The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch
Published 2015 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch
Authors
Keywords
-
Journal
eLife
Volume 4, Issue -, Pages -
Publisher
eLife Sciences Organisation, Ltd.
Online
2015-04-27
DOI
10.7554/elife.06421
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Nucleotide Exchange in Dimeric MCAK Induces Longitudinal and Lateral Stress at Microtubule Ends to Support Depolymerization
- (2014) Kyle M. Burns et al. STRUCTURE
- Microtubule-Depolymerizing Kinesins
- (2013) Claire E. Walczak et al. Annual Review of Cell and Developmental Biology
- Aurora B Inhibits MCAK Activity through a Phosphoconformational Switch that Reduces Microtubule Association
- (2013) Stephanie C. Ems-McClung et al. CURRENT BIOLOGY
- The molecular basis for kinesin functional specificity during mitosis
- (2013) Julie P. I. Welburn Cytoskeleton
- A Second Tubulin Binding Site on the Kinesin-13 Motor Head Domain Is Important during Mitosis
- (2013) Dong Zhang et al. PLoS One
- Structural Model for Tubulin Recognition and Deformation by Kinesin-13 Microtubule Depolymerases
- (2013) Ana B. Asenjo et al. Cell Reports
- The microtubule-binding protein Cep170 promotes the targeting of the kinesin-13 depolymerase Kif2b to the mitotic spindle
- (2012) Julie P. I. Welburn et al. MOLECULAR BIOLOGY OF THE CELL
- Depolymerizing Kinesins Kip3 and MCAK Shape Cellular Microtubule Architecture by Differential Control of Catastrophe
- (2011) Melissa K. Gardner et al. CELL
- Mitotic Centromere-associated Kinesin (MCAK) Mediates Paclitaxel Resistance
- (2011) Anutosh Ganguly et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Overexpression of Mitotic Centromere-Associated Kinesin Stimulates Microtubule Detachment and Confers Resistance to Paclitaxel
- (2011) A. Ganguly et al. MOLECULAR CANCER THERAPEUTICS
- The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition
- (2011) H. Y. K. Kaan et al. SCIENCE
- XDS
- (2010) Wolfgang Kabsch ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Phosphorylation of mammalian Sgo2 by Aurora B recruits PP2A and MCAK to centromeres
- (2010) Y. Tanno et al. GENES & DEVELOPMENT
- PLK1 Phosphorylates Mitotic Centromere-associated Kinesin and Promotes Its Depolymerase Activity
- (2010) Liangyu Zhang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Functional and Spatial Regulation of Mitotic Centromere- Associated Kinesin by Cyclin-Dependent Kinase 1
- (2010) Mourad Sanhaji et al. MOLECULAR AND CELLULAR BIOLOGY
- Aurora B Phosphorylates Spatially Distinct Targets to Differentially Regulate the Kinetochore-Microtubule Interface
- (2010) Julie P.I. Welburn et al. MOLECULAR CELL
- Half-Site Inhibition of Dimeric Kinesin Head Domains by Monomeric Tail Domains†
- (2009) David D. Hackney et al. BIOCHEMISTRY
- A new model for binding of kinesin 13 to curved microtubule protofilaments
- (2009) Anke M. Mulder et al. JOURNAL OF CELL BIOLOGY
- Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK
- (2009) Jeremy R Cooper et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Aurora A Phosphorylates MCAK to Control Ran-dependent Spindle Bipolarity
- (2008) Xin Zhang et al. MOLECULAR BIOLOGY OF THE CELL
- Phosphorylation Relieves Autoinhibition of the Kinetochore Motor Cenp-E
- (2008) Julien Espeut et al. MOLECULAR CELL
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreFind the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
Search