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The dynamic instability of microtubules is not modulated by alpha-tubulin tyrosinylation.

Abstract:

The tyrosinylation of chick brain alpha-tubulin and the effects of the tyrosinylation status on the assembly and dynamic instability of chick brain MAP2:tubulin microtubule protein have been examined. Each of the eight major alpha-isotypes can be tyrosinylated in vitro, irrespective of whether a C-terminal tyrosine is genetically encoded. The extent of tyrosinylation is however limited to congruent to 0.3 mol.mol-1. The tyrosinylation status (0 vs. 0.3 mol.mol-1) has no effect on either the a...

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Publication status:
Published

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Publisher copy:
10.1002/cm.970200104

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
Cell motility and the cytoskeleton
Volume:
20
Issue:
1
Pages:
30-37
Publication date:
1991-01-05
DOI:
EISSN:
1097-0169
ISSN:
0886-1544
URN:
uuid:07d6a7f0-7c8f-40be-8b6b-322821bb22dc
Source identifiers:
72647
Local pid:
pubs:72647

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