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Microtubule-Destabilizing Agents: Structural and Mechanistic Insights from the Interaction of Colchicine and Vinblastine with Tubulin

https://doi.org/10.1007/128_2008_11

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Structural Basis of the Activity of the Microtubule‐Stabilizing Agent Epothilone A Studied by NMR Spectroscopy in Solution

inferredcites →https://doi.org/10.1006/jmbi.2001.5077openalex-snapshot

Refined structure of αβ-tubulin at 3.5 Å resolution 1 1Edited by I. A. Wilson

inferredcites →https://doi.org/10.1007/978-1-59745-442-1_16openalex-snapshot

Studying Drug-Tubulin Interactions by X-Ray Crystallography

inferredcites →https://doi.org/10.1007/bf00234410openalex-snapshot

Guanosine-5?-triphosphate hydrolysis and tubulin polymerization

inferredcites →https://doi.org/10.1007/s002490050154openalex-snapshot

General features of the recognition by tubulin of colchicine and related compounds

inferredcites →https://doi.org/10.1016/0006-291x(81)91697-1openalex-snapshot

GTPase activity of the tubulin-colchicine in relation with tubulin-tubulin interactions

inferredcites →https://doi.org/10.1016/0014-4827(73)90269-3openalex-snapshot

Potentiation of vinblastine crystal formation in vivo by puromycin and colcemid

inferredcites →https://doi.org/10.1016/0022-2836(82)90035-3openalex-snapshot

Interaction of vinblastine with steady-state microtubules in vitro

inferredcites →https://doi.org/10.1016/0022-2836(84)90248-1openalex-snapshot

Arrangement of protofilaments in two forms of tubulin crystal induced by vinblastine

inferredcites →https://doi.org/10.1016/0163-7258(92)90028-xopenalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.ab.2004.06.033openalex-snapshot

Mass spectrometric measurement of differential reactivity of cysteine to localize protein–ligand binding sites.

inferredcites →https://doi.org/10.1016/j.bmc.2005.09.069openalex-snapshot

Identification of 12Cysβ on tubulin as the binding site of tubulyzine

inferredcites →https://doi.org/10.1016/j.ceb.2004.11.001openalex-snapshot

Microtubule plus-end-tracking proteins: mechanisms and functions

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Microtubule polymerases and depolymerases

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CLIP-170/Tubulin-Curved Oligomers Coassemble at Microtubule Ends and Promote Rescues

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Microtubule Assembly Dynamics at the Nanoscale

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Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1

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Interfacial inhibition of macromolecular interactions: nature's paradigm for drug discovery

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Effect of antimitotic drugs on tubulin GTPase activity and self-assembly.

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[26] Raster3D: Photorealistic molecular graphics

inferredcites →https://doi.org/10.1016/s0092-8674(00)00069-6openalex-snapshot

The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex

inferredcites →https://doi.org/10.1016/s0092-8674(00)80961-7openalex-snapshot

High-Resolution Model of the Microtubule

inferredcites →https://doi.org/10.1016/s0959-440x(03)00029-0openalex-snapshot

Tubulin rings: which way do they curve?

inferredcites →https://doi.org/10.1016/s0969-2126(02)00827-4openalex-snapshot

Microtubule Structure at 8 Å Resolution

inferredcites →https://doi.org/10.1016/s1074-5521(02)00284-3openalex-snapshot

Small Molecules, Big Impact

inferredcites →https://doi.org/10.1021/bi00062a003openalex-snapshot

Assembly of purified GDP-tubulin into microtubules induced by taxol and taxotere: Reversibility, ligand stoichiometry, and competition

inferredcites →https://doi.org/10.1021/bi00118a015openalex-snapshot

Mechanism of inhibition of microtubule polymerization by colchicine: inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes

inferredcites →https://doi.org/10.1021/bi00541a030openalex-snapshot

Polymerization of the tubulin-colchicine complex and guanosine 5'-triphosphate hydrolysis

inferredcites →https://doi.org/10.1021/bi0487387openalex-snapshot

Localization of the Antimitotic Peptide and Depsipeptide Binding Site on β-Tubulin

inferredcites →https://doi.org/10.1021/bi060334mopenalex-snapshot

The Nucleotide Switch of Tubulin and Microtubule Assembly: A Polymerization-Driven Structural Change

inferredcites →https://doi.org/10.1021/bi701147fopenalex-snapshot

Insight into the GTPase Activity of Tubulin from Complexes with Stathmin-like Domains

inferredcites →https://doi.org/10.1021/bi961325oopenalex-snapshot

Continuous Monitoring of Pi Release Following Nucleotide Hydrolysis in Actin or Tubulin Assembly Using 2-Amino-6-mercapto-7-methylpurine Ribonucleoside and Purine-Nucleoside Phosphorylase as an Enzyme-Linked Assay

inferredcites →https://doi.org/10.1021/bi971491bopenalex-snapshot

Stathmin: A Tubulin-Sequestering Protein Which Forms a Ternary T2S Complex with Two Tubulin Molecules

inferredcites →https://doi.org/10.1021/bi9830765openalex-snapshot

Phosphate Release during Microtubule Assembly: What Stabilizes Growing Microtubules?

