodent islet am ...... and the design of inhibitors.
@en
prefLabel
The ability of rodent islet am ...... and the design of inhibitors.
@en
P2860
P356
P1433
P1476
The ability of rodent islet am ...... and the design of inhibitors.
@en
P2093
Fanling Meng
P2860
P304
P356
10.1021/BI901751B
P407
P577
2010-02-01T00:00:00Z