Wu J - Search Results

1

Evidence of the residues involved in ligand recognition in the second extracellular loop of the prostacyclin receptor characterized by high resolution 2D NMR techniques.

Ruan KH, Wu J, So SP, Jenkins LA. Ruan KH, et al. Among authors: wu j. Arch Biochem Biophys. 2003 Oct 1;418(1):25-33. doi: 10.1016/s0003-9861(03)00401-6. Arch Biochem Biophys. 2003. PMID: 13679079

2

Solution structure and topology of the N-terminal membrane anchor domain of a microsomal cytochrome P450: prostaglandin I2 synthase.

Ruan KH, So SP, Zheng W, Wu J, Li D, Kung J. Ruan KH, et al. Among authors: wu j. Biochem J. 2002 Dec 15;368(Pt 3):721-8. doi: 10.1042/BJ20021001. Biochem J. 2002. PMID: 12193162 Free PMC article.

3

Identification of residues important for ligand binding of thromboxane A2 receptor in the second extracellular loop using the NMR experiment-guided mutagenesis approach.

So SP, Wu J, Huang G, Huang A, Li D, Ruan KH. So SP, et al. Among authors: wu j. J Biol Chem. 2003 Mar 28;278(13):10922-7. doi: 10.1074/jbc.M209337200. Epub 2003 Jan 27. J Biol Chem. 2003. PMID: 12551898 Free article.

Through two-dimensional (1)H NMR experiments, the overall three-dimensional structure of a constrained synthetic peptide mimicking the eLP2 had been determined by our group (Ruan, K.-H., So, S.-P., Wu, J., Li, D., Huang, A., and Kung, J. (2001) Biochemistry 4 …

Through two-dimensional (1)H NMR experiments, the overall three-dimensional structure of a constrained synthetic peptide mimicking the eLP2 …

4

Determination of the membrane contact residues and solution structure of the helix F/G loop of prostaglandin I2 synthase.

Wu J, So SP, Ruan KH. Wu J, et al. Arch Biochem Biophys. 2003 Mar 1;411(1):27-35. doi: 10.1016/s0003-9861(02)00728-2. Arch Biochem Biophys. 2003. PMID: 12590920

5

Identification of the residues in the helix F/G loop important to catalytic function of membrane-bound prostacyclin synthase.

Deng H, Wu J, So SP, Ruan KH. Deng H, et al. Among authors: wu j. Biochemistry. 2003 May 20;42(19):5609-17. doi: 10.1021/bi026749z. Biochemistry. 2003. PMID: 12741817

6

Solution structure of the third extracellular loop of human thromboxane A2 receptor.

Wu J, So SP, Ruan KH. Wu J, et al. Arch Biochem Biophys. 2003 Jun 15;414(2):287-93. doi: 10.1016/s0003-9861(03)00192-9. Arch Biochem Biophys. 2003. PMID: 12781781

7

Structural and functional characterization of the first intracellular loop of human thromboxane A2 receptor.

Geng L, Wu J, So SP, Huang G, Ruan KH. Geng L, et al. Among authors: wu j. Arch Biochem Biophys. 2004 Mar 15;423(2):253-65. doi: 10.1016/j.abb.2004.01.001. Arch Biochem Biophys. 2004. PMID: 15001390

8

NMR structure of the thromboxane A2 receptor ligand recognition pocket.

Ruan KH, Wu J, So SP, Jenkins LA, Ruan CH. Ruan KH, et al. Among authors: wu j. Eur J Biochem. 2004 Jul;271(14):3006-16. doi: 10.1111/j.1432-1033.2004.04232.x. Eur J Biochem. 2004. PMID: 15233797 Free article.

9

The N-terminal membrane anchor domain of the membrane-bound prostacyclin synthase involved in the substrate presentation of the coupling reaction with cyclooxygenase.

Ruan KH, Deng H, Wu J, So SP. Ruan KH, et al. Among authors: wu j. Arch Biochem Biophys. 2005 Mar 15;435(2):372-81. doi: 10.1016/j.abb.2004.12.018. Arch Biochem Biophys. 2005. PMID: 15708381

10

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.

Zhang L, Huang G, Wu J, Ruan KH. Zhang L, et al. Among authors: wu j. Biochemistry. 2005 Aug 30;44(34):11389-401. doi: 10.1021/bi050483p. Biochemistry. 2005. PMID: 16114876

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