What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Cell biology, Biochemistry, Transport protein, Protein structure and Endosome.
His Cell biology study combines topics from a wide range of disciplines, such as Protein kinase domain and Binding site.
Biochemistry is a component of his Ubiquitin, Tyrosine, Amino acid, Enzyme and Thermus thermophilus studies.
The concepts of his Protein structure study are interwoven with issues in Biophysics, Endoplasmic reticulum, Stereochemistry and Glycoside hydrolase.
His Endosome study integrates concerns from other disciplines, such as Golgi apparatus and Endocytosis.
His Ubiquitin ligase research integrates issues from Protein targeting, Mediator, Transcription and Moiety.
His most cited work include:
- Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation (557 citations)
- Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation (557 citations)
- An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae. (193 citations)
What are the main themes of his work throughout his whole career to date?
Biochemistry, Cell biology, Stereochemistry, Crystallography and Thermus thermophilus are his primary areas of study.
Binding site, Protein structure, Ubiquitin, Peptide sequence and Enzyme are among the areas of Biochemistry where the researcher is concentrating his efforts.
His Binding site research includes elements of Biophysics and Moiety.
Many of his studies on Cell biology involve topics that are commonly interrelated, such as Receptor.
The study incorporates disciplines such as NEU2, Sialidase, Mutant and Substrate in addition to Stereochemistry.
He works mostly in the field of Thermus thermophilus, limiting it down to concerns involving DNA and, occasionally, Circular dichroism and ATP hydrolysis.
He most often published in these fields:
- Biochemistry (46.89%)
- Cell biology (25.99%)
- Stereochemistry (18.64%)
What were the highlights of his more recent work (between 2012-2021)?
- Biochemistry (46.89%)
- Cell biology (25.99%)
- Glycan (6.21%)
In recent papers he was focusing on the following fields of study:
His main research concerns Biochemistry, Cell biology, Glycan, Crystallization and Crystallography.
Ryuichi Kato performs integrative study on Biochemistry and α dystroglycan.
His Cell biology research incorporates themes from HEK 293 cells and Ubiquitin.
His study in the field of Ubiquitin binding also crosses realms of Zinc finger.
Ryuichi Kato interconnects Mannose, Transferase, Fukutin, Stereochemistry and Ribitol in the investigation of issues within Glycan.
As a part of the same scientific study, Ryuichi Kato usually deals with the Binding site, concentrating on Molecular model and frequently concerns with Biophysics.
Between 2012 and 2021, his most popular works were:
- Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins. (88 citations)
- Mechanism Underlying IκB Kinase Activation Mediated by the Linear Ubiquitin Chain Assembly Complex (72 citations)
- Structural basis of the autophagy-related LC3/Atg13 LIR complex: recognition and interaction mechanism. (69 citations)
In his most recent research, the most cited papers focused on:
His primary scientific interests are in Cell biology, Biochemistry, Ubiquitin, Plasma protein binding and Phosphorylation.
His work on Enzyme activator as part of general Cell biology study is frequently linked to Nuclear protein, bridging the gap between disciplines.
His study of Ubiquitin binding is a part of Ubiquitin.
The Serine research Ryuichi Kato does as part of his general Phosphorylation study is frequently linked to other disciplines of science, such as BAG3, Optineurin and I-Kappa-B Kinase, therefore creating a link between diverse domains of science.
His Serine research includes themes of Protein structure and Kinase.
His HEK 293 cells study incorporates themes from Transport protein, Signal transducing adaptor protein and Binding site.
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