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Yoshihiko Ikeguchi

Researcher at Penn State Milton S. Hershey Medical Center

Publications -  10
Citations -  635

Yoshihiko Ikeguchi is an academic researcher from Penn State Milton S. Hershey Medical Center. The author has contributed to research in topics: Spermidine & Spermine. The author has an hindex of 9, co-authored 10 publications receiving 591 citations. Previous affiliations of Yoshihiko Ikeguchi include Pennsylvania State University & Josai University.

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X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome.

TL;DR: The clinical features observed in SRS are consistent with cerebellar dysfunction and a defective functioning of red nucleus neurons, which, at least in rats, contain high levels of spermine, and the presence of MR reflects a role for s permine in cognitive function, possibly by sper mine's ability to function as an ‘intrinsic gateway’ molecule for inward rectifier K+ channels.
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The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor

TL;DR: The crystal structure of the PAPT from Thermotoga maritima has been solved to 1.5 Å resolution and reveals deep cavities for binding substrate and cofactor, and a loop that envelops the active site, suggesting a universal catalytic mechanism.
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Crystal Structure of Human Spermine Synthase IMPLICATIONS OF SUBSTRATE BINDING AND CATALYTIC MECHANISM

TL;DR: The spermine synthase·5′-methylthioadenosine structure provides a plausible explanation for the potent inhibition of the reaction by this product and the stronger inhibition of spermining synthase compared with spermidine synthase.
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Structure and mechanism of spermidine synthases.

TL;DR: Comparison of the structures of the human spermidine synthase with both substrates and products and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction.
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Spermine Synthesis Is Required for Normal Viability, Growth, and Fertility in the Mouse

TL;DR: It is shown that spermine synthesis is needed for normal growth, viability, and fertility in male mice and that regulation of sPermine synthase content is not required.