Mechanism of the microtubule GTPase reaction.
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Summary
It was found that GDP inhibition of the microtubule GTPase rate results from GDP competition for GTP at the tubulin subunit E-site, and there is no additional effect of GDP on the GTP enzyme rate resulting from exchange into Tubulin subunits at microtubules ends.
- Type
- article
- Published
- 1990-05-25
- Cited by
- 31
- References
- 2
- Access
- Open access
- OpenAlex
- https://openalex.org/W1580916182
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:11891915
Keywords
GTPase, Mechanism (biology), Cell biology, Microtubule, Chemistry
References
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- Nucleotide hydrolysis in cytoskeletal assembly.
- Quantitative evaluation of the lengths of homobifunctional protein cross‐linking reagents used as molecular rulers
- Microtubule dynamics and microtubule caps: a time-resolved cryo- electron microscopy study
- Localization of an exchangeable GTP binding site at the plus end of microtubules.
- Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules.
- Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice.
- Dynamic properties of nucleated microtubules: GTP utilisation in the subcritical concentration regime.
- Kidney ischemia-reperfusion regulates expression and distribution of tubulin subunits, beta-actin and rho GTPases in proximal tubules.
- Microtubule polymerization dynamics.
- Dominant-Lethal α-Tubulin Mutants Defective in Microtubule Depolymerization in Yeast
- Identification of microtubule growth deceleration and its regulation by conserved and novel proteins
- Dynamics of microtubules: highlights of recent computational and experimental investigations
- Microtubules grow by the addition of bent guanosine triphosphate tubulin to the tips of curved protofilaments
- Energy consumption in chemical fuel-driven self-assembly
- Chemically Fueled Dissipative Self-Assembly that Exploits Cooperative Catalysis.
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