Carbohydrate mimetics in drug discovery

The Organic Chemistry of Sugars

Volumn , Issue , 2005, Pages 803-862

  Ernst, Beat ^a   Kolb, Hartmuth C ^b   Schwardt, Oliver ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85056048538     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420027952     Document Type: Chapter

References (365)

1. Alper, J, Searching for medicine’s sweet spot, Science, 291, 2338-2343, 2001.
2. McAuliffe, J C, Hindsgaul, O, Carbohydrate drugs-an ongoing challenge, Chem. Ind., 170-174, 1997.
3. Hounsell, E F, Glycosylation targets for drug design, Carbohydr. Res., 300, 47-48, 1997.
4. Nagai, Y, A challenge to the riddle of the carbohydrate chain, Pure Appl. Chem., 69, 1893-1896, 1997.
5. Dwek, R A, Glycobiology: toward understanding the function of sugars, Chem. Rev., 96, 683-720, 1996.
6. Simon, P M, Pharmaceutical oligosaccharides, Drug Discov. Today, 1, 522-528, 1996.
7. Petitou, M, Herbert, J-M, A new generation of antithrombotics based on synthetic oligosaccharides, In Carbohydrate-Based Drug Discovery, Wong, C-H, Ed., Wiley-VCH, Weinheim, pp. 441-460, 2003.
8. Petitou, M, Casu, B, Lindahl, U, 1976-1983, a critical period in the history of heparin: the discovery of the antithrombin binding site, Biochemie., 85, 83-89, 2003.
9. w.
10. Petitou, M, Duchaussoy, P, Herbert, J-M, Duc, G, El Hajji, M, Branellec, J-F, Donat, F, Necciari, J, Cariou, R, Bouthier, J, Garrigou, E, The synthetic pentasaccharide fondaparinux: First in the class of antithrombotic agents that selectively inhibit coagulation factor Xa, Semin. Thromb. Hemost., 28, 393-402, 2002.
11. Reviews on Glycopeptide Antibiotics: Williams, D H, Bardsley, B, The vancomycin group of antibiotics and the fight against resistant bacteria, Angew. Chem. Int. Ed., 38, 1172-1193, 1999.
12. Kaplan, J, Korty, B D, Axelsen, P H, Loll, P J, The role of sugar residues in molecular recognition by vancomycin, J. Med. Chem., 44, 1837-1840, 2001.
13. Nicolaou, K C, Boddy, C N C, Bräse, S, Winssinger, N, Chemistry, biology, and medicine of the glycopeptide antibiotics, Angew. Chem. Int. Ed., 38, 2096-2152, 1999.
14. Reviews on Aminoglycosides: Ferrier, R J, Blattner, R, Field, R A, Furneaux, R H, Gardiner, J M, Hoberg, J, Kartha, K P R, Tilbrook, D M G, Tyler, P C, Wightmen, R H, Antibiotics, Carbohydr. Chem., 33, 257-274, 2002.
15. Dworkin, R J, Aminoglycosides for the treatment of Gram-negative infections: therapeutic use, resistance and future outlook, Drug Resist Update, 2, 173-179, 1999.
16. Zembower, T R, Noskin, G A, Postelnick, M J, Nguyen, C, Peterson, L R, The utility of aminoglycosides in an era of emerging drug resistance, Int. J. Antimicrob. Agents, 10, 95-105, 1998.
17. Danishefsky, S J, Allen, J R, From the laboratory to the clinic: a retrospective on fully synthetic carbohydrate-based anticancer vaccines, Angew. Chem. Int. Ed., 39, 836-863, 2000.
18. Koganty, R R, Reddish, M A, Longenecker, B M, Glycopeptide-and carbohydrate-based synthetic vaccines for the immunotherapy of cancer, Drug Discov. Today, 1, 190-198, 1996.
19. Gruner, S A W, Locardi, E, Lohof, E, Kessler, H, Carbohydrate-based mimetics in drug design: sugar amino acids and carbohydrate scaffolds, Chem. Rev., 102, 491-514, 2002.
20. Schweizer, F, Glycosamino acids: Building blocks for combinatorial synthesis-Implications for drug discovery, Angew. Chem. Int. Ed., 41, 230-253, 2002.
