Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.

about

Drosophila Insulin-Like Peptides DILP2 and DILP5 Differentially Stimulate Cell Signaling and Glycogen Phosphorylase to Regulate Longevity.Probing the correlation between insulin activity and structural stability through introduction of the rigid A6-A11 bond

P2860

Q55035084-9520565C-03BE-42EE-A345-503AE4561CA6 Q57174414-6A377DEF-9027-4A8F-9749-E04E3A6DA97C

P2860

Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.

Item

http://www.wikidata.org/entity/Q47135854

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Insulin in motion: The A6-A11 ...... required for insulin activity.

@en

Insulin in motion: The A6-A11 ...... required for insulin activity.

@nl

type

Item

label

Insulin in motion: The A6-A11 ...... required for insulin activity.

@en

Insulin in motion: The A6-A11 ...... required for insulin activity.

@nl

prefLabel

Insulin in motion: The A6-A11 ...... required for insulin activity.

@en

Insulin in motion: The A6-A11 ...... required for insulin activity.

@nl

P1476

Insulin in motion: The A6-A11 ...... required for insulin activity.

@en

P2093

Alessia Belgi

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

Andrea J Robinson

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

Bianca van Lierop

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

Carlie Delaine

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

Shee Chee Ong

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

Sofianos Andrikopoulos

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

P2860

Insulin signalling and the regulation of glucose and lipid metabolism

Insulin increases cell surface GLUT4 levels by dose dependently discharging GLUT4 into a cell surface recycling pathway

Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I

How insulin engages its primary binding site on the insulin receptor

Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing

Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding

The A-chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice

Receptor binding redefined by a structural switch in a mutant human insulin

Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues

Protective hinge in insulin opens to enable its receptor engagement

P2888

s41598-017-16876-3

P304

17239

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

P31

scholarly article

P356

10.1038/S41598-017-16876-3

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

P577

2017-12-08T00:00:00Z

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

P6179

1093156852

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

P698

29222417

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

P921

Insulin

P932

5722942

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

Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.

about

P2860

P2860

Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P6179

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P6179

P698

P921

P932