Warning: The NCBI web site requires JavaScript to function. more...
Generate a file for use with external citation management software.
Department of Biochemistry, University of North Carolina, Chapel Hill 27599-7260.
Although compelling evidence has been obtained for heterogeneity in the structure of subunits in microtubules, it has not been possible to prove that this results from the presence of tubulin-GDP and tubulin-GTP in polymers. There are reasons to exclude the existence of even a monolayer of tubulin-GTP subunits at microtubule ends. Dynamic behavior appears to be best accounted for by a mechanism in which tubulin-GDP in microtubules exists in two conformations. The mechanism of microtubule-associated protein binding to microtubules and the role of phosphorylation on this reaction are discussed.
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on