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Li Shao, Ph.D. - Publications

Affiliations: 
2002 Stony Brook University, Stony Brook, NY, United States 
Area:
Biochemistry, Cell Biology
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2003 Shao L, Haltiwanger RS. O-fucose modifications of epidermal growth factor-like repeats and thrombospondin type 1 repeats: unusual modifications in unusual places. Cellular and Molecular Life Sciences : Cmls. 60: 241-50. PMID 12678489 DOI: 10.1007/s000180300019  0.597
2002 Shao L, Moloney DJ, Haltiwanger R. Fringe modifies O-fucose on mouse Notch1 at epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region. The Journal of Biological Chemistry. 278: 7775-82. PMID 12486116 DOI: 10.1074/Jbc.M212221200  0.608
2002 Shao L, Moloney DJ, Haltiwanger RS. O-glycosylation of EGF repeats: Identification and initial characterization of a UDP-glucose: Protein O-glucosyltransferase Glycobiology. 12: 763-770. PMID 12460944 DOI: 10.1093/Glycob/Cwf085  0.576
2002 Panin VM, Shao L, Lei L, Moloney DJ, Irvine KD, Haltiwanger RS. Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe. The Journal of Biological Chemistry. 277: 29945-52. PMID 12036964 DOI: 10.1074/Jbc.M204445200  0.611
2001 Wang Y, Shao L, Shi S, Harris RJ, Spellman MW, Stanley P, Haltiwanger RS. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. The Journal of Biological Chemistry. 276: 40338-45. PMID 11524432 DOI: 10.1074/Jbc.M107849200  0.586
2000 Moloney DJ, Panin VM, Johnston SH, Chen J, Shao L, Wilson R, Wang Y, Stanley P, Irvine KD, Haltiwanger RS, Vogt TF. Fringe is a glycosyltransferase that modifies Notch. Nature. 406: 369-75. PMID 10935626 DOI: 10.1038/35019000  0.568
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