Conformational transitions of the cross-linking domains of elastin during self-assembly - Wikidata - awgldk - TriplyDB

Conformational transitions of the cross-linking domains of elastin during self-assembly

Conformational transitions of the cross-linking domains of elastin during self-assembly

http://www.wikidata.org/entity/Q30359229

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Direct observation of structure and dynamics during phase separation of an elastomeric protein.Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Contribution of domain 30 of tropoelastin to elastic fiber formation and material elasticity.The Coupled Bio-Chemo-Electro-Mechanical Behavior of Glucose Exposed Arterial Elastin.Quarterly intrinsic disorder digest (April-May-June, 2014).Is quercetin an alternative natural crosslinking agent to genipin for long-term dermal scaffolds implantation?Fusion of fibroblast growth factor 21 to a thermally responsive biopolymer forms an injectable depot with sustained anti-diabetic action.

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P2860

Conformational transitions of the cross-linking domains of elastin during self-assembly

http://www.wikidata.org/entity/Q30359229

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

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2014年論文

@zh-tw

2014年论文

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name

Conformational transitions of the cross-linking domains of elastin during self-assembly

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Conformational transitions of the cross-linking domains of elastin during self-assembly

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type

label

Conformational transitions of the cross-linking domains of elastin during self-assembly

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Conformational transitions of the cross-linking domains of elastin during self-assembly

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prefLabel

Conformational transitions of the cross-linking domains of elastin during self-assembly

@ast

Conformational transitions of the cross-linking domains of elastin during self-assembly

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JBC.M113.533893

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Journal of Biological Chemistry

P1476

Conformational transitions of the cross-linking domains of elastin during self-assembly

@en

P2093

Fred W Keeley

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Karen Simonetti

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

Lisa D Muiznieks

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Richard Stahl

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Sean E Reichheld

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Simon Sharpe

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P2860

Probability-based protein secondary structure identification using combined NMR chemical-shift data

Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

The CCPN data model for NMR spectroscopy: development of a software pipeline

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Prediction of protein conformation

Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.

Structure and energetics of the hydrogen-bonded backbone in protein folding.

Backbone motion in elastin's hydrophobic domains as detected by (2) H NMR spectroscopy.

Solid-state (13)C NMR reveals effects of temperature and hydration on elastin

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10057-10068

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scholarly article

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10.1074/JBC.M113.533893

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