The kinesin-13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization

The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK

(2011) Kathleen M. Hertzer et al.   CELL CYCLE

An atomic-level mechanism for activation of the kinesin molecular motors

(2010) C. V. Sindelar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

ATPase Cycle of the Nonmotile Kinesin NOD Allows Microtubule End Tracking and Drives Chromosome Movement

(2009) Jared C. Cochran et al.   CELL

Mitotic Microtubule Crosslinkers: Insights from Mechanistic Studies

(2009) Erwin J.G. Peterman et al.   CURRENT BIOLOGY

Kinesin superfamily motor proteins and intracellular transport

(2009) Nobutaka Hirokawa et al.   NATURE REVIEWS MOLECULAR 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

Structures of kinesin motor proteins

(2009) Alexander Marx et al.   CELL MOTILITY AND THE CYTOSKELETON

A kinesin-13 mutant catalytically depolymerizes microtubules in ADP

(2008) Michael Wagenbach et al.   JOURNAL OF CELL BIOLOGY

Visualisation of a Kinesin-13 Motor on Microtubule End Mimics

(2008) Carolyn A. Moores et al.   JOURNAL OF MOLECULAR BIOLOGY