ArticleThe EMBO journal2001
Analysis of heterodimer formation by Xklp3A/B, a newly cloned kinesin-II from Xenopus laevis.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 37 citations in OpenAlex.
- 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
- Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025Article
- A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport.Nature communications · 2025Article
- Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020Review
- Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control ineLife · 2020Article
- Kinesin-2 motors adapt their stepping behavior for processive transport on axonemes and microtubules.EMBO reports · 2017Article
- Intraflagellar transport velocity is governed by the number of active KIF17 and KIF3AB motors and their motility properties under load.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Biochemical and molecular dynamic simulation analysis of a weak coiled coil association between kinesin-II stalks.PloS one · 2012Article
- How kinesin-2 forms a stalk.Molecular biology of the cell · 2011Article
- Torque generation by one of the motor subunits of heterotrimeric kinesin-2.Biochemical and biophysical research communications · 2010Article
- Cryo-electron tomography of microtubule-kinesin motor complexes.Journal of structural biology · 2010Article
- Multiple kinesin motors coordinate cytoplasmic RNA transport on a subpopulation of microtubules in Xenopus oocytes.Developmental cell · 2008Article
- Tracking melanosomes inside a cell to study molecular motors and their interaction.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Stability and specificity of heterodimer formation for the coiled-coil neck regions of the motor proteins Kif3A and Kif3B: the role of unstructured oppositely charged regions.The journal of peptide research : official journal of the American Peptide Society · 2005Article
- The two motor domains of KIF3A/B coordinate for processive motility and move at different speeds.Biophysical journal · 2004Article
- Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragment.EMBO reports · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
kinesin-II motor proteins are composed of two different kinesin-like motor proteins and one cargo binding subunit. Here we report the cloning of a new member of the kinesin-II superfamily, Xklp3A from Xenopus laevis, which forms a heterodimeric complex with Xklp3B. The heterodimer formation properties between Xklp3A and B have been tested in vitro using reticulocyte lysate expression and immunoprecipitation. To this end we produced a series of Xklp3A and B constructs of varying length and tested their propensity for heterodimer formation. We could demonstrate that, in contrast to conventional kinesin, the critical domains for heterodimer formation in Xklp3A/B are located at the C-terminal end of the stalk. Neither the neck nor the highly charged stretches after the neck region, which are typical of kinesins-II, are required for heterodimer formation, nor do they prevent homodimer formation. Dimerization is controlled by a cooperative mechanism between the C-terminal coiled-coil segments. Classical trigger sites were not identified. The critical regions for dimerization exhibit a very high degree of sequence conservation among equivalent members of the kinesin-II family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.