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Biology subjects

Morioka, M. S.

Publications and source records attributed to Morioka, M. S..

2 recordsLinked to original sources

Kawasemi-Colours: an open end-to-end platform for structure-colour design based on avian structural colour

Structural colour provides durable, pigment-free colouration by controlling the interaction of light with nanostructured materials rather than by using wavelength-selective pigments. In birds, non-iridescent blue and green plumage arises from coherent scattering by quasi-ordered keratin-air nanostructures, making these natural systems attractive models for sustainable colour engineering. Despite decades of research on their optical mechanisms, open end-to-end implementations that connect biological nanostructures with colour prediction, inverse design and physics-based evaluation remain limited. Here I present Kawasemi Colours, an open end-to-end platform for structure-colour design based on avian structural colour. From published electron micrographs, I assembled a provenance-tracked dataset of spongy, channel and quasi-ordered sphere nanostructures with associated colour metadata. I extracted interpretable structural descriptors, developed compact forward models that predict colour from nanostructure images, and implemented an analytic inverse design tool that generates candidate structures for a target colour. Both directions are provided through self-contained interactive web applications. Kawasemi Colours provides an open framework for studying and designing structural colour from biological nanostructures. By integrating curated data, interpretable machine learning, wave optics, and interactive design tools, the platform lowers the barrier to comparative structural-colour research and provides a cumulative foundation for testing and refining structure-colour relationships as new biological data become available.

bioinformatics↗

CDK1 dependent phosphorylation of hTERT contributes to cancer progression

The telomerase reverse transcriptase is upregulated in the majority of human cancers and contributes directly to cell transformation. Here we report that hTERT is phosphorylated at threonine 249 during mitosis by the serine/threonine kinase CDK1. Clinicopathological analyses revealed that phosphorylation of hTERT at threonine 249 occurs more frequently in advanced cancers. Using CRISPR/Cas9 genome editing, we introduced substitution mutations at threonine 249 in the endogenous hTERT locus and found that phosphorylation of threonine 249 is necessary for hTERT-mediated RNA dependent RNA polymerase (RdRP) activity but dispensable for reverse transcriptase activity. Cap Analysis of Gene Expression (CAGE) demonstrated that hTERT phosphorylation at 249 regulates the expression of specific genes that are necessary for cancer cell proliferation and tumor formation. These observations indicate that phosphorylation at threonine 249 regulates hTERT RdRP and contributes to cancer progression in a telomerase independent manner.

cancer biology↗