Monomeric and dimeric states exhibited by the kinesin-related motor protein KIF1A
Author:
Publisher
Wiley
Subject
Endocrinology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.2005.00255.x/fullpdf
Reference20 articles.
1. Reconstitution of Membrane Transport Powered by a Novel Dimeric Kinesin Motor of the Unc104/Kif1a Family Purified from Dictyostelium
2. The Kinesin-like Motor Protein KIF1C Occurs in Intact Cells as a Dimer and Associates with Proteins of the 14-3-3 Family
3. Direct Visualization of the Movement of the Monomeric Axonal Transport Motor UNC-104 along Neuronal Processes in LivingCaenorhabditis elegans
4. Characterization of the Movement of the Kinesin Motor KIF1A in Living Cultured Neurons
5. Conversion of Unc104/KIF1A Kinesin into a Processive Motor After Dimerization
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1. Positive charge in the K-loop of the kinesin-3 motor KIF1A regulates superprocessivity by enhancing microtubule affinity in the one-head–bound state;Journal of Biological Chemistry;2023-02
2. Advances in the study of axon–associated vesicles;Frontiers in Molecular Neuroscience;2022-12-05
3. The net charge of the K-loop regulates KIF1A superprocessivity by enhancing microtubule affinity in the one-head-bound state;2022-08-21
4. Motor domain-mediated autoinhibition dictates axonal transport by the kinesin UNC-104/KIF1A;PLOS Genetics;2021-11-29
5. A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle;Journal of Biological Chemistry;2020-12
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