21. Schwab, M E, Bartholdi, D, Degeneration and regeneration of axons in the lesioned spinal cord, Physiol. Rev., 76, 319-370, 1996.
22. Qiu, J, Cai, D, Filbin, M T, Glial inhibition of nerve regeneration in the mature mammalian CNS, Glia., 29, 166-174, 2000.
23. Fournier, A E, Strittmatter, S M, Repulsive factors and axon regeneration in the CNS, Curr. Opin. Neurobiol., 11, 89-94, 2001.
24. Huber, A B, Schwab, M E, Review: Nogo-A, a potent inhibitor of neurite outgrowth and regeneration, Biol. Chem., 381, 407-419, 2000.
25. Brittis, P A, Flanagan, J G, Nogo domains and a Nogo receptor: implications for axon regeneration, Neuron., 30, 11-14, 2001.
26. Huang, D W, McKerracher, L, Braun, P E, David, S, A therapeutic vaccine approach to stimulate axon regeneration in the adult mammalian spinal cord, Neuron., 24, 639-647, 1999.
27. Trapp, B D, Myelin-associated glycoprotein: location and potential functions, Ann. NY Acad. Sci., 605, 29-43, 1990.
28. Mukhopadhyay, G, Doherty, P, Walsh, F S, Crocker, P R, Filbin, M T, A novel role for myelin-associated glycoprotein as an inhibitor of axonal regeneration, Neuron., 13, 757-767, 1994.
29. McKerracher, L, David, S, Jackson, D L, Kottis, V, Dunn, R J, Braun, P E, Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth, Neuron., 13, 805-811, 1994.
30. Prinjha, R, Moore, S E, Vinson, M, Blake, S, Morrow, R, Christie, G, Michalovich, D, Simmons, D L, Walsh, F S, Neurobiology: inhibitor of neurite outgrowth in humans, Nature, 403, 383-384, 2000.
31. Chen, M S, Huber, A B, van der Haar, M E, Frank, M, Schnell, L, Spillmann, A A, Christ, F, Schwab, M E, Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1, Nature, 403, 434-439, 2000.
32. GrandPré, T, Nakamura, F, Vartanian, T, Strittmatter, S M, Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein, Nature, 403, 439-444, 2000.
33. Wang, K C, Koprivica, V, Kim, J A, Sivasankaran, R, Guo, Y, Neve, R L, He, Z, Oligodendrocytemyelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth, Nature, 417, 941-944, 2002.
34. Baumann, N, Pham-Dinh, D, Biology of oligodendrocyte and myelin in the mammalian central nervous system, Physiol. Rev., 81, 871-927, 2001.
35. Huber, A B, Weinmann, O, Brosamle, C, Oertle, T, Schwab, M E, Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions, J. Neurosci., 22, 3553-3567, 2002.
36. Liu, B P, Fournier, A, GrandPré, T, Strittmatter, S M, Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor, Science, 297, 1190-1193, 2002.
37. Fournier, A E, GrandPré, T, Strittmatter, S M, Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration, Nature, 409, 341-346, 2001.
38. Domeniconi, M, Cao, Z, Spencer, T, Sivasankaran, R, Wang, K C, Nikulina, E, Kimura, N, Cai, H, Deng, K, Gao, Y, He, Z, Filbin, M T, Myelin-associated glycoprotein interacts with the Nogo66 receptor to inhibit neurite outgrowth, Neuron., 35, 283-290, 2002.
39. Woolf, C J, Bloechlinger, S, It takes more than two to Nogo, Science, 297, 1132-1134, 2002.
40. Kelm, S, Pelz, A, Schauer, R, Filbin, M T, Song, T, de Bellard, M E, Schnaar, R L, Mahoney, J A, Hartnell, A, Bradfield, P, Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily, Curr. Biol., 4, 965-972, 1994.
41. Powell, L D, Varki, A, I-type lectins, J. Biol. Chem., 270, 14243-14246, 1995.
42. Crocker, P R, Varki, A, Siglecs in the immune system, Immunology, 103, 137-145, 2001.
43. Schachner, M, Bartsch, