S
Shigeaki Harayama
Researcher at Chuo University
Publications - 292
Citations - 20554
Shigeaki Harayama is an academic researcher from Chuo University. The author has contributed to research in topics: Gene & Peptide sequence. The author has an hindex of 78, co-authored 291 publications receiving 19389 citations. Previous affiliations of Shigeaki Harayama include National Institute of Technology and Evaluation & Japan Women's University.
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Journal ArticleDOI
Biodegradation of high-molecular-weight polycyclic aromatic hydrocarbons by bacteria.
TL;DR: Interest in the biodegradation mechanisms and environmental fate of polycyclic aromatic hydrocarbons is prompted by their ubiquitous distribution and their potentially deleterious effects on human health.
Journal ArticleDOI
PCR amplification and direct sequencing of gyrB genes with universal primers and their application to the detection and taxonomic analysis of Pseudomonas putida strains.
S Yamamoto,Shigeaki Harayama +1 more
TL;DR: The article corrects the article on p. 1104, column 2, 5 lines from the bottom: " each of the primers at a concentration of 1 mM" should read "each of thePrimers atA concentration of1 (mu)M."
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Molecular mechanisms of genetic adaptation to xenobiotic compounds.
TL;DR: In this article, a range of genetic mechanisms, such as gene transfer, mutational drift, and genetic recombination and transposition, can accelerate the evolution of catabolic pathways in bacteria.
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Phylogeny of the genus Pseudomonas: intrageneric structure reconstructed from the nucleotide sequences of gyrB and rpoD genes.
Satoshi Yamamoto,Hiroaki Kasai,Dawn L. Arnold,Robert W. Jackson,Alan Vivian,Shigeaki Harayama +5 more
TL;DR: Phylogenetic analysis of the genus Pseudomonas: was conducted by using the combined gyrB and rpoD nucleotide sequences of 31 validly described species of Pseudomanas: (a total of 125 strains).
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Functional and Evolutionary Relationships Among Diverse Oxygenases
TL;DR: Oxygenases that incorporate one or two atoms of dioxygen into substrates are found in many metabolic pathways and according to their sequence similarities, the oxygenases can be grouped into several protein families.