Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

about

Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.How Do Gyrating Beads Accelerate Amyloid Fibrillization?

P2860

Q39545174-82D9341C-C5DA-43B7-B716-88776199DBB1 Q50932731-69C93DA5-7B26-4387-932A-8DF2DF59ACDF

P2860

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

Item

http://www.wikidata.org/entity/Q36552590

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@ast

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@en

type

Item

label

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@ast

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@en

prefLabel

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@ast

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@en

P1476

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

@en

P2093

Emma V Yates

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

Kadi-Liis Saar

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

Séverine Saunier

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

Thomas Müller

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

Tuomas P J Knowles

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

P2860

Mechanisms of protein-folding diseases at a glance

Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies

Protein misfolding, functional amyloid, and human disease

Protein folding and misfolding

Gene expression profiling of breast cancer

Protein aggregation and neurodegenerative disease

Soft lithography for micro- and nanoscale patterning

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism

Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status

P304

555-560

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

P31

scholarly article

P356

10.1016/J.BPJ.2015.11.3523

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

P407

English

P433

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

P478

110

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

P50

Chris Dobson

P577

2016-02-01T00:00:00Z

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

P5875

292949386

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

P698

26840721

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

P921

microfluidics

P932

4744157

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

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

about

P2860

P2860

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932