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

Protein kinase C (PKC) isozymes play a critical role in many signal transduction pathways and are also main targets of tumor-promoting phorbol esters. Conventional and novel PKC isozymes contain two cysteine-rich C 1 domains (C 1 A and C 1 B), both of which are candidates for phorbol ester binding sites. These C 1 domains of about 50-70 amino acids were synthesized by an Fmocsolid phase strategy, and were successfully folded by zinc treatment. We measured the dissociation constants (Kd's) of [3H] phorbol-12, 13-dibutyrate for all PKC C 1 peptides. Most of the C 1 peptides showed strong PDBu binding affinities with Kd's in the nanomolar range (0.45-7.4 nM) comparable to the respective whole PKC isozymes. The resultant C 1 peptide library can be used to screen for new ligands with PKC isozyme and importantly C 1 domain selectivity. We have recently developed a new lactone analogue of benzolactams (6) which shows significant selectivity in the PKCη-C 1 B binding on the basis of the structure-activity relationship of teleocidin-type tumor promoters.

yūki gōsei kagaku kyōkaishi/yuuki gousei kagaku kyoukaishi

Synthesis and Functional Analysis of the Cysteine-rich Domains of Protein Kinase C (PKC) for Development of New Medicinal Leads with PKC Isozyme and C1 Domain Selectivity.