Stathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin Dimers*
Open Access
- 8 October 2010
- journal article
- Published by Elsevier BV
- Vol. 285 (41), 31672-31681
- https://doi.org/10.1074/jbc.m110.141929
Abstract
No abstract availableThis publication has 66 references indexed in Scilit:
- Mechanisms of force generation by end-on kinetochore-microtubule attachmentsCurrent Opinion in Cell Biology, 2010
- Variations in the colchicine-binding domain provide insight into the structural switch of tubulinProceedings of the National Academy of Sciences of the United States of America, 2009
- Detection of GTP-Tubulin Conformation in Vivo Reveals a Role for GTP Remnants in Microtubule RescuesScience, 2008
- Structural insight into the inhibition of tubulin by vinca domain peptide ligandsEMBO Reports, 2008
- Stathmin/Op18 is a novel mediator of vinblastine activityFEBS Letters, 2008
- The lattice as allosteric effector: Structural studies of αβ- and γ-tubulin clarify the role of GTP in microtubule assemblyProceedings of the National Academy of Sciences of the United States of America, 2008
- Visualisation of a Kinesin-13 Motor on Microtubule End MimicsJournal of Molecular Biology, 2008
- Purification of brain tubulin through two cycles of polymerization–depolymerization in a high-molarity bufferProtein Expression and Purification, 2003
- Use of TLS parameters to model anisotropic displacements in macromolecular refinementActa Crystallographica Section D-Biological Crystallography, 2001
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994