Publications by authors named "T Iyanagi"

Objectives: To quantitatively analyse by artificial intelligence (AI) the communication skills of physicians in an acute care hospital for geriatric care following a multimodal comprehensive care communication skills training programme and to qualitatively explore the educational benefits of this training programme.

Design: A convergent mixed-methods study, including an intervention trial with a quasi-experimental design, was conducted to quantitatively analyse the communication skills of physicians. Qualitative data were collected via physicians' responses to an open-ended questionnaire administered after the training.

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Distinct isoforms of FAD-containing ferredoxin-NADP oxidoreductase (FNR) and ferredoxin (Fd) are involved in photosynthetic and non-photosynthetic electron transfer systems. The FNR (FAD)-Fd [2Fe-2S] redox pair complex switches between one- and two-electron transfer reactions in steps involving FAD semiquinone intermediates. In cyanobacteria and some algae, one-electron carrier Fd serves as a substitute for low-potential FMN-containing flavodoxin (Fld) during growth under low-iron conditions.

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In inferior shoulder dislocation (ISD) cases, closed reduction usually achieves reduction and irreducible ISD is extremely rare. To date, only two cases requiring open reduction have been reported. Herein, we describe a case of an irreducible ISD that required open reduction.

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NAD(P)H-dependent electron-transfer (ET) systems require three functional components: a flavin-containing NAD(P)H-dehydrogenase, one-electron carrier and metal-containing redox center. In principle, these ET systems consist of one-, two- and three-components, and the electron flux from pyridine nucleotide cofactors, NADPH or NADH to final electron acceptor follows a linear pathway: NAD(P)H → flavin → one-electron carrier → metal containing redox center. In each step ET is primarily controlled by one- and two-electron midpoint reduction potentials of protein-bound redox cofactors in which the redox-linked conformational changes during the catalytic cycle are required for the domain-domain interactions.

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