English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

2',3'-Cyclic nucleotide-3'-phosphodiesterase (CNP) is firmly associated with tubulin from brain tissue and FRTL-5 thyroid cells as demonstrated by copolymerization with microtubules through several warm/cold cycles, the presence of CNP activity in purified tubulin preparations, and identical behavior during various extraction procedures. CNP acts as a microtubule-associated protein in promoting microtubule assembly at low mole ratios. This activity resides in the C terminus of the enzyme, which, by itself, promotes microtubule assembly at higher mole ratios. Phosphorylation of CNP interferes with its assembly-promoting activity, as does deletion of the C terminus, which leads to abnormal microtubule distribution in the cell. Submembranous colocalization of the proteins and CNP-dependent microtubule organization suggest that CNP is a membrane-bound microtubule-associated protein that can link tubulin to membranes and may regulate cytoplasmic microtubule distribution.

2′,3′-Cyclic nucleotide 3′-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin