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Phosphorylation of tau by glycogen synthase kinase 3beta affects the ability of tau to promote microtubule self-assembly.
- M. Utton, A. Vandecandelaere, +5 authors B. Anderton
- Chemistry, Medicine
- The Biochemical journal
- 1 May 1997
The regulation of microtubule assembly can be controlled by phosphorylation of tau at sites accessible to GSK-3beta by a mechanism that does not necessarily involve the dissociation of t Tau from the microtubules. Expand
Differences in the regulation of microtubule dynamics by microtubule-associated proteins MAP1B and MAP2.
- A. Vandecandelaere, B. Pedrotti, M. Utton, R. Calvert, P. Bayley
- Biology, Medicine
- Cell motility and the cytoskeleton
Numerical simulations illustrate that microtubule dynamics are strongly influenced by relatively small changes in the strength of a limited subset of subunit interactions in the lattice. Expand
Response of microtubules to the addition of colchicine and tubulin-colchicine: evaluation of models for the interaction of drugs with microtubules.
The work further confirms the existence of colchicine-binding sites with low affinity along the microtubule lattice, which suggests that part of the colcho-binding site on tubulin remains available in the polymer, and indicates drug-induced disassembly can be extremely slow. Expand
Regulation of microtubule dynamic instability by tubulin-GDP.
Tu-GDP appears to exemplify the action of a relatively simple factor with the potential capability for regulation of microtubule dynamics in a cellular environment, as observed experimentally and well reproduced by computer simulation. Expand
Effects of the tubulin-colchicine complex on microtubule dynamic instability.
Computer simulation shows that Monte Carlo simulations show that Tu-Col can cause major suppression of the dynamic transitions of microtubules without inducing bulk microtubule disassembly, which could be important for the regulation of micro Tubulin-colchicine dynamics in vivo. Expand
Phosphate release during microtubule assembly: what stabilizes growing microtubules?
- A. Vandecandelaere, M. Brune, M. Webb, S. Martin, P. Bayley
- Chemistry, Medicine
- 4 June 1999
Nucleotide hydrolysis can keep pace with tubulin-GTP addition rates of 200 molecules per second per microtubule and that extended caps are not generated in normal assembly, nor are they required to stabilize growing micro Tubule or to support the phenomenon of dynamic instability of microtubules at the steady state. Expand
Functional Differences of Tau Isoforms Containing 3 or 4 C-terminal Repeat Regions and the Influence of Oxidative Stress*
- M. Utton, G. Gibb, I. Burdett, B. Anderton, A. Vandecandelaere
- Medicine, Biology
- The Journal of Biological Chemistry
- 7 September 2001
We report functional differences between tau isoforms with 3 or 4 C-terminal repeats and a difference in susceptibility to oxidative conditions, with respect to the regulation of microtubule dynamics… Expand
Evidence for an alternative pathway for colchicine binding to tubulin, based on the binding kinetics of the constituent rings.
- Y. Engelborghs, C. Dumortier, A. D'Hoore, A. Vandecandelaere, T. Fitzgerald
- Medicine, Chemistry
- The Journal of biological chemistry
- 5 January 1993
Stopped-flow kinetic studies reveal that fast TMA binding competes for the initial binding of colchicine, indicating that TMA also binds slowly in a second mode or site and the binding of TMA is practically thermoneutral. Expand
The pathological importance of microtubules and tau