Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol.
about
Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAASInhibition of IAPP Aggregation and Toxicity by Natural Products and DerivativesBinding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current statusBridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive PotentialEffects of several quinones on insulin aggregation.The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.Resveratrol inhibits the formation of multiple-layered β-sheet oligomers of the human islet amyloid polypeptide segment 22-27Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactionsAmyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.General 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.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionNatural biomolecules and protein aggregation: emerging strategies against amyloidogenesisPancreatic β-Cell Membrane Fluidity and Toxicity Induced by Human Islet Amyloid Polypeptide Species.Herbal therapies for type 2 diabetes mellitus: chemistry, biology, and potential application of selected plants and compoundsProtein folding and aggregation into amyloid: the interference by natural phenolic compoundsIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-β-D-glucose.Effects of dietary polyphenols on neuroregulatory factors and pathways that mediate food intake and energy regulation in obesity.A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide.Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates.Graphene oxide inhibits hIAPP amyloid fibrillation and toxicity in insulin-producing NIT-1 cells.Rational design of an orthosteric regulator of hIAPP aggregation.Inhibition of human amylin fibril formation by insulin-mimetic vanadium complexes.Implications of peptide assemblies in amyloid diseases.Kinetic profile of amyloid formation in the presence of an aromatic inhibitor by nuclear magnetic resonance.Amylin uncovered: a review on the polypeptide responsible for type II diabetes.Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol.Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives.Foldamer-mediated manipulation of a pre-amyloid toxinUnfolding Novel Mechanisms of Polyphenol Flavonoids for Better Glycaemic Control: Targeting Pancreatic Islet Amyloid Polypeptide (IAPP).Probing the binding affinity of amyloids to reduce toxicity of oligomers in diabetes.Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.Folded small molecule manipulation of islet amyloid polypeptide.Single-molecule fluorescence spectroscopy using phospholipid bilayer nanodiscs.Influence of a curcumin derivative on hIAPP aggregation in the absence and presence of lipid membranes.Resveratrol improves cognition and reduces oxidative stress in rats with vascular dementia.Aspirin, diabetes, and amyloid: re-examination of the inhibition of amyloid formation by aspirin and ketoprofenRuthenium complexes as novel inhibitors of human islet amyloid polypeptide fibril formation.A direct fluorescence-based technique for cellular localization of amylin.
P2860
Q24336425-A310BDC5-E24B-45DB-96D9-9AFF47035B8AQ27013875-9094D150-1741-4BB5-B487-E04B7992446AQ28393352-E4C6A3AF-3F14-4A2B-AB57-00EB9AF38F08Q29994589-E0AAEADA-30FE-4A57-94AD-5564E3916497Q33876973-9DDF25B6-CD86-4750-A9EE-36B37448BACDQ34660220-25AEE9F6-6935-4D65-80F7-9BC6DF6F4E21Q34688893-B8A4B769-9282-4B78-8D62-3C2F3E2B23D1Q35027146-98DEFED4-E72D-48BE-BAF9-BE8E693AE56FQ35139664-0A9C5DDB-61DF-4643-8809-7F38B28CA951Q35280161-DDBFEA73-A288-483F-AC24-9B995B7C0E71Q36307453-C08770A5-3F1E-408D-8E80-940A91462FC6Q36499539-39BFF843-FFAE-40E9-BAB9-93AEB6F8ECCCQ36538570-419624AD-3BD4-4473-8811-43E77E6C0466Q36583195-7C574121-395E-4ACA-98D8-2BD1C4DC93D7Q36801780-B6D5CEE0-5BE8-4132-954E-C7F3E4E24D2FQ37007345-3ADED7F3-BEAA-414B-84ED-C6C9E2CB1332Q37120813-87F16A3A-A37E-446D-A319-55472797FB3FQ37642975-D39DAE72-6F3F-4FEC-B0CD-70FE6A1223AFQ38057717-07D7A154-3C13-4381-A924-A63017C56C45Q38545239-3EDB1929-DAF2-4CCC-8157-4D2408E7F439Q38802989-124EB8DE-BA3F-4689-92F5-5C8221068ADAQ38815275-A2DB818F-9C80-4247-8C5B-0AA0B17F651AQ38925916-6DE57400-3D59-4BD5-B6C4-1A91E5686BB8Q39006181-6D65ECA0-EB37-4F98-99C8-B3E114FBB3D6Q39431937-6CAF72F2-1E4D-4D53-839C-DA30B69537D8Q39731518-C2C9C432-BCD4-4CEA-98F1-B02C36B82CB3Q39846208-B223152B-DEB0-4073-9575-193C4E7EA516Q39864309-A23593A6-F1E0-4898-89EE-9C6C0A743CC0Q40484092-5B36B94A-1394-4EC6-8C45-D13675AAB836Q40736828-D37D432F-81DD-43D6-AC25-8E6A0DA12B8EQ41195653-1D46D28B-835C-49E4-B8AB-6909934CCE93Q41247722-2D7C9F3F-852E-48F5-9E83-D2F43F957FF6Q41492334-874D09AC-AC74-448C-B40B-B60737269F8AQ41847205-B025D231-0BC1-4820-9DEF-9B89067A28A9Q41870217-3EE97826-A182-4451-9F1A-32EE4548C528Q41980210-2B32B1A8-7EB1-4BA5-9889-2A4B3E70329BQ41986372-10A6FBE7-D95B-4941-BABA-8B81598C9C5AQ42231575-196BDB39-ED8C-4737-9D2F-9FE374EC67AEQ43821791-1D1DFF93-11D3-4CF0-B67A-D13076F6D63AQ45169860-446E23E7-21DB-45BC-A877-AF3FD1E9D83C
P2860
Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@en
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@nl
type
label
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@en
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@nl
prefLabel
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@en
Inhibiting islet amyloid polyp ...... red wine compound resveratrol.
@nl
P2093
P356
P1433
P1476
Inhibiting islet amyloid polyp ...... red wine compound resveratrol
@en
P2093
Andrea Gohlke
Daniel Sellin
Diana Radovan
Rajesh Mishra
P304
P356
10.1002/CBIC.200800762
P577
2009-02-01T00:00:00Z