KE-HE RUAN to Amino Acid Sequence
This is a "connection" page, showing publications KE-HE RUAN has written about Amino Acid Sequence.
Connection Strength
0.593
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Involvement of non-conserved residues important for PGE2 binding to the constrained EP3 eLP2 using NMR and site-directed mutagenesis. FEBS Lett. 2008 Aug 20; 582(19):2863-8.
Score: 0.052
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Assembling NMR structures for the intracellular loops of the human thromboxane A2 receptor: implication of the G protein-coupling pocket. Arch Biochem Biophys. 2008 Feb 01; 470(1):73-82.
Score: 0.050
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A profile of the residues in the second extracellular loop that are critical for ligand recognition of human prostacyclin receptor. FEBS J. 2008 Jan; 275(1):128-37.
Score: 0.050
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Engineering of a protein with cyclooxygenase and prostacyclin synthase activities that converts arachidonic acid to prostacyclin. Biochemistry. 2006 Nov 28; 45(47):14003-11.
Score: 0.046
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Solution structure of the first intracellular loop of prostacyclin receptor and implication of its interaction with the C-terminal segment of G alpha s protein. Biochemistry. 2006 Feb 14; 45(6):1734-44.
Score: 0.044
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A strategy using NMR peptide structures of thromboxane A2 receptor as templates to construct ligand-recognition pocket of prostacyclin receptor. BMC Biochem. 2005 Nov 04; 6:23.
Score: 0.043
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A profile of the residues in the first intracellular loop critical for Gs-mediated signaling of human prostacyclin receptor characterized by an integrative approach of NMR-experiment and mutagenesis. Biochemistry. 2005 Aug 30; 44(34):11389-401.
Score: 0.043
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NMR structure of the thromboxane A2 receptor ligand recognition pocket. Eur J Biochem. 2004 Jul; 271(14):3006-16.
Score: 0.039
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Structural and functional characterization of the first intracellular loop of human thromboxane A2 receptor. Arch Biochem Biophys. 2004 Mar 15; 423(2):253-65.
Score: 0.038
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Solution structure of the third extracellular loop of human thromboxane A2 receptor. Arch Biochem Biophys. 2003 Jun 15; 414(2):287-93.
Score: 0.037
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Identification of the residues in the helix F/G loop important to catalytic function of membrane-bound prostacyclin synthase. Biochemistry. 2003 May 20; 42(19):5609-17.
Score: 0.036
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Determination of the membrane contact residues and solution structure of the helix F/G loop of prostaglandin I2 synthase. Arch Biochem Biophys. 2003 Mar 01; 411(1):27-35.
Score: 0.036
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Identification of residues important for ligand binding of thromboxane A2 receptor in the second extracellular loop using the NMR experiment-guided mutagenesis approach. J Biol Chem. 2003 Mar 28; 278(13):10922-7.
Score: 0.036
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The short-neurotoxin-binding regions on the alpha-chain of human and Torpedo californica acetylcholine receptors. Biochem J. 1991 Mar 15; 274 ( Pt 3):849-54.
Score: 0.016
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Acetylcholine receptor-alpha-bungarotoxin interactions: determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Proc Natl Acad Sci U S A. 1990 Aug; 87(16):6156-60.
Score: 0.015
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Profile of the regions on the alpha-chain of human acetylcholine receptor recognized by autoantibodies in myasthenia gravis. Mol Immunol. 1992 Dec; 29(12):1507-14.
Score: 0.004
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Epitope-specific suppression of antibody response in experimental autoimmune myasthenia gravis by a monomethoxypolyethylene glycol conjugate of a myasthenogenic synthetic peptide. Proc Natl Acad Sci U S A. 1992 Jul 01; 89(13):5852-6.
Score: 0.004
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Primary structure of human thromboxane synthase determined from the cDNA sequence. J Biol Chem. 1992 Jan 15; 267(2):789-93.
Score: 0.004