J
Jamie L. Gilmore
Researcher at Kyoto University
Publications - 19
Citations - 515
Jamie L. Gilmore is an academic researcher from Kyoto University. The author has contributed to research in topics: DNA binding site & RNA. The author has an hindex of 8, co-authored 17 publications receiving 452 citations. Previous affiliations of Jamie L. Gilmore include University of Nebraska Medical Center.
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Journal ArticleDOI
Novel nanomaterials for clinical neuroscience.
TL;DR: An overview of novel nanomaterials that have potential to improve diagnosis and therapy of neurodegenerative disorders and how to enable these materials to cross the blood brain barrier will allow efficient systemic delivery of therapeutic and diagnostic agents to the brain.
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Single-Molecule Dynamics of the DNA−EcoRII Protein Complexes Revealed with High-Speed Atomic Force Microscopy
Jamie L. Gilmore,Yuki Suzuki,Gintautas Tamulaitis,Virginijus Siksnys,Kunio Takeyasu,Yuri L. Lyubchenko +5 more
TL;DR: A model in which the EcoRII restriction enzyme employs a three-site binding mechanism to catalyze cleavage of a single recognition site is proposed, which is involved in the formation and dynamics of a catalytically active three- site complex.
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Visual Analysis of Concerted Cleavage by Type IIF Restriction Enzyme SfiI in Subsecond Time Region
Yuki Suzuki,Jamie L. Gilmore,Shige H. Yoshimura,Robert M. Henderson,Yuri L. Lyubchenko,Kunio Takeyasu +5 more
TL;DR: It is proposed that the SfiI tetramer can remain bound to one of the sites even after cleavage, allowing the other site on the DNA molecule to fill the empty DNA-binding cleft by combining a one-dimensional diffusion-mediated sliding and a segment transfer mechanism.
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Direct visualization of the EcoRII-DNA triple synaptic complex by atomic force microscopy.
Luda S. Shlyakhtenko,Jamie L. Gilmore,Alex Portillo,Gintautas Tamulaitis,Virginijus Siksnys,Yuri L. Lyubchenko +5 more
TL;DR: Atomic force microscopy was used to test this model for the EcoRII restriction enzyme and provide direct visualization and characterization of synaptic protein-DNA complexes involving three DNA binding sites, and showed that the dimeric form of the protein is responsible for the formation of other types of synaptic complexes.
Journal ArticleDOI
Probing in vivo dynamics of mitochondria and cortical actin networks using high-speed atomic force/fluorescence microscopy.
Aiko Yoshida,Nobuaki Sakai,Yoshitsugu Uekusa,Katashi Deguchi,Jamie L. Gilmore,Masahiro Kumeta,Shuichi Ito,Kunio Takeyasu +7 more
TL;DR: A combined atomic force/optical microscope system is used to analyze membrane‐based cellular events at nanometer‐scale resolution in live cells to provide novel insights into the structural aspects of the entire cell membrane machinery which can be visualized with high temporal and spatial resolution.