Rational design of an orthosteric regulator of hIAPP aggregation.

about

An optimal hydrogen-bond surrogate for α-helices.Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.Selective inhibition of cancer cells by enzyme-induced gain of function of phosphorylated melittin analogues.

P2860

Q36813449-B89253B1-5BC0-41B8-8915-A0A437E11E4D Q37251550-4625EBFB-F74E-409C-9B02-264538B73252 Q52641548-4D3F63C1-F545-436D-834F-40D216FA5F78

P2860

Rational design of an orthosteric regulator of hIAPP aggregation.

Item

http://www.wikidata.org/entity/Q38925916

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Rational design of an orthosteric regulator of hIAPP aggregation.

@en

type

Item

label

Rational design of an orthosteric regulator of hIAPP aggregation.

@en

prefLabel

Rational design of an orthosteric regulator of hIAPP aggregation.

@en

P1476

Rational design of an orthosteric regulator of hIAPP aggregation.

@en

P2093

De-Sheng Zhao

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

Yan-Mei Li

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

Yong-Xiang Chen

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

P2860

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Atomic View of a Toxic Amyloid Small Oligomer

Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.

Toxic fibrillar oligomers of amyloid-β have cross-β structure.

Prediction of protein-protein interface sequence diversity using flexible backbone computational protein design.

Cyclen-hybrid compound captures copper to protect INS-1 cells from islet amyloid polypeptide cytotoxicity by inhibiting and lysing effects.

Synthetic alpha-helix mimetics as agonists and antagonists of islet amyloid polypeptide aggregation.

Conformational transition of amyloid beta-peptide.

Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid.

P304

2095-2098

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

P31

scholarly article

P356

10.1039/C4CC06739H

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

P577

2014-12-23T00:00:00Z

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

P698

25536011

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

Rational design of an orthosteric regulator of hIAPP aggregation.

about

P2860

P2860

Rational design of an orthosteric regulator of hIAPP aggregation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698