Antivascular and antitumor properties of the tubulin-binding chalcone TUB091 - Wikidata - awgldk - TriplyDB

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

http://www.wikidata.org/entity/Q27705273

about

Capsaicin synergizes with camptothecin to induce increased apoptosis in human small cell lung cancers via the calpain pathway.Chalcone Derivatives: Promising Starting Points for Drug Design.Chalcone: A Privileged Structure in Medicinal Chemistry.2-Amino-3-methylcarboxy-5-heptyl-thiophene (TJ191) is a selective anti-cancer small molecule that targets low TβRIII-expressing malignant T-cell leukemia/lymphoma cells.The "Yin and Yang" of Natural Compounds in Anticancer Therapy of Triple-Negative Breast Cancers

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Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

http://www.wikidata.org/entity/Q27705273

description

2016 nî lūn-bûn

@nan

2016 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի մայիսին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

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name

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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type

label

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

@en

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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prefLabel

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

@ast

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

@en

Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

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ONCOTARGET.9527

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Antivascular and antitumor properties of the tubulin-binding chalcone TUB091

@en

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Andrea E Prota

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

Domenico Ribatti

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

Gonzalo Sáez-Calvo

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

Katja Bargsten

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

María-Dolores Canela

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

María-José Camarasa

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

María-Luisa Jimeno

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

Oskía Bueno

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

Sandra Liekens

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

Sonsoles Velázquez

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

P2860

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Refined structure of alpha beta-tubulin at 3.5 A resolution

Variations in the colchicine-binding domain provide insight into the structural switch of tubulin

A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end

A TOG: -tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase

Structural basis of tubulin tyrosination by tubulin tyrosine ligase

Molecular mechanism of action of microtubule-stabilizing anticancer agents

The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization

Microtubule-binding agents: a dynamic field of cancer therapeutics.

Structure of the alpha beta tubulin dimer by electron crystallography

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14325-14342

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scholarly article

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10.18632/ONCOTARGET.9527

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9

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8

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Eva-María Priego

Michel O Steinmetz

Maria-Jésus Pérez-Pérez

Mohammed Benkheil

J. Fernando Díaz

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2017-02-01T00:00:00Z

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27224920

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5362409

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