Amyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligands

Item

http://www.wikidata.org/entity/Q28547085

description

2015 nî lūn-bûn

@nan

2015 թուականին հրատարակուած գիտական յօդուած

@hyw

2015 թվականին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Amyloidogenic propensity of a ...... y and interaction with ligands

@ast

Amyloidogenic propensity of a ...... y and interaction with ligands

@en

Amyloidogenic propensity of a ...... y and interaction with ligands

@nl

type

Item

label

Amyloidogenic propensity of a ...... y and interaction with ligands

@ast

Amyloidogenic propensity of a ...... y and interaction with ligands

@en

Amyloidogenic propensity of a ...... y and interaction with ligands

@nl

prefLabel

Amyloidogenic propensity of a ...... y and interaction with ligands

@ast

Amyloidogenic propensity of a ...... y and interaction with ligands

@en

Amyloidogenic propensity of a ...... y and interaction with ligands

@nl

P1476

Amyloidogenic propensity of a ...... y and interaction with ligands

@en

P2093

Eduardo D Prieto

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

José M Delfino

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

Lucrecia M Curto

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

Nahuel A Ramella

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

Omar J Rimoldi

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

Silvana A Rosú

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

P2860

The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis

Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis

Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

Biological activity and pathological implications of misfolded proteins.

The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.

Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments.

Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.

P304

e0124946

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0124946

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

P407

English

P433

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

P478

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

P50

María Alejandra Tricerri

P577

2015-01-01T00:00:00Z

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

P5875

276068404

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

P698

25950566

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

P932

4423886

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