What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Biochemistry, Protease, Molecular biology, Complementary DNA and Peptide sequence.
His study in Calpain, Ubiquitin ligase, Ubiquitin, DNA ligase and Cullin is done as part of Biochemistry.
His research in Protease intersects with topics in Plasmid, Protein subunit and Saccharomyces cerevisiae.
His studies deal with areas such as Amino acid, Protein kinase C, Expression vector and Northern blot as well as Molecular biology.
His Northern blot research is multidisciplinary, incorporating perspectives in cDNA library, Molecular cloning and Nucleic acid sequence.
Hiroshi Kawasaki interconnects Protein structure, Phylogenetics and Gene duplication in the investigation of issues within Peptide sequence.
His most cited work include:
- Tissue-specific expression of three distinct types of rabbit protein kinase C (418 citations)
- Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. (326 citations)
- Classification and evolution of EF-hand proteins (306 citations)
What are the main themes of his work throughout his whole career to date?
Biochemistry, Molecular biology, Peptide sequence, Complementary DNA and Chromatography are his primary areas of study.
His study in Protein subunit, Enzyme, Protease, Calpain and Amino acid falls within the category of Biochemistry.
His work in Molecular biology addresses issues such as Molecular cloning, which are connected to fields such as Sequence analysis.
The Peptide sequence study combines topics in areas such as Protein structure, Lectin, Saccharomyces cerevisiae and Escherichia coli.
The concepts of his Complementary DNA study are interwoven with issues in Nucleic acid sequence, Restriction map and Protein primary structure.
In his research on the topic of Chromatography, Two-dimensional gel electrophoresis and Isoelectric focusing is strongly related with Gel electrophoresis.
He most often published in these fields:
- Biochemistry (65.38%)
- Molecular biology (32.05%)
- Peptide sequence (29.49%)
What were the highlights of his more recent work (between 1999-2015)?
- Biochemistry (65.38%)
- Proteasome (7.69%)
- Phosphorylation (6.41%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Biochemistry, Proteasome, Phosphorylation, Chromatography and Gel electrophoresis.
Biochemistry connects with themes related to Electrospray ionization in his study.
His Proteasome research incorporates themes from Ubiquitin, F-box protein, Cell division control protein 4, Ubiquitin ligase complex and Endoplasmic reticulum.
As part of the same scientific family, Hiroshi Kawasaki usually focuses on Phosphorylation, concentrating on Protein subunit and intersecting with Phosphatase, Peptide mass fingerprinting, Protease, Mass spectrometry and Molecular biology.
He has included themes like A protein and Polyacrylamide in his Chromatography study.
His Gel electrophoresis research is multidisciplinary, incorporating elements of Two-dimensional gel electrophoresis and Sodium dodecyl sulfate.
Between 1999 and 2015, his most popular works were:
- E3 ubiquitin ligase that recognizes sugar chains (294 citations)
- A Critical Role for the Proteasome Activator PA28 in the Hsp90-dependent Protein Refolding (70 citations)
- Electrophoretic analysis of phosphorylation of the yeast 20S proteasome. (67 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Biochemistry, Proteasome, Ubiquitin, Cell division control protein 4 and F-box protein.
His research integrates issues of Gel electrophoresis and Activator in his study of Proteasome.
Molecular biology covers Hiroshi Kawasaki research in Gel electrophoresis.
His Activator research incorporates elements of Enzyme activator, Biophysics, Protein folding, Luciferase and Hsp90.
His Ubiquitin study frequently draws parallels with other fields, such as Endoplasmic reticulum.
His Two-dimensional gel electrophoresis research includes themes of Phosphatase and Peptide mass fingerprinting.
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