Z
Zhengliang L. Wu
Researcher at Massachusetts Institute of Technology
Publications - 59
Citations - 1327
Zhengliang L. Wu is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Glycan & Heparan sulfate. The author has an hindex of 17, co-authored 57 publications receiving 1242 citations. Previous affiliations of Zhengliang L. Wu include Beth Israel Deaconess Medical Center & Northeast Ohio Medical University.
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Journal ArticleDOI
Analysis of Heparan Sulfate Oligosaccharides with Ion Pair-Reverse Phase Capillary High Performance Liquid Chromatography-Microelectrospray Ionization Time-of-Flight Mass Spectrometry†
Balagurunathan Kuberan,Miroslaw Lech,Lijuan Zhang,Zhengliang L. Wu,David L. Beeler,Robert D. Rosenberg +5 more
TL;DR: These findings should undoubtedly pave the way in deciphering multiple functional arrangements, ascribed to many biological activities, which are predictably embedded in a single large chaotic, yet well-organized HS polysaccharide chain.
Journal ArticleDOI
Enzymatic synthesis of antithrombin III-binding heparan sulfate pentasaccharide.
Balagurunathan Kuberan,Miroslaw Lech,David L. Beeler,Zhengliang L. Wu,Robert D. Rosenberg,Robert D. Rosenberg +5 more
TL;DR: The biosynthesis of bioactive HS oligosaccharides is reported using an engineered set of cloned enzymes that mimics the Golgi apparatus in vitro and rapidly and efficiently assembled the antithrombin III–binding pentasaccharide in just 6 steps, in contrast to the approximately 60 steps needed for its chemical synthesis.
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The involvement of heparan sulfate (HS) in FGF1/HS/FGFR1 signaling complex.
Zhengliang L. Wu,Lijuan Zhang,Lijuan Zhang,Tomio Yabe,Balagurunathan Kuberan,David L. Beeler,Andre Love,Andre Love,Robert D. Rosenberg,Robert D. Rosenberg +9 more
TL;DR: A mechanism for the FGF·FGFR signaling complex formation on cell membrane was proposed, where FGF and FGFR have their own binding sites on HS and a distinct ternary complex formation site is directly responsible for mitogenic activity.
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Structure and functions of human oxysterol 7α-hydroxylase cDNAs and gene CYP7B1
TL;DR: The cloned human CYP7B1 cDNA encodes a polypeptide of 506 amino acid residues that shares 40% sequence identity to human cholesterol 7alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in the conversion of cholesterol to bile acids in the liver.
Journal ArticleDOI
Universal phosphatase-coupled glycosyltransferase assay.
TL;DR: In this paper, a nonradioactive glycosyltransferase assay is described, which takes advantage of specific phosphatases that can be added into GAs to quantitatively release inorganic phosphate from the leaving groups of GAs.