Publications by authors named "Y Nakasone"

Context: Chronic kidney disease (CKD) is a worldwide health problem. Recent literature has shown an association of hemoglobin glycation index (HGI) and CKD in patients with dysglycemia.

Objective: The aim of this study was to reveal the impact of HGI as a predictor for incident CKD in the general population.

View Article and Find Full Text PDF
Article Synopsis
  • Photoactivated adenylate cyclases (PACs), like OaPAC from Oscillatoria acuminata, are proteins that change their cAMP levels based on light and have a unique structure with a BLUF domain and an adenylate cyclase domain.* -
  • When researchers used the transient grating method, they found that light causes specific changes in the protein's structure and its ability to function, particularly when both parts of the dimer (the protein's two units) are activated by light.* -
  • The study highlighted the significance of the W90 residue for OaPAC's activity and proposed a reaction scheme to explain how light influences the protein's signaling dynamics.*
View Article and Find Full Text PDF

Cyanobacteriochromes (CBCRs) derived from cyanobacteria are linear-tetrapyrrole-binding photoreceptors related to the canonical red/far-red reversible phytochrome photoreceptors. CBCRs contain chromophore-binding cGMP-specific phosphodiesterase/adenylate cyclase/FhlA (GAF) domains that are highly diverse in their primary sequences and are categorized into many subfamilies. Among this repertoire, the biliverdin (BV)-binding CBCR GAF domains receive considerable attention for their in vivo optogenetic and bioimaging applications because BV is a mammalian intrinsic chromophore and can absorb far-red light that penetrates deep into the mammalian body.

View Article and Find Full Text PDF

A sensor of blue-light using flavin adenine dinucleotide (BLUF) is a typical blue light photoreceptor domain that is found in many photosensor proteins in bacteria and some eukaryotic algae. SyPixD in Synechocystis is one of the well-studied BLUF proteins. In the dark state, it forms a decamer and, upon photoexcitation, a dissociation reaction takes place to yield dimers.

View Article and Find Full Text PDF