Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Alternate fast and slow stepping of a heterodimeric kinesin molecule.

Nature cell biology - 1 Dec 2003

Kaseda Kuniyoshi, Higuchi Hideo, Hirose Keiko

Abstract excerpt

A conventional kinesin molecule travels continuously along a microtubule in discrete 8-nm steps. This processive movement is generally explained by models in which the two identical heads of a kinesin move in a 'hand-over-hand' manner. Here, we show that a single heterodimeric kinesin molecule (in which one of the two heads is mutated in a nucleotide-binding site) exhibits fast and slow (with the dwell time at...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Dimerization
Share to Kinesins
Share to Microtubules

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Conformation

Share to Molecular Motor Proteins

Share to Protein Transport

Share to Time Factors

Source

Identifiers

PMID: 14634664
DOI: 10.1038/ncb1067

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alternate fast and slow stepping of a heterodimeric kinesin molecule.PMID 14634664Read ↗

Direct observation of intermediate states during the stepping motion of kinesin-1.Semantic proximity Read ↗

Kinesin walks hand-over-hand.Semantic proximity Read ↗

Rapid double 8-nm steps by a kinesin mutant.Semantic proximity Read ↗

Dynamics of dimeric kinesins: Limping, effect of longitudinal force, effects of neck linker extension and mutation, and comparison between kinesin-1 and kinesin-2.Semantic proximity Read ↗

Asymmetry in kinesin walking.Semantic proximity Read ↗

Measuring kinesin's first step.Semantic proximity Read ↗

The role of ATP hydrolysis for kinesin processivity.Semantic proximity Read ↗

Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin.Semantic proximity Read ↗

Model for kinetics of wild-type and mutant kinesins.Semantic proximity Read ↗

Interaction between motor domains can explain the complex dynamics of heterodimeric kinesins.Semantic proximity Read ↗

Modular photostable fluorescent DNA blocks dissect the effects of pathogenic mutant kinesin on collective transportSemantic proximity Read ↗

Neck-region–microtubule interactions direct counterclockwise stepping of kinesin-1Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.