Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation.
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Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusMechanisms of islet amyloidosis toxicity in type 2 diabetesOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesSensitivity 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 solubilityMorin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.Structural 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 inhibitorsGeneral amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers.Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Mechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics.Amyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactionsIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Cyclic N-terminal loop of amylin forms non amyloid fibers.Islet amyloid polypeptide toxicity and membrane interactionsMechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitorAspirin, diabetes, and amyloid: re-examination of the inhibition of amyloid formation by aspirin and ketoprofenDissecting the role of single regions of an IAPP mimic and IAPP in inhibition of Aβ40 amyloid formation and cytotoxicity.A Hot-Segment-Based Approach for the Design of Cross-Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self-Assembly.
P2860
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P2860
Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation.
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
Combination of kinetically sel ...... hibition of amyloid formation.
@en
type
label
Combination of kinetically sel ...... hibition of amyloid formation.
@en
prefLabel
Combination of kinetically sel ...... hibition of amyloid formation.
@en
P2860
P356
P1476
Combination of kinetically sel ...... hibition of amyloid formation.
@en
P2093
Fanling Meng
P2860
P304
14340-14342
P356
10.1021/JA1046186
P407
P577
2010-10-01T00:00:00Z