Koichi Kato focuses on Biochemistry, Stereochemistry, Endoplasmic reticulum, Glycan and Endoplasmic-reticulum-associated protein degradation. Biochemistry is often connected to Biophysics in his work. His Stereochemistry study integrates concerns from other disciplines, such as Protein structure, Ubiquitin and Lysine.
His Endoplasmic reticulum research includes elements of Lectin, Membrane protein and Glycoprotein. His work in Glycoprotein addresses issues such as Cell biology, which are connected to fields such as Saccharomyces cerevisiae and Protein subunit. His research investigates the connection with Endoplasmic-reticulum-associated protein degradation and areas like Mannose which intersect with concerns in Protein folding, Mannosidases and alpha-Mannosidase.
His primary scientific interests are in Biochemistry, Stereochemistry, Glycan, Biophysics and Nuclear magnetic resonance spectroscopy. His Biochemistry research focuses on Glycoprotein, Endoplasmic reticulum, Protein structure, Mannose and Glycosylation. His research integrates issues of Immunoglobulin G, Recombinant DNA and Cell biology in his study of Glycoprotein.
His Stereochemistry research is multidisciplinary, relying on both Residue, Ubiquitin and Molecule. His biological study spans a wide range of topics, including Chaperone and Proteasome. Koichi Kato works mostly in the field of Nuclear magnetic resonance spectroscopy, limiting it down to topics relating to Crystallography and, in certain cases, Two-dimensional nuclear magnetic resonance spectroscopy, as a part of the same area of interest.
The scientist’s investigation covers issues in Biophysics, Stereochemistry, Molecular dynamics, Cell biology and Biochemistry. The Biophysics study combines topics in areas such as KaiA, Circadian clock, KaiC and Phosphorylation. His studies deal with areas such as Amino acid, Aspartic acid, Residue, Catalysis and Deamidation as well as Stereochemistry.
His Cell biology research integrates issues from Peroxidase, Desiccation tolerance, Gene and Tardigrade. His work on Glycoprotein, Mannose and Pyridoxal as part of general Biochemistry study is frequently connected to Kynurenine and Kynurenic acid, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. His work carried out in the field of Glycoprotein brings together such families of science as Immunoglobulin G, Endoplasmic reticulum, Recombinant DNA and Secretory pathway.
Koichi Kato mainly investigates Biophysics, Biochemistry, Immunoglobulin G, Molecular dynamics and Glycoprotein. His work in the fields of Biochemistry, such as Isozyme, Non-competitive inhibition and Docking, intersects with other areas such as Kynurenine and Carbenoxolone. The concepts of his Immunoglobulin G study are interwoven with issues in Receptor and Small-angle X-ray scattering.
His studies in Molecular dynamics integrate themes in fields like Conformational isomerism, Fucosylation, Nuclear magnetic resonance spectroscopy and Fragment crystallizable region. Koichi Kato has included themes like Transfection, Protein folding, Endoplasmic reticulum, Thioredoxin and Mannose in his Glycoprotein study. His Cell biology research is multidisciplinary, incorporating elements of Glycosylation and Enzyme.
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Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.
Yoshinao Wada;Parastoo Azadi;Catherine E. Costello;Anne Dell.
Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)
Mitsunori Shiroishi;Kimiko Kuroki;Linda Rasubala;Kouhei Tsumoto.
Proceedings of the National Academy of Sciences of the United States of America (2006)
Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1.
Shigeki Matsumiya;Yoshiki Yamaguchi;Jun-ichi Saito;Mayumi Nagano.
Journal of Molecular Biology (2007)
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
Eri Sakata;Yoshiki Yamaguchi;Eiji Kurimoto;Jun Kikuchi.
EMBO Reports (2003)
Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.
Erin M. Quan;Yukiko Kamiya;Yukiko Kamiya;Daiki Kamiya;Vladimir Denic.
Molecular Cell (2008)
A protein kinase C-beta-selective inhibitor ameliorates neural dysfunction in streptozotocin-induced diabetic rats.
J Nakamura;K Kato;Y Hamada;M Nakayama.
Aβ polymerization through interaction with membrane gangliosides
Katsumi Matsuzaki;Koichi Kato;Koichi Kato;Katsuhiko Yanagisawa.
Biochimica et Biophysica Acta (2010)
Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin.
K Kato;S Goto;Y Inaguma;K Hasegawa.
Journal of Biological Chemistry (1994)
Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans.
Nobuko Hosokawa;Yukiko Kamiya;Daiki Kamiya;Koichi Kato;Koichi Kato.
Journal of Biological Chemistry (2009)
Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy.
Yoshiki Yamaguchi;Mamiko Nishimura;Mayumi Nagano;Hirokazu Yagi.
Biochimica et Biophysica Acta (2006)
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