about
The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structureCrystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ionIdentification of G protein-coupled receptor genes from the human genome sequenceSelective antagonism by naloxonazine of antinociception by Tyr-D-Arg-Phe-beta-Ala, a novel dermorphin analogue with high affinity at mu-opioid receptorsMRGD, a MAS-related G-protein coupled receptor, promotes tumorigenisis and is highly expressed in lung cancerIdentification of novel peptide agonists from a random peptide library for a 5-oxo-ETE receptor, a receptor for bioactive lipids.Identification of physiologically active substances as novel ligands for MRGPRDIn vivo and in vitro evaluation of novel μ-opioid receptor agonist compounds.Identification and molecular docking studies for novel inverse agonists of SREB, super conserved receptor expressed in brain.Functional conversion of the homologous proteins alpha-lactalbumin and lysozyme by exon exchangeDiverse signaling systems activated by the sweet taste receptor in human GLP-1-secreting cells.The N-terminal domain of GPR61, an orphan G-protein-coupled receptor, is essential for its constitutive activity.Stimulation of increases in intracellular calcium and prostaglandin E2 generation in Chinese hamster ovary cells expressing receptor-Galpha16 fusion proteins.Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu.Production and characterization of the recombinant human mu-opioid receptor from transgenic silkworms.Mutation analysis and molecular modeling for the investigation of ligand-binding modes of GPR84.Structural studies of the contractile tail sheath protein of bacteriophage T4. 2. Structural analyses of the tail sheath protein, Gp18, by limited proteolysis, immunoblotting, and immunoelectron microscopy.Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone.Mapping of functional sites on the primary structure of the contractile tail sheath protein of bacteriophage T4 by mutation analysis.Most of it started with T4 phage and was then taken over.A novel partial agonist of GPBA reduces blood glucose level in a murine glucose tolerance test.Mapping of functional sites on the primary structure of the tail lysozyme of bacteriophage T4 by mutational analysis.Cloning, expression and characterization of horse L-ferritin in Escherichia coli.Expression and characterization of a baseplate protein for bacteriophage Mu, gp44.A possible novel mechanism of action of genistein and daidzein for activating thyroid hormone receptor (TR)-mediated transcription.Melanoma antigen family A4 protein produced by transgenic silkworms induces antitumor immune responses.The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein.Observation of the membrane binding activity and domain structure of gpV, which comprises the tail spike of bacteriophage P2.Site-Specific Reactivities of Cysteine Residues in Horse L-ApoferritinRedesign of the substrate-binding site of hen egg white lysozyme based on the molecular evolution of C-type lysozymesStructure of the Central Hub of Bacteriophage Mu Baseplate Determined by X-ray Crystallography of gp44Three-dimensional structures of bacteriophage neck subunits are shared in Podoviridae, Siphoviridae and Myoviridae[Recruitment of enzymatic function to alpha-lactalbumin by protein engineering]Structural studies of the contractile tail sheath protein of bacteriophage T4. 1. Conformational change of the tail sheath upon contraction as probed by differential chemical modificationExpression of goat alpha-lactalbumin in Escherichia coli and its refolding to biologically active proteinStoichiometry and inter-subunit interaction of the wedge initiation complex, gp10-gp11, of bacteriophage T4Observation of unexpected molecular binding activity for Mu phage tail fibre chaperonesGPR31 and GPR151 are activated under acidic conditionsPhage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Shigeki Takeda
@ast
Shigeki Takeda
@en
Shigeki Takeda
@es
Shigeki Takeda
@nl
type
label
Shigeki Takeda
@ast
Shigeki Takeda
@en
Shigeki Takeda
@es
Shigeki Takeda
@nl
prefLabel
Shigeki Takeda
@ast
Shigeki Takeda
@en
Shigeki Takeda
@es
Shigeki Takeda
@nl
P1006
P214
P1006
P106
P214
P31
P496
0000-0001-8979-1133
P7859
lccn-n2005015247