Structural insight into the inhibition of tubulin by vinca domain peptide ligands-Reference-Cited by-同舟云学术

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

Published:2008-09-12 Issue:11 Volume:9 Page:1101-1106
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Cormier Anthony¹,Marchand Matthieu¹,Ravelli Raimond B G²³,Knossow Marcel¹,Gigant Benoît¹

Affiliation:

1. Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), CNRS, Bat. 34 1 avenue de la Terrasse 91198 Gif‐sur‐Yvette France

2. European Molecular Biology Laboratory (EMBL), Grenoble Outstation 6 rue Jules Horowitz, BP 181 38042 Grenoble France

3. Section for Electron Microscopy, Leiden University Medical Center (LUMC) 2333 ZC Einthovenweg 20 Leiden The Netherlands

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1038/embor.2008.171

Reference28 articles.

1. Stathmin Slows down Guanosine Diphosphate Dissociation from Tubulin in a Phosphorylation-Controlled Fashion

2. Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites;Bai RL;J Biol Chem,1990

3. Structure-activity studies with chiral isomers and with segments of the antimitotic marine peptide dolastatin 10

4. Differential effects of active isomers, segments, and analogs of dolastatin 10 on ligand interactions with tubulin

5. Interactions of the Sponge-Derived Antimitotic Tripeptide Hemiasterlin with Tubulin: Comparison with Dolastatin 10 and Cryptophycin 1

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