スポンサーリンク
Laboratory Of Structure-function Biochemistry Kyushu University | 論文
- Chemical Syntheses of Phenylalanine Derivatives Containing Halogenated Benzene Ring as Structural Explorers for Elucidation of Molecular Mechanisms of Receptor Interacions
- Effects of Substitution of Hydrophobic Amino Acids by Tryptophan on Receptor Binding and Biological Activity of Neuropeptide Nociceptin
- The Effects of Arg→Trp and Lys→Trp Substitutions for Arg-Lys^ Residues in a Superagonist [Arg-Lys^]-Nociceptin on the ORL1 Receptor Binding and Activation
- Histidines as Structurally Essential Residue for the Delta Opioid Receptor Activation
- Structural Studies of [2',6'-Dimethyl-L-tyrosine^1]Endomorphin-2 Analogues Containing Proline Mimics
- Essential Amino Acid Residues in the ORL1 Receptor Transmembrane Domains for Receptor Activation
- Leucine-14 of Nociceptin Is a Structural Element in the CH/π Interaction with the Receptor Aromatic Group
- Structural Requirements in Activation of Opioid Receptor-Like ORL1 Receptor by Nociceptin
- Phosphatase assay for multi-phosphorylated substrates using phosphatase specific-motif antibody
- The Trp residue of opioid receptor TM5 present at the cell membrane interface is a molecular anchor for full activation
- Exploration of the Binding Site of ORL1 Nociceptin Receptor Antagonist
- Functional Analysis of a Histidine Residue Essential for Receptor Activation of Delta Opioid Receptor
- Receptor Binding Characteristics of Tritium-Labeled Pure Antagonist Peptide for Hyperalgesic Nociceptin ORL1 Receptor
- Structural Analysis of Delta Opioid Receptor Dimer by Bivalent Deltorphin II Analogs
- Affinity Labeling of the ORL1 Nociceptin Receptor by Cys(Npys)-Elongated RYYRIK Peptide Antagonist
- Structural Essentials of Hyperalgesic Nociceptin ORL1 Receptor for Ligand Binding and Receptor Activation
- Structural Characteristics of Thr-Gly Dipeptide Repeat in the Drosophila Clock Protein PERIOD
- Processing of Precursor Protein of the Cricket Gryllus bimaclatus Circadian Rhythm Neuropeptide PDF and PAP and Their Axonal Transport
- Effects of the Halogenation of Phe-Phenyl Group of Two Consecutive Residues in Endomorphin-2 on the Interaction with the μ-Opioid Receptors
- The Effect of Halogenation of Phe-Phenyl Group of Two Consecutive Phe Residues Present in Neuropeptide Substance P on Its Specific Receptor Interaction