Functional characterization of ECP-heparin interaction: a novel molecular model - Test2 - elhamkhani - TriplyDB

Functional characterization of ECP-heparin interaction: a novel molecular model

Functional characterization of ECP-heparin interaction: a novel molecular model

http://www.wikidata.org/entity/Q35070393

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Docking server for the identification of heparin binding sites on proteins.Cell Penetrating Peptide Derived from Human Eosinophil Cationic Protein Decreases Airway Allergic Inflammation.

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P2860

Functional characterization of ECP-heparin interaction: a novel molecular model

http://www.wikidata.org/entity/Q35070393

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2013 nî lūn-bûn

@nan

2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Functional characterization of ECP-heparin interaction: a novel molecular model

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Functional characterization of ECP-heparin interaction: a novel molecular model

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type

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Functional characterization of ECP-heparin interaction: a novel molecular model

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Functional characterization of ECP-heparin interaction: a novel molecular model

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Functional characterization of ECP-heparin interaction: a novel molecular model

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Functional characterization of ECP-heparin interaction: a novel molecular model

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JOURNAL.PONE.0082585

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Functional characterization of ECP-heparin interaction: a novel molecular model

@en

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Margaret Dah-Tsyr Chang

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

Noboru Tomiya

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

Pei-Chun Lien

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

Ping-Hsueh Kuo

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Sim-Kun Ng

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Ta-Jen Hung

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Tse-Hao Chang

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Wen-Chi Cheng

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Yuan-Chuan Lee

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P2860

Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family

Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease

INTEGRATOR: interactive graphical search of large protein interactomes over the Web.

Crystal structure of eosinophil cationic protein at 2.4 A resolution

Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution

Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN). High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors

Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different heparan sulfate motifs

Atomic resolution (0.98 A) structure of eosinophil-derived neurotoxin

The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site

The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopy

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e82585

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scholarly article

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10.1371/JOURNAL.PONE.0082585

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12

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8

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2013-12-11T00:00:00Z

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259355002

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24349317

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3859622

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