What is he best known for?
The fields of study he is best known for:
Wataru Hashimoto focuses on Biochemistry, Enzyme, Lyase, Escherichia coli and Stereochemistry.
Biochemistry is often connected to Bacteria in his work.
Wataru Hashimoto studies Enzyme, namely Glycosidic bond.
Wataru Hashimoto connects Lyase with Depolymerization in his study.
His work is dedicated to discovering how Escherichia coli, Molecular biology are connected with NADH kinase, Kinase and NAD+ kinase and other disciplines.
Wataru Hashimoto interconnects Catalytic triad, Crystal structure, Enzyme Gene, Hydrogen bond and Protein structure in the investigation of issues within Stereochemistry.
His most cited work include:
- Transformation of Saccharomyces cerevisiae and other fungi: methods and possible underlying mechanism. (153 citations)
- Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. (117 citations)
- Bioethanol production from marine biomass alginate by metabolically engineered bacteria (115 citations)
What are the main themes of his work throughout his whole career to date?
His scientific interests lie mostly in Biochemistry, Stereochemistry, Enzyme, Bacteria and Escherichia coli.
He integrates many fields, such as Biochemistry and Depolymerization, in his works.
His work deals with themes such as Hydrolase, Residue, Crystal structure, Substrate and Glycoside hydrolase, which intersect with Stereochemistry.
The Glycosidic bond, Active site and NAD+ kinase research he does as part of his general Enzyme study is frequently linked to other disciplines of science, such as Streptococcus pyogenes, therefore creating a link between diverse domains of science.
His study in the fields of Gene cluster under the domain of Bacteria overlaps with other disciplines such as Strain.
His Escherichia coli study also includes
- Molecular biology together with Nucleic acid sequence, Open reading frame and Gene,
- Peptide sequence which connect with Protein structure.
He most often published in these fields:
- Biochemistry (65.29%)
- Stereochemistry (25.29%)
- Enzyme (24.71%)
What were the highlights of his more recent work (between 2013-2020)?
- Biochemistry (65.29%)
- ATP-binding cassette transporter (15.88%)
- Stereochemistry (25.29%)
In recent papers he was focusing on the following fields of study:
Wataru Hashimoto mostly deals with Biochemistry, ATP-binding cassette transporter, Stereochemistry, Mutant and Bacteria.
Glycosaminoglycan, Binding protein, Enzyme, Periplasmic space and Polysaccharide are the core of his Biochemistry study.
His ATP-binding cassette transporter study integrates concerns from other disciplines, such as Protein structure, Cytoplasm and Docking.
His studies deal with areas such as Heparan sulfate, Heparin and Yeast extract, Tryptone as well as Stereochemistry.
His Mutant research integrates issues from Enzyme assay, Crystal structure and Hydrogen bond.
The various areas that Wataru Hashimoto examines in his Bacteria study include Pectin and Microbiology.
Between 2013 and 2020, his most popular works were:
- Structure-based conversion of the coenzyme requirement of a short-chain dehydrogenase/reductase involved in bacterial alginate metabolism (29 citations)
- Structure of a Bacterial ABC Transporter Involved in the Import of an Acidic Polysaccharide Alginate (21 citations)
- Probiotics in human gut microbiota can degrade host glycosaminoglycans. (16 citations)
In his most recent research, the most cited papers focused on:
Wataru Hashimoto spends much of his time researching Biochemistry, ATP-binding cassette transporter, Protein structure, Stereochemistry and Transport protein.
Glycosaminoglycan, Dehydrogenase, Lyase, Cofactor and Heparin are the primary areas of interest in his Biochemistry study.
He has included themes like Antiparallel and Active site in his Lyase study.
Wataru Hashimoto interconnects Peptide sequence, Neisseria and Moiety in the investigation of issues within Protein structure.
The Stereochemistry study combines topics in areas such as Heparan sulfate and Enzyme.
His Transport protein study combines topics from a wide range of disciplines, such as Periplasmic space, Binding protein, Membrane, Protein quaternary structure and Oligosaccharide.
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