What is he best known for?
The fields of study he is best known for:
His primary areas of study are Biochemistry, Escherichia coli, RNase H, Stereochemistry and Enzyme.
His study in Biochemistry is interdisciplinary in nature, drawing from both Strain and Bacillus subtilis.
The various areas that Shigenori Kanaya examines in his Escherichia coli study include Isoelectric point, Mutant, Site-directed mutagenesis, Molecular biology and RNase P.
His RNase H study combines topics in areas such as Crystallography, DNA and Homology.
The concepts of his Stereochemistry study are interwoven with issues in Hydrogen bond, Thermostability, Binding site and Active site.
The Enzyme study combines topics in areas such as Residue and Amino acid.
His most cited work include:
- Three-dimensional structure of ribonuclease H from E. coli (304 citations)
- Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution. (180 citations)
- How does RNase H recognize a DNA.RNA hybrid (163 citations)
What are the main themes of his work throughout his whole career to date?
Shigenori Kanaya mainly investigates Biochemistry, RNase P, Crystallography, Stereochemistry and Escherichia coli.
His Biochemistry study frequently draws connections to other fields, such as Molecular biology.
His is involved in several facets of RNase P study, as is seen by his studies on RNase H and RNase PH.
His research integrates issues of Hydrolase, Crystallization and Protein structure in his study of Crystallography.
His Stereochemistry research includes elements of Mutant, Crystal structure, Active site, Substrate and Binding site.
His Escherichia coli research is multidisciplinary, incorporating perspectives in Molecular cloning, Mutagenesis, Site-directed mutagenesis and Recombinant DNA.
He most often published in these fields:
- Biochemistry (51.54%)
- RNase P (25.00%)
- Crystallography (24.07%)
What were the highlights of his more recent work (between 2011-2021)?
- Biochemistry (51.54%)
- Stereochemistry (24.07%)
- RNase P (25.00%)
In recent papers he was focusing on the following fields of study:
Shigenori Kanaya focuses on Biochemistry, Stereochemistry, RNase P, Subtilisin and Mutant.
Biochemistry is a component of his Thermococcus kodakarensis, Hydrolase, Enzyme, Peptide sequence and Protein structure studies.
His Enzyme study integrates concerns from other disciplines, such as Secretion and Operon, Escherichia coli.
His studies deal with areas such as Biosynthesis, Crystal structure, Active site, Substrate and Bacillus circulans as well as Stereochemistry.
His RNase P research includes themes of DNA and Ribonuclease.
His RNase H study combines topics from a wide range of disciplines, such as Folding, Crystallography, RNase PH and Sulfolobus tokodaii.
Between 2011 and 2021, his most popular works were:
- Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach. (123 citations)
- Crystal Structure and Thermodynamic and Kinetic Stability of Metagenome-Derived LC-Cutinase (53 citations)
- Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii (38 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Biochemistry, Active site, Hydrolase, Enzyme and Peptide sequence.
His work deals with themes such as Molecular biology, Evolvability and Microbiology, which intersect with Biochemistry.
Shigenori Kanaya has included themes like RNase P, RNase H and Stereochemistry in his Active site study.
His work investigates the relationship between Enzyme and topics such as Thermococcus kodakarensis that intersect with problems in Proteases and Protease.
His Peptide sequence research incorporates elements of Clostridium thermocellum, Denaturation, Binding site and Glycoside hydrolase.
Shigenori Kanaya combines subjects such as Cutinase, PelB leader sequence and Escherichia coli with his study of Lipase.
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