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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Myosin from Physarum polycephalum, a lower eukaryote, interacts in an ATPdependent manner with actin without any requirment for Ca 2+ , namely, in the absence of Ca 2+ . When Ca 2+ is present at μM levels, the interaction is inhibited. This «calcium inhibition» is attributable to Ca 2+ that is bound to a calcium-binding myosin light chain of 16,084 daltons. Phosphorylation of myosin on the heavy chain and/or the 18-kDa light chain is required for the actin-myosin interaction. The kinases for the heavy and light chains are also subject to calcium inhibition, which is mediated by a calcium-dependent inhibitory factor of 40,508 daltons

biomedical research

&lt;b&gt;COPPER METABOLISM IN THE MACULAR MOUSE, AN ANIMAL MODEL FOR MENKES’KINKY HAIR DISEASE: CHANGES IN THE CYTOCHROME&lt;i&gt; C&lt;/i&gt; OXIDASE ACTIVITY AND COPPER CONTENT IN VARIOUS ORGANS AFTER COPPER &lt;/b&gt;&lt;b&gt;ADMINISTRATION &lt;/b&gt;