ArticleThe EMBO journal2001
Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa.
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 15 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
15 citing papers in PubMed, 41 citations in OpenAlex.
- A Kinesin Vdkin2 Required for Vacuole Formation, Mycelium Growth, and Penetration Structure Formation ofJournal of fungi (Basel, Switzerland) · 2022Article
- Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022Review
- Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run.The Journal of biological chemistry · 2016Article
- Kinesin walks the line: single motors observed by atomic force microscopy.Biophysical journal · 2011Article
- Autoinhibition of the kinesin-2 motor KIF17 via dual intramolecular mechanisms.The Journal of cell biology · 2010Article
- Mammalian Kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition.PLoS biology · 2009Article
- Dissection of kinesin's processivity.PloS one · 2009Article
- Formation and reversible dissociation of coiled coil of peptide to the C-terminus of the HSV B5 protein: a time-resolved spectroscopic analysis.Biophysical journal · 2007Article
- Flexibility of the neck domain enhances Kinesin-1 motility under load.Biophysical journal · 2006Article
- Review: regulation mechanisms of Kinesin-1.Journal of muscle research and cell motility · 2006Review
- The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.Biophysical journal · 2005Article
- The complex interplay between the neck and hinge domains in kinesin-1 dimerization and motor activity.Molecular biology of the cell · 2005Article
- Article
- Single fungal kinesin motor molecules move processively along microtubules.Biophysical journal · 2003Article
- A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core.The EMBO journal · 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
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungal conventional kinesins are unusually fast microtubule motor proteins. To compare the functional organization of fungal and animal conventional kinesins, a set of C-terminal deletion mutants of the Neurospora crassa conventional kinesin, NcKin, was investigated for its biochemical and biophysical properties. While the shortest, monomeric construct comprising the catalytic core and the neck-linker (NcKin343) displays very high steady-state ATPase (k(cat) = 260/s), constructs including both the full neck and adjacent hinge domains (NcKin400, NcKin433 and NcKin480) show wild-type behaviour: they are dimeric, show fast gliding and slower ATP turnover rates (k(cat) = 60-84/s), and are chemically processive. Unexpectedly, a construct (NcKin378, corresponding to Drosophila KHC381) that includes just the entire coiled-coil neck is a monomer. Its ATPase activity is slow (k(cat) = 27/s), and chemical processivity is abolished. Together with a structural analysis of synthetic neck peptides, our data demonstrate that the NcKin neck domain behaves differently from that of animal conventional kinesins and may be tuned to drive fast, processive motility.
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.