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1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1.
Solution 1H NMR is used to probe the environments of the donor protons of eight strong hydrogen bonds on the distal side of the heme substrate in the cyanide-inhibited, substrate-bound complex ofExpand
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Solution 1H, 15N NMR spectroscopic characterization of substrate-bound, cyanide-inhibited human heme oxygenase: water occupation of the distal cavity.
A solution NMR spectroscopic study of the cyanide-inhibited, substrate-bound complex of uniformly (15)N-labeled human heme oxygenase, hHO, has led to characterization of the active site with respectExpand
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Two New Nitrone Alkaloids from Huperzia serrata
Two new nitrone alkaloids were isolated from the whole plant of Huperzia serrata (Thunb.) Trev. They are both phlegmarine-type lycopodium alkaloids with a nitrone moiety. Their structures wereExpand
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A site-specific genomic integration strategy for sustained expression of glucagon-like peptide-1 in mouse muscle for controlling energy homeostasis.
The incretin hormone glucagon-like peptide-1 (GLP-1) exerts important functions in controlling glucose and energy homeostasis. Endogenous GLP-1 has a very short half-life due to DPP-IV-mediatedExpand
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Chiral-recognition chromatography of β-blockers on continuous polymer beds with immobilized cellulase as enantioselective protein
Columns prepared by coupling cellulase as a chiral selector to silica beads are very efficient for the separation of enantiomers. In this paper we show that continuous polymer beds compete favorablyExpand
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Solution NMR Characterization of an Unusual Distal H-bond Network in the Active Site of the Cyanide-inhibited, Human Heme Oxygenase Complex of the Symmetric Substrate, 2,4-Dimethyldeuterohemin* 210
The presence of variable static hemin orientational disorder about the α-γ-meso axis in the substrate complexes of mammalian heme oxygenase, together with the incomplete averaging of a second,Expand
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Solution 1H NMR Investigation of the Active Site Molecular and Electronic Structures of Substrate-bound, Cyanide-inhibited HmuO, a Bacterial Heme Oxygenase fromCorynebacterium diphtheriae * 210
The molecular structure and dynamic properties of the active site environment of HmuO, a heme oxygenase (HO) from the pathogenic bacterium Corynebacterium diphtheriae, have been investigated by 1HExpand
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Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch.
  • G. Wu, Y. Li, +4 authors Houming Wu
  • Chemistry, Medicine
  • Biochemical and biophysical research…
  • 5 October 2000
From the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem.Expand
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1H NMR Investigation of the Solution Structure of Substrate-free Human Heme Oxygenase
1H NMR was used to investigate the molecular structure, and dynamic properties of soluble, recombinant, substrate-free human heme oxygenase (apohHO) on a comparative basis with similar studies on theExpand
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