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Shigenori Kanaya

Researcher at Osaka University

Publications -  246
Citations -  8197

Shigenori Kanaya is an academic researcher from Osaka University. The author has contributed to research in topics: RNase P & RNase H. The author has an hindex of 46, co-authored 246 publications receiving 7597 citations. Previous affiliations of Shigenori Kanaya include National Institutes of Health & Tokyo Institute of Technology.

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Three-dimensional structure of ribonuclease H from E. coli

TL;DR: The three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 Å resolution by X-ray crystallography and it was found to belong to the α + β class of structures, consisting of two distinct domains.
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Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach.

TL;DR: LC-cutinase* not only serves as a good model for understanding the molecular mechanism of PET-degrading enzyme but also is potentially applicable for surface modification and degradation of PET.
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Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution.

TL;DR: The crystal structure of RNase H from Escherichia coli has been determined by the multiple isomorphous replacement method, and refined by the stereochemically restrained least-squares procedure to a crystallographic R-factor of 0.196 at 1.48 A resolution, and reveals the details of hydrogen bonding, electrostatic and hydrophobic interactions between intra- and intermolecular residues.
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How does RNase H recognize a DNA.RNA hybrid

TL;DR: The mechanism of RNase H substrate recognition is proposed from a model of a chemically modified DNA, andRNA hybrids can be explained as well as cleavage modes in modified heteroduplexes.
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Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes

TL;DR: Significant progress has been made in this decade in identifying novel RNases’H with respect to their biochemical properties and structures, and elucidating catalytic mechanism and substrate recognition mechanism of RNase H.