inferredcites →https://doi.org/10.1021/jm050502topenalex-snapshot

A Common Pharmacophore for a Diverse Set of Colchicine Site Inhibitors Using a Structure-Based Approach

inferredcites →https://doi.org/10.1021/jm050761iopenalex-snapshot

Design and Biological Evaluation of Novel Tubulin Inhibitors as Antimitotic Agents Using a Pharmacophore Binding Model with Tubulin

inferredcites →https://doi.org/10.1038/277665a0openalex-snapshot

Promotion of microtubule assembly in vitro by taxol

inferredcites →https://doi.org/10.1038/34465openalex-snapshot

Structure of the αβ tubulin dimer by electron crystallography

inferredcites →https://doi.org/10.1038/embor.2008.171openalex-snapshot

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

inferredcites →https://doi.org/10.1038/nature02393openalex-snapshot

Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain

inferredcites →https://doi.org/10.1038/nature03566openalex-snapshot

Structural basis for the regulation of tubulin by vinblastine

inferredcites →https://doi.org/10.1038/nature03606openalex-snapshot

Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly

inferredcites →https://doi.org/10.1038/nature04928openalex-snapshot

Assembly dynamics of microtubules at molecular resolution

inferredcites →https://doi.org/10.1038/nature06386openalex-snapshot

Reconstitution of a microtubule plus-end tracking system in vitro

inferredcites →https://doi.org/10.1038/nsb0698-451openalex-snapshot

Tubulin and FtsZ form a distinct family of GTPases

inferredcites →https://doi.org/10.1073/pnas.74.12.5372openalex-snapshot

Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.

inferredcites →https://doi.org/10.1074/jbc.271.44.27677openalex-snapshot

Metal Binding Properties of a Monoclonal Antibody Directed toward Metal-Chelate Complexes

inferredcites →https://doi.org/10.1074/jbc.271.6.2897openalex-snapshot

Thermodynamics of Colchicinoid-Tubulin Interactions

inferredcites →https://doi.org/10.1074/jbc.m204263200openalex-snapshot

The Local Electrostatic Environment Determines Cysteine Reactivity of Tubulin

inferredcites →https://doi.org/10.1074/jbc.m402110200openalex-snapshot

Direct Photoaffinity Labeling by Dolastatin 10 of the Amino-terminal Peptide of β-Tubulin Containing Cysteine 12

inferredcites →https://doi.org/10.1074/jbc.m407816200openalex-snapshot

Macromolecular Accessibility of Fluorescent Taxoids Bound at a Paclitaxel Binding Site in the Microtubule Surface

inferredcites →https://doi.org/10.1074/jbc.m704101200openalex-snapshot

Heightened Sensitivity to Paclitaxel in Class IVa β-Tubulin-transfected Cells Is Lost as Expression Increases

inferredcites →https://doi.org/10.1083/jcb.114.5.977openalex-snapshot

Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study.

inferredcites →https://doi.org/10.1083/jcb.146.6.1289openalex-snapshot

Op18/Stathmin Mediates Multiple Region-Specific Tubulin and Microtubule-Regulating Activities

inferredcites →https://doi.org/10.1091/mbc.11.5.1887openalex-snapshot

Structure–Function Relationships in Yeast Tubulins

inferredcites →https://doi.org/10.1091/mbc.3.10.1155openalex-snapshot

Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP.

inferredcites →https://doi.org/10.1093/emboj/19.4.572openalex-snapshot

Op18/stathmin caps a kinked protofilament‐like tubulin tetramer

inferredcites →https://doi.org/10.1107/s0021889891004399openalex-snapshot

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

inferredcites →https://doi.org/10.1111/j.1432-1033.1986.tb09721.xopenalex-snapshot

Binding of gossypol to purified tubulin and inhibition of its assembly into microtubules

inferredcites →https://doi.org/10.1126/science.1099190openalex-snapshot

The Binding Mode of Epothilone A on α,ß-Tubulin by Electron Crystallography

inferredcites →https://doi.org/10.1139/o90-197openalex-snapshot

The discovery of the vinca alkaloids—chemotherapeutic agents against cancer

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MICROTUBULE POLYMERIZATION DYNAMICS

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Amino acid substitutions at proline 220 of β-tubulin confer resistance to paclitaxel and colcemid

inferredcites →https://doi.org/10.1242/jcs.47.1.237openalex-snapshot

Spirals and paracrystals induced by vinca alkaloids: evidence that microtubule-associated proteins act as polycations

inferredcites →https://doi.org/10.1247/csf.24.265openalex-snapshot

Tubulin 30 Years Later

inferredcites →https://doi.org/10.1247/csf.24.299openalex-snapshot

Microtubule's Conformational Cap.

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Modulation of Microtubule Dynamics by Drugs. A Paradigm for the Actions of Cellular Regulators.

inferredcites →https://doi.org/10.2174/1568011023354263openalex-snapshot

Antimitotic Peptides and Depsipeptides

inferredcites →https://doi.org/10.2174/1568011023354290openalex-snapshot

Mechanism of Action of Antitumor Drugs that Interact with Microtubules and Tubulin

inferredcites →https://doi.org/10.2174/187152007780058650openalex-snapshot

Recent Progress in Discovery and Development of Antimitotic Agents

inferredcites →https://doi.org/10.4161/cc.6.17.4633openalex-snapshot

The Tubulin Code

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Additional file 1 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 2 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 3 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 4 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 5 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 6 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 7 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

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Additional file 8 of CDK6-PI3K signaling axis is an efficient target for attenuating ABCB1/P-gp mediated multi-drug resistance (MDR) in cancer cells

inferred← citeshttps://doi.org/10.6084/m9.figshare.20381869openalex-snapshot

Additional file 1 of Preliminary mechanistic insights of a brain-penetrant microtubule imaging PET ligand in a tau-knockout mouse model

inferred← citeshttps://doi.org/10.70675/48cfd5e7z542dz4aebz8922z3b14d21430d3openalex-snapshot

Synthèse et évaluation pharmacologique de composés originaux de la famille des méthoxynaphtalènes et lignanes arylnaphtalènes à visée antitumorale

inferred← citeshttps://doi.org/10.7554/elife.01637openalex-snapshot

The Caenorhabditis elegans microtubule minus-end binding homolog PTRN-1 stabilizes synapses and neurites

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