Biochemistry, Biophysics, Stereochemistry, Nuclear magnetic resonance spectroscopy and Crystallography are his primary areas of study. The various areas that Ichio Shimada examines in his Biophysics study include Extracellular, Receptor, Intracellular, KcsA potassium channel and Protein–protein interaction. Ichio Shimada interconnects Gating, Helix, Crystal structure, Immunoglobulin light chain and Ion channel in the investigation of issues within Stereochemistry.
His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Immunoglobulin G, Molecular mass, Two-dimensional nuclear magnetic resonance spectroscopy, Analytical chemistry and Peptide. He has researched Crystallography in several fields, including Peptide sequence, Molecule, Nuclear Overhauser effect and Binding site. His study in Binding site is interdisciplinary in nature, drawing from both Supramolecular chemistry, Plasma protein binding and Cyclic nucleotide-binding domain.
His primary areas of investigation include Biochemistry, Biophysics, Stereochemistry, Crystallography and Nuclear magnetic resonance spectroscopy. His research brings together the fields of Molecular biology and Biochemistry. His study on Biophysics also encompasses disciplines like
His Stereochemistry course of study focuses on Peptide and Peptide sequence. His work on Crystal structure as part of general Crystallography research is frequently linked to Paramagnetism, bridging the gap between disciplines. His Nuclear magnetic resonance spectroscopy research incorporates themes from Computational chemistry, Drug discovery and Analytical chemistry.
Ichio Shimada mainly investigates Biophysics, Cell biology, Protein structure, Nuclear magnetic resonance spectroscopy and Receptor. His research in Biophysics intersects with topics in G protein-coupled receptor, G protein and Binding site. His work carried out in the field of Binding site brings together such families of science as Plasma protein binding and Ion channel.
The various areas that Ichio Shimada examines in his Nuclear magnetic resonance spectroscopy study include Effector, Computational chemistry and Solubility. The Receptor study combines topics in areas such as Ligand, Cell, Signal transduction and Stereochemistry. His Actin research is under the purview of Biochemistry.
His scientific interests lie mostly in Biophysics, Receptor, Protein structure, G protein-coupled receptor and Plasma protein binding. In his papers, Ichio Shimada integrates diverse fields, such as Biophysics and Ceramide Transfer Protein. His Receptor research incorporates elements of Macrophage, Tumor progression, Stereochemistry and Immunotherapy.
His G protein-coupled receptor research includes themes of Lipid bilayer, Ligand, Membrane protein and Drug discovery. His Plasma protein binding study integrates concerns from other disciplines, such as Poly-binding protein, Amino acid, Gating and Binding site. His study looks at the relationship between Binding site and topics such as Allosteric regulation, which overlap with Molecular dynamics.
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.
Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures.
Hiroaki Gouda;Hidetaka Torigoe;Akiko Saito;Moriyuki Sato.
Biochemistry (1992)
A novel NMR method for determining the interfaces of large protein-protein complexes.
Hideo Takahashi;Tamiji Nakanishi;Keiichiro Kami;Yoji Arata.
Nature Structural & Molecular Biology (2000)
Efficacy of the β₂-adrenergic receptor is determined by conformational equilibrium in the transmembrane region.
Yutaka Kofuku;Takumi Ueda;Junya Okude;Yutaro Shiraishi.
Nature Communications (2012)
Differential N-glycan patterns of secreted and intracellular IgG produced in Trichoplusia ni cells.
Tsu-An Hsu;Noriko Takahashi;Yoshinori Tsukamoto;Koichi Kato.
Journal of Biological Chemistry (1997)
Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography.
H. Nakagawa;Y. Kawamura;K. Kato;I. Shimada.
Analytical Biochemistry (1995)
Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases
Yuji Funakoshi;Yusuke Doi;Nao Hosoda;Naoyuki Uchida.
Genes & Development (2007)
Structural Basis of the Interaction between Chemokine Stromal Cell-derived Factor-1/CXCL12 and Its G-protein-coupled Receptor CXCR4
Yutaka Kofuku;Chie Yoshiura;Takumi Ueda;Hiroaki Terasawa.
Journal of Biological Chemistry (2009)
Functional Dynamics of Deuterated β2-Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy†
Yutaka Kofuku;Takumi Ueda;Takumi Ueda;Junya Okude;Yutaro Shiraishi.
Angewandte Chemie (2014)
Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins.
Hideo Takahashi;Jae Il Kim;Hye Jung Min;Kazuki Sato.
Journal of Molecular Biology (2000)
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures
Ichio Shimada;Takumi Ueda;Yutaka Kofuku;Matthew T. Eddy.
Nature Reviews Drug Discovery (2019)
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