Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

about

Amyloid-β-neuropeptide interactions assessed by ion mobility-mass spectrometry.Selenoprotein P and selenoprotein M block Zn2+ -mediated Aβ42 aggregation and toxicity.New Insights into Drug Reaction with Eosinophilia and Systemic Symptoms Pathophysiology.

P2860

Q36879051-57D56D30-E292-41C5-90B8-10931EAD00C5 Q38315714-90C2D987-9B7E-49A4-AD19-EAEC7EDBAE20 Q47140255-5D408EFB-1BC6-46FD-A6D8-78B2EA4D22CF

P2860

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

Item

http://www.wikidata.org/entity/Q39271013

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh

2012年學術文章

@zh-hant

name

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@en

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@nl

type

Item

label

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@en

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@nl

prefLabel

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@en

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

@nl

P1476

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides

@en

P2093

Hema Jegasothy

http://www.w3.org/2001/XMLSchema#string

Louise Bennett

http://www.w3.org/2001/XMLSchema#string

Lynne Waddington

http://www.w3.org/2001/XMLSchema#string

Prashant Bharadwaj

http://www.w3.org/2001/XMLSchema#string

Rabia Sarroukh

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease

Intracellular amyloid-beta in Alzheimer's disease

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo

Peptide and protein mimetics inhibiting amyloid beta-peptide aggregation.

Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Abeta1-40 fibrillogenesis.

Disrupting beta-amyloid aggregation for Alzheimer disease treatment.

Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation.

CSF amyloid-beta-peptides in Alzheimer's disease, dementia with Lewy bodies and Parkinson's disease dementia

N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure.

P304

92-103

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1039/C2FO30111C

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Vincent Raussens

Richard Head

Ralph Martins

P577

2012-09-27T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

231213923

http://www.w3.org/2001/XMLSchema#string

P698

23014463

http://www.w3.org/2001/XMLSchema#string

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

about

P2860

P2860

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698