KE-HE RUAN to Models, Molecular
This is a "connection" page, showing publications KE-HE RUAN has written about Models, Molecular.
Connection Strength
1.152
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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: 0.218
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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: 0.189
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Solution structure of a common substrate mimetic of cyclooxygenase-downstream synthases bound to an engineered thromboxane A2 synthase using a high-resolution NMR technique. Arch Biochem Biophys. 2005 Dec 15; 444(2):165-73.
Score: 0.189
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An active triple-catalytic hybrid enzyme engineered by linking cyclo-oxygenase isoform-1 to prostacyclin synthase that can constantly biosynthesize prostacyclin, the vascular protector. FEBS J. 2008 Dec; 275(23):5820-9.
Score: 0.058
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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: 0.055
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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: 0.048
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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: 0.047
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Advance in understanding the biosynthesis of prostacyclin and thromboxane A2 in the endoplasmic reticulum membrane via the cyclooxygenase pathway. Mini Rev Med Chem. 2004 Aug; 4(6):639-47.
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: 0.043
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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: 0.042
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Evidence of the residues involved in ligand recognition in the second extracellular loop of the prostacyclin receptor characterized by high resolution 2D NMR techniques. Arch Biochem Biophys. 2003 Oct 01; 418(1):25-33.
Score: 0.041
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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: 0.040
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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: 0.040
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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: 0.039
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Substrate access channel topology in membrane-bound prostacyclin synthase. Biochem J. 2002 Mar 15; 362(Pt 3):545-51.
Score: 0.037
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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: 0.016
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Role of Val509 in time-dependent inhibition of human prostaglandin H synthase-2 cyclooxygenase activity by isoform-selective agents. J Biol Chem. 1996 Aug 09; 271(32):19134-9.
Score: 0.006