H
Hisakazu Mihara
Researcher at Tokyo Institute of Technology
Publications - 274
Citations - 4978
Hisakazu Mihara is an academic researcher from Tokyo Institute of Technology. The author has contributed to research in topics: Peptide & Peptide sequence. The author has an hindex of 36, co-authored 272 publications receiving 4695 citations. Previous affiliations of Hisakazu Mihara include Rockefeller University & Nagasaki University.
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Peptide and Protein Mimetics Inhibiting Amyloid β-Peptide Aggregation
TL;DR: Various peptides and peptide derivatives have been constructed using the "Abeta binding element" based on the structural models of Abeta amyloid fibrils and the mechanisms of self-assembly to further understanding of the mechanism(s) behind fibril formation and enable targeted drug discovery against AD.
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Protein-detecting microarrays: Current accomplishments and requirements
TL;DR: The sequencing of the human genome has been successfully completed and offers the chance of obtaining a large amount of valuable information for understanding complex cellular events simply and rapidly in a single experiment.
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Binding of cationic α-helical peptides to plasmid DNA and their gene transfer abilities into cells
Takuro Niidome,Naoya Ohmori,Akitoyo Ichinose,Akihiro Wada,Hisakazu Mihara,Toshiya Hirayama,Haruhiko Aoyagi +6 more
TL;DR: A novel transfection method using cationic amphiphilic α-helical oligopeptides with repeated sequences is developed, which indicates that the internalization of the peptide-DNA aggregates would be mediated by the endocytosis pathway.
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Label and Label-Free Detection Techniques for Protein Microarrays
TL;DR: A brief overview of this remarkable innovation from the perspectives of label and label-free techniques in transducing nano-biological events is presented.
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Peptide and protein synthesis by segment synthesis-condensation
Emil Thomas Kaiser,Hisakazu Mihara,Genevieve A. Laforet,Jeffery W. Kelly,Lee Walters,Mark A. Findeis,Tomikazu Sasaki +6 more
TL;DR: In this article, an oxime support increases the ease with which intermediate protected peptides can be synthesized and makes this approach useful for the synthesis of peptides in which secondary structural elements have been redesigned.