Teppei Ikeya

ORCID: 0000-0002-6721-3727
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About
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Research Areas
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Advanced NMR Techniques and Applications
  • RNA and protein synthesis mechanisms
  • Advanced MRI Techniques and Applications
  • Glycosylation and Glycoproteins Research
  • Metabolomics and Mass Spectrometry Studies
  • NMR spectroscopy and applications
  • Protein Kinase Regulation and GTPase Signaling
  • Bacteriophages and microbial interactions
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Calcium Carbonate Crystallization and Inhibition
  • Molecular spectroscopy and chirality
  • Ion channel regulation and function
  • Genetic Neurodegenerative Diseases
  • Cell death mechanisms and regulation
  • Genetics, Bioinformatics, and Biomedical Research
  • Cancer-related Molecular Pathways
  • Cancer, Hypoxia, and Metabolism
  • Lipid Membrane Structure and Behavior
  • Ubiquitin and proteasome pathways
  • Trace Elements in Health
  • Protein Tyrosine Phosphatases
  • Metabolism, Diabetes, and Cancer

Tokyo Metropolitan University
2014-2025

RIKEN Center for Biosystems Dynamics Research
2021

Health First
2019

Japan Science and Technology Agency
2014-2018

Goethe University Frankfurt
2008-2011

Frankfurt Institute for Advanced Studies
2009-2011

Nagoya University
2007

Japan Biological Informatics Consortium
2006

National Institute of Advanced Industrial Science and Technology
2005-2006

Tokyo University of Science
2006

Recent developments in in-cell NMR techniques have allowed us to study proteins detail inside living eukaryotic cells. In order complement the existing protocols, and extend range of possible applications, we introduce a novel approach for observing spectra using sf9 cell/baculovirus system. High-resolution 2D (1)H-(15)N correlation were observed four model expressed Furthermore, 3D triple-resonance Streptococcus protein G B1 domain cells by nonlinear sampling overcome short lifetime samples...

10.1021/ja310928u article EN Journal of the American Chemical Society 2013-01-18

Proteins in living cells interact specifically or nonspecifically with an enormous number of biomolecules. To understand the behavior proteins under intracellular crowding conditions, it is indispensable to observe their three-dimensional (3D) structures at atomic level a physiologically natural environment. We demonstrate first de novo protein structure determinations eukaryotes sf9 cell/baculovirus system using NMR data from exclusively. The method was applied five proteins, rat...

10.1002/anie.201900840 article EN Angewandte Chemie International Edition 2019-04-02

The γ-secretase complex has a decisive role in the development of Alzheimer’s disease, that it cleaves precursor to create amyloid β peptide whose aggregates form senile plaques encountered brains patients. Γ-secretase is member intramembrane-cleaving proteases which process their transmembrane substrates within bilayer. Many mutations early onset familial disease are linked presenilin 1, catalytic component γ-secretase, active requires its endoproteolytic cleavage into N-terminal and...

10.1073/pnas.1000778107 article EN Proceedings of the National Academy of Sciences 2010-05-05

Abstract I nvestigating three-dimensional (3D) structures of proteins in living cells by in-cell nuclear magnetic resonance (NMR) spectroscopy opens an avenue towards understanding the structural basis their functions and physical properties under physiological conditions inside cells. In-cell NMR provides data at atomic resolution non-invasively, has been used to detect protein-protein interactions, thermodynamics protein stability, behavior intrinsically disordered proteins, etc. However,...

10.1038/srep38312 article EN cc-by Scientific Reports 2016-12-02

Abstract The symbiotic nitrogen-fixing bacterium Bradyrhizobium japonicum ( B.japonicum ) enables high soybean yields with little or no nitrogen fertiliser. A two component regulatory system comprising FixL, a histidine kinase O 2 -sensing activity, and FixJ, response regulator, controls the expression of genes involved in fixation, such as fixK nifA . Only under anaerobic conditions, monophosphate group is transferred from FixL to N-terminal receiver domain FixJ (FixJ N ), which eventually...

10.1007/s12104-025-10221-w article EN cc-by Biomolecular NMR Assignments 2025-02-01

Recently we have developed the stereo-array isotope labeling (SAIL) technique to overcome conventional molecular size limitation in NMR protein structure determination by employing complete stereo- and regiospecific patterns of stable isotopes. SAIL sharpens signals simplifies spectra without loss requisite structural information, thus making large classes proteins newly accessible detailed solution determination. The automated calculation program CYANA can efficiently analyze SAIL-NOESY...

10.1002/mrc.1815 article EN Magnetic Resonance in Chemistry 2006-01-01

The product of gene At3g16450.1 from Arabidopsis thaliana is a 32 kDa, 299‐residue protein classified as resembling myrosinase‐binding (MyroBP). MyroBPs are found in plants part complex with the glucosinolate‐degrading enzyme myrosinase, and suspected to play role myrosinase‐dependent defense against pathogens. Many MyroBP‐related proteins composed repeated homologous sequences unknown structure. We report here three‐dimensional structure , which consists two tandem repeats. Because size...

10.1111/j.1742-4658.2008.06717.x article EN FEBS Journal 2008-11-11

Abstract Proteins in living cells interact specifically or nonspecifically with an enormous number of biomolecules. To understand the behavior proteins under intracellular crowding conditions, it is indispensable to observe their three‐dimensional (3D) structures at atomic level a physiologically natural environment. We demonstrate first de novo protein structure determinations eukaryotes sf9 cell/baculovirus system using NMR data from exclusively. The method was applied five proteins, rat...

10.1002/ange.201900840 article EN Angewandte Chemie 2019-04-02

This study demonstrates that boronic acid-containing polymers coated onto solid support function as synthetic mitogens for mouse lymphocytes.The polymer was synthesized by radical copolymerization of 3acrylamidophenylboronic acid with dimethylacrylamide (poly(AAPBA-DMAA)).The in the trigonal form copolymer activated lymphocytes, probably crosslinkage to glycoprotein moieties on plasma membrane surface, case lectin stimulation.A higher concentration phenylboronic surface resulted greater...

10.22203/ecm.v012a04 article EN European Cells and Materials 2006-08-03

Nuclear Magnetic Resonance (NMR) spectroscopy is a tool to investigate threedimensional (3D) structures and dynamics of biomacromolecules at atomic resolution in solution or more natural environments such as living cells. Since NMR data are principally only spectra with peak signals, it required properly deduce structural information from the sparse experimental their imperfections uncertainty, visualize 3D conformations by structure calculation. In order efficiently analyse data, Rieping et...

10.1088/1742-6596/699/1/012005 article EN Journal of Physics Conference Series 2016-03-01

Amorphous calcium carbonate (ACC) is an important precursor phase for the formation of aragonite crystals in shells Pinctada fucata. To identify ACC-binding protein inner layer shell, extracts from shell were used experiments. Semiquantitative analyses using liquid chromatography–mass spectrometry revealed that paramyosin was strongly associated with ACC shell. We discovered paramyosin, a major component adductor muscle, included myostracum, which microstructure attached to muscle. Purified...

10.1021/acs.langmuir.3c03820 article EN Langmuir 2024-04-12

Shellfish and crustaceans use calcium carbonate (CaCO3) as a protective shell exoskeleton. CaCO3 is major biomineral component in invertebrates. The Pinctada fucata contains two crystal polymorphs, with outer prismatic inner nacreous layers. Diverse organic materials play significant roles microstructure formation organic–inorganic interactions. Pif 80 has repeated acidic basic amino acid low-complexity region that specifically binds to aragonite crystals. In this study, we aimed elucidate...

10.1021/acs.cgd.3c00467 article EN Crystal Growth & Design 2023-06-23
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