ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2000
Searching for kinesin's mechanical amplifier.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 36 citations in OpenAlex.
- Intracellular Cargo Transport by Kinesin-3 Motors.Biochemistry. Biokhimiia · 2017Review
- Structural Correlation of the Neck Coil with the Coiled-coil (CC1)-Forkhead-associated (FHA) Tandem for Active Kinesin-3 KIF13A.The Journal of biological chemistry · 2016Article
- Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites.Biophysical journal · 2014Article
- The molecular basis for kinesin functional specificity during mitosis.Cytoskeleton (Hoboken, N.J.) · 2013Review
- Mapping the structural and dynamical features of kinesin motor domains.PLoS computational biology · 2013Article
- Reconstructing the phylogeny of 21 completely sequenced arthropod species based on their motor proteins.BMC genomics · 2009Article
- The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly.Molecular biology of the cell · 2007Article
- A comparative study of motor-protein motions by using a simple elastic-network model.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Switch-based mechanism of kinesin motors.Nature · 2001Article
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 2 institutions in 1 country.
Funding
Abstract
Kinesin, a microtubule-based motor, and myosin, an actin-based motor, share a similar core structure, indicating that they arose from a common ancestor. However, kinesin lacks the long lever-arm domain that is believed to drive the myosin power stroke. Here, we present evidence that a much smaller region of ca. 10-40 amino acids serves as a mechanical element for kinesin motor proteins. These 'neck regions' are class conserved and have distinct structures in plus-end and minus-end-directed kinesin motors. Mutagenesis studies also indicate that the neck regions are involved in coupling ATP hydrolysis and energy into directional motion along the microtubule. We suggest that the kinesin necks drive motion by undergoing a conformational change in which they detach and re-dock onto the catalytic core during the ATPase cycle. Thus, kinesin and myosin have evolved unique mechanical elements that amplify small, nucleotide-dependent conformational changes that occur in their similar catalytic cores.
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.