Shriver et al ., Heparinase II from F lavobacterium heparinum. Role of cysteine in enzymatic activity as probed by chemical modification and site-directed mutagenesis. J Biol Chem. Sep. 4, l998;273(36):22904-12.
Shriver et al ., Heparinase II from F lavobacterium heparinum. Role of histidine residues in enzymatic activity as probed by chemical modification and site-directed mutagenesis. J Biol Chem. Apr. 24, l998;273(l7):l0l60-7.
Shriver et al., Biochemical investigations and mapping of the calcium-binding sites of heparinase I from F lavobacterium heparinum. J Biol Chem. Feb. 12, l999;274(7):4082-8.
Shriver et al., Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site. Proc Natl Acad Sci U S A. Sep. 12, 2000;97(l9):10359-64.
Shriver et al., Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin. Proc Natl Acad Sci U S A. Sep. 12, 2000;97(l9):10365-70.
Sievers et al., Clinical studies of new “biologic” approaches to therapy of acute myeloid leukemia with monoclonal antibodies and immunoconjugates. Curr Opin Oncol. Jan. 2000;12(1):30-5.
Silver et al., Heparinase III limits rat arterial smooth muscle cell proliferation in vitro and in vivo. Eur J Pharmacol. Jun. 12, l998;35l(l):79-83.
Solokoff et al., Targeting angiogenic pathways involving tumorstromal interaction to treat advanced human pro state cancer. Cancer Metastasis Rev. 1998-1999;17(4):307-15.
Su et al., Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from F lavobacterium heparinum. Appl. Environ. Microbiol. 1996 62: 2723-2734. Sundaram et al., Rational design of low-molecular weight heparins with improved in vivo activity. Proc Natl Acad Sci U S A. Jan. 21, 2003;l00(2):65l-6.
Takahashi et al., Cellular markers that distinguish the phases of hemangioma during infancy and childhood. J Clin Invest. Jun. l994;93(6):2357-64.
Taylor et al., Protamine is an inhibitor of angiogenesis. Nature. May 27, l982;297(5864):307-12.
Torcia et al., Interferon-alpha-induced inhibition of B16 melanoma cell proliferation: interference with the bFGF autocrine growth circuit. Biochem Biophys Res Commun. Sep. 7, 1999;262(3):838-44. Turnbull et al., Heparan sulfate: decoding a dynamic multifunctional cell regulator. Trends Cell Biol. Feb. 2001;11(2):75-82.
Valentine et al., Low-molecular-weight heparin therapy and mortality. Semin Thromb Hemost. 1997;23(2):173-8.
Venkataraman et al., Sequencing complex polysaccharides. Science. Oct. 15, l999;286(5439):537-42.
Wang et al., Antisense targeting of basic fibroblast growth factor and fibroblast growth factor receptor-1 in human melanomas blocks intratumoral angiogenesis and tumor growth. Nat Med. Aug. l997;3(8):887-93.
Weitz, Jeffrey I., Low-Molecular-Weight Heparins. N Engl J Med. Sep. 4, l997;337(l0):688-98.
Whisstock et al., Prediction of protein function from protein sequence and structure. Q Rev Biophys. Aug. 2003;36(3):307-40. Wishart et al., A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J Biol Chem. Nov. 10, l995;270(45):26782-5.
Witkowski et al., Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry. Sep. 7, 1999;38(36):11643-50.
Woll et al., Uveal melanoma: natural history and treatment options for metastatic disease. Melanoma Res. Dec. 1999;9(6):575-81. Yamada et al., Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding site of porcine intestinal heparin. J Biol Chem. Mar. 5, 1993;268(7):4780-7. Yang et al., Purification and characterization of heparinase from F lavobacterium heparinum. J Biol Chem. Feb. 10, l985;260(3): 1849-57.
Yoder et al., New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science. Jun. 4, l993;260(5l 13): 1503-7.
Yoder et al., Unusual structural features in the parallel beta-helix in pectate lyases. Structure. Dec. 15, 1993;1(4):241-51.
Zacharski et al., Blood coagulation activation in cancer: challenges for cancer treatment. Hamostaseologic. 1995;15: 14-20.
Zaia et al.,Tandem mass spectrometry of sulfated heparin-like glycosaminoglycan oligosaccharides. Anal Chem. May 15, 2003;75(l0):2445-55.
Zhang et al., 6-O-sulfotransferase-1 represents a critical enzyme in the anticoagulant heparan sulfate bio synthetic pathway. J Biol Chem. Nov. 9, 200l;276(45):423 1 1-21.
Zhao et al., Rapid, sensitive structure analysis of oligosaccharides. Proc Natl Acad Sci U S A. Mar. 4, 1997;94(5):1629-33.
