M
Masaharu Ueno
Researcher at University of Toyama
Publications - 19
Citations - 366
Masaharu Ueno is an academic researcher from University of Toyama. The author has contributed to research in topics: Catalysis & Liposome. The author has an hindex of 5, co-authored 19 publications receiving 352 citations.
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Journal ArticleDOI
Development of a non-viral multifunctional envelope-type nano device by a novel lipid film hydration method.
Kentaro Kogure,Rumiko Moriguchi,Kentaro Sasaki,Masaharu Ueno,Shiroh Futaki,Hideyoshi Harashima +5 more
TL;DR: MEND, having octaarginine on the envelope as a device for membrane penetration to enhance cellular uptake, showed a 1000-fold higher transfection activity than DPC and represents a promising non-viral gene delivery system.
Journal ArticleDOI
Delivery of Condensed DNA by Liposomal Non-viral Gene Delivery System into Nucleus of Dendritic Cells
Takashi Nakamura,Rumiko Moriguchi,Kentaro Kogure,Arisa Minoura,Tomoya Masuda,Hidetaka Akita,Kazunori Kato,Hirofumi Hamada,Masaharu Ueno,Shiroh Futaki,Shiroh Futaki,Hideyoshi Harashima +11 more
TL;DR: Novel double-membranous non-viral gene delivery system modified with SV-40 T antigen-derived nuclear localization signal (NLS-DMEND) for delivery of luciferase plasmid DNA to nucleus of non-dividing mouse bone marrow-derived dendritic cells (BMDC).
Journal ArticleDOI
Construction of a multifunctional envelope-type nano device by a SUV*-fusion method.
Kentaro Sasaki,Kentaro Kogure,Sinji Chaki,Yoshitaka Kihira,Masaharu Ueno,Hideyoshi Harashima +5 more
TL;DR: It is confirmed that a transferrin-modified MEND could deliver a gene into a cell through receptor-mediated endocytosis and the successful construction of a small and homogenous MEND by a novel SUV*-fusion method.
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Effect of dicetylphosphate or stearic acid on spontaneous transfer of protein from influenza virus-infected cells to dimyristoylphosphatidylcholine liposomes.
TL;DR: The alteration of membrane properties, such as construction of the surface or stability of transferred protein in liposomes, due to the specific structure of DCP or SA is responsible for the enhancement of spontaneous protein transfer by the presence of the amphiphilic components.
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Development of a membrane fusible drug carrier from erythrocytes by the spontaneous transfer of viral fusion protein from influenza virus-infected cells
TL;DR: By using an HA-reconstituted ghost (HA-ghost), which entrapped fluorescent-labeled ovalbumin, 25% of the protein was incorporated into cells through the fusion of the HA-ghost with the cell membrane.