ArticleBiochemistry2006
Pathway of ATP hydrolysis by monomeric kinesin Eg5.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- Nonequilibrium Self-Assembly of Microtubules Through Stepwise Sequential Interactions of DNA.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- LncRNA NEAT1 suppresses cellular senescence in hepatocellular carcinoma via KIF11-dependent repression of CDKN2A.Clinical and translational medicine · 2023Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- These motors were made for walking.Protein science : a publication of the Protein Society · 2020Review
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Article
- The Kinesin-5 Chemomechanical Cycle Is Dominated by a Two-heads-bound State.The Journal of biological chemistry · 2016Article
- Effects of protonation on the hydrolysis of triphosphate in vacuum and the implications for catalysis by nucleotide hydrolyzing enzymes.BMC biochemistry · 2016Article
- Motile properties of the bi-directional kinesin-5 Cin8 are affected by phosphorylation in its motor domain.Scientific reports · 2016Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Kinesin-2 KIF3AB exhibits novel ATPase characteristics.The Journal of biological chemistry · 2014Article
- Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Review
- A metal switch for controlling the activity of molecular motor proteins.Nature structural & molecular biology · 2011Article
- The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Biophysical journal · 2011Article
- Loop 5-directed compounds inhibit chimeric kinesin-5 motors: implications for conserved allosteric mechanisms.The Journal of biological chemistry · 2011Article
- Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding.The Journal of biological chemistry · 2010Article
- The conserved L5 loop establishes the pre-powerstroke conformation of the Kinesin-5 motor, eg5.Biophysical journal · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Kinesin-5 family members including human Eg5/KSP contribute to the plus-end-directed force necessary for the assembly and maintenance of the bipolar mitotic spindle. We have used monomeric Eg5-367 in the nucleotide-free state to evaluate the role of microtubules at each step in the ATPase cycle. The pre-steady-state kinetic results show that the microtubule-Eg5 complex binds MgATP tightly, followed by rapid ATP hydrolysis with a subsequent slow step that limits steady-state turnover. We show that microtubules accelerate the kinetics of each step in the ATPase pathway, suggesting that microtubules amplify the nucleotide-dependent structural transitions required for force generation. The experimentally determined rate constants for phosphate product release and Eg5 detachment from the microtubule were similar, suggesting that these two steps are coupled with one occurring at the slow rate after ATP hydrolysis followed by the second step occurring more rapidly. The rate of this slow step correlates well with the steady-state k(cat), indicative that it is the rate-limiting step of the mechanism.
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.