Structural insight into the inhibition of tubulin by vinca domain peptide ligands - Wikidata - awgldk - TriplyDB

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

http://www.wikidata.org/entity/Q27652119

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CLASP2 Has Two Distinct TOG Domains That Contribute Differently to Microtubule Dynamics Eribulin binds at microtubule ends to a single site on tubulin to suppress dynamic instability Variations in the colchicine-binding domain provide insight into the structural switch of tubulin Stathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin Dimers Structural plasticity of tubulin assembly probed by vinca-domain ligands Microtubule-binding agents: a dynamic field of cancer therapeutics.Structural Insights into the Pharmacophore of Vinca Domain Inhibitors of Microtubules Structural Basis of Microtubule Destabilization by Potent Auristatin Anti-Mitotics Maytansine and cellular metabolites of antibody-maytansinoid conjugates strongly suppress microtubule dynamics by binding to microtubules Synthesis and Cytotoxicity Evaluation of C4- and C5-Modified Analogues of the α,β-Unsaturated Lactone of Pironetin A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs A previously undescribed tubulin binder Structure-activity relationships of ustiloxin analogues.Synthesis and biological evaluation of benzo[b]furans as inhibitors of tubulin polymerization and inducers of apoptosis.Interactions of halichondrin B and eribulin with tubulin.Drugs that target dynamic microtubules: a new molecular perspective Design and synthesis of imidazo[2,1-b]thiazole-chalcone conjugates: microtubule-destabilizing agents.Tubulin inhibitor identification by bioactive conformation alignment pharmacophore-guided virtual screening.Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.Structures of potent anticancer compounds bound to tubulin SYNTHESIS AND BIOLOGICAL EVALUATION OF BIARYL ANALOGS OF ANTITUBULIN COMPOUNDS Biosynthetic investigation of phomopsins reveals a widespread pathway for ribosomal natural products in Ascomycetes.Novel Azetidine-Containing TZT-1027 Analogues as Antitumor Agents.Mechanism for the catastrophe-promoting activity of the microtubule destabilizer Op18/stathmin New microtubule-inhibiting anticancer agents.The tubulin colchicine domain: a molecular modeling perspective.Molecular simulations of drug-receptor complexes in anticancer research.Synthesis and evaluation of hybrid molecules targeting the vinca domain of tubulin.Synthesis and biological evaluation of imidazo[2,1-b][1,3,4]thiadiazole-linked oxindoles as potent tubulin polymerization inhibitors.Synthesis and cytotoxic activity of 2-anilinopyridine-3-acrylamides as tubulin polymerization inhibitors.Classification of ligand molecules in PDB with graph match-based structural superposition.(-)-Rhazinilam and the diphenylpyridazinone NSC 613241: Two compounds inducing the formation of morphologically similar tubulin spirals but binding apparently to two distinct sites on tubulin.The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration Relating nucleotide-dependent conformational changes in free tubulin dimers to tubulin assembly.Design, Synthesis, and Cytotoxic Evaluation of Novel Tubulysin Analogues as ADC Payloads.Drug–tubulin interactions interrogated by transient absorption spectroscopy Marine Peptides and Proteins with Cytotoxic and Antitumoral Properties

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P2860

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

http://www.wikidata.org/entity/Q27652119

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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type

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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Structural insight into the inhibition of tubulin by vinca domain peptide ligands

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P1476

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

@en

P2093

Anthony Cormier

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

Benoît Gigant

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

Marcel Knossow

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

Matthieu Marchand

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

Raimond B G Ravelli

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

P2860

The 4 A X-ray structure of a tubulin:stathmin-like domain complex

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

Dynamic instability of microtubule growth

High-resolution model of the microtubule

Tumor-specific antivascular effect of TZT-1027 (Soblidotin) elucidated by magnetic resonance imaging and confocal laser scanning microscopy.

Evolution of the total syntheses of ustiloxin natural products and their analogues

Synchronous oscillations in microtubule polymerization

Tubulin and FtsZ form a distinct family of GTPases.

Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B.

Interference of GTP hydrolysis in the mechanism of microtubule assembly: an experimental study

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1101-6

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scholarly article

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2011987

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10.1038/EMBOR.2008.171

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11

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9

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2008-11-01T00:00:00Z

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23253469

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18787557

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2581847

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