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.
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.
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.
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.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation
Simin Rahighi;Simin Rahighi;Fumiyo Ikeda;Masato Kawasaki;Masato Kawasaki;Masato Akutsu;Masato Akutsu;Masato Akutsu.
An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae.
Ryuichi Kato;Hideyuki Ogawa.
Nucleic Acids Research (1994)
Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide
Norio Kudo;Keigo Kumagai;Nario Tomishige;Toshiyuki Yamaji.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting.
Satoshi Hirano;Masato Kawasaki;Hideaki Ura;Ryuichi Kato.
Nature Structural & Molecular Biology (2006)
Crystal Structure of the Human Cytosolic Sialidase Neu2: EVIDENCE FOR THE DYNAMIC NATURE OF SUBSTRATE RECOGNITION
Leonard M.G. Chavas;Leonard M.G. Chavas;Cristina Tringali;Paola Fusi;Bruno Venerando.
Journal of Biological Chemistry (2005)
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.
Mitsuaki Sugahara;Tsutomu Mikawa;Takashi Kumasaka;Masaki Yamamoto.
The EMBO Journal (2000)
Structural basis for recognition of acidic-cluster dileucine sequence by GGA1
Tomoo Shiba;Hiroyuki Takatsu;Terukazu Nogi;Naohiro Matsugaki.
Intracellular phosphatidylserine is essential for retrograde membrane traffic through endosomes
Yasunori Uchida;Junya Hasegawa;Daniel Chinnapen;Takao Inoue.
Proceedings of the National Academy of Sciences of the United States of America (2011)
Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins.
Vladimir V. Rogov;Hironori Suzuki;Mija Marinković;Verena Lang.
Scientific Reports (2017)
Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.
Tomoo Shiba;Masato Kawasaki;Hiroyuki Takatsu;Terukazu Nogi;Terukazu Nogi.
Nature Structural & Molecular Biology (2003)
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