Y
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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Journal ArticleDOI
X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome.
A. Lauren Cason,Yoshihiko Ikeguchi,Cindy Skinner,Tim Wood,Kenton R. Holden,Herbert A. Lubs,Francisco Martínez,Richard J. Simensen,Roger E. Stevenson,Anthony E. Pegg,Charles E. Schwartz +10 more
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.
Journal ArticleDOI
The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor
Sergey Korolev,Yoshihiko Ikeguchi,Tatiana Skarina,S. Beasley,Cheryl H. Arrowsmith,Aled M. Edwards,Aled M. Edwards,Andrzej Joachimiak,Anthony E. Pegg,Alexei Savchenko +9 more
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
Hong Wu,Jinrong Min,Hong Zeng,Diane E. McCloskey,Yoshihiko Ikeguchi,Peter Loppnau,Anthony J. Michael,Anthony E. Pegg,Alexander N. Plotnikov,Alexander N. Plotnikov +9 more
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.
Journal ArticleDOI
Structure and mechanism of spermidine synthases.
Hong Wu,Jinrong Min,Yoshihiko Ikeguchi,Hong Zeng,Aiping Dong,Peter Loppnau,Anthony E. Pegg,Alexander N. Plotnikov +7 more
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.