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Hideaki Yoshimura

Publications and source records attributed to Hideaki Yoshimura.

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Optical turbulence retrieval of heterogeneous media

The transport of intensity equation (TIE) has revolutionized phase retrieval in optical microscopy, yet its application to complex media with absorption/scattering remains challenging. Here, we present a coupled TIE-TPE (transport of phase equation) framework derived directly from the paraxial wave equation with complex optical potential. By decomposing the refractive index field into a spatially uniform mean field and local fluctuation field, our approach enables simultaneous reconstruction of refractive-index fluctuations and attenuation coefficients without linearization assumptions. We establish reconstruction validity bounds that define the measurable parameter region where reconstruction remains physically consistent. Experimental demonstration with microlens arrays and HeLa cells shows robust recovery of optical properties even in the transparent-limit regime where attenuation signals approach detection thresholds. Furthermore, we provide the first experimental verification of attenuation symmetry -- a fundamental property of wave propagation that characterizes reciprocity in light-matter interactions.

physics.optics

Signaling activations through G-protein-coupled-receptor aggregations

Eukaryotic cells transmit extracellular signal information to cellular interiors through the formation of a ternary complex made up of a ligand (or agonist), G-protein, and G-protein coupled receptor (GPCR). Previously formalized theories of ternary complex formation have mainly assumed that observable states of receptors can only take the form of monomers. Here, we propose a multiary complex model of GPCR signaling activations via the vector representation of various unobserved aggregated receptor states. Our results from model simulations imply that receptor aggregation processes can govern cooperative effects in a regime inaccessible by previous theories. In particular, we show how the affinity of ligand-receptor binding can be largely varied by various oligomer formations in the low concentration range of G-protein stimulus.

q-bio.MN