ArticleThe Journal of biological chemistry2016
Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Heterotrimeric kinesin-2 autoinhibition mediated by interactions of the CC2 and proximal tail domains with the motor domains is essential for cilium formation and maintenance.bioRxiv : the preprint server for biology · 2026Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors.Molecules (Basel, Switzerland) · 2019Article
- Kinesin-2 heterodimerization alters entry into a processive run along the microtubule but not stepping within the run.The Journal of biological chemistry · 2018Article
- Emerging mechanisms of dynein transport in the cytoplasm versus the cilium.Biochemical Society transactions · 2018Review
- Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018Review
- Intraflagellar transport: mechanisms of motor action, cooperation, and cargo delivery.The FEBS journal · 2017Review
- Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements.Nature structural & molecular biology · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Mammalian KIF3AB is an N-terminal processive kinesin-2 that is best known for its roles in intracellular transport. There has been significant interest in KIF3AB to define the key principles that underlie its processivity but also to define the mechanistic basis of its sensitivity to force. In this study, the kinetics for entry into the processive run were quantified. The results show for KIF3AB that the kinetics of microtubule association at 7 μm
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Registered trials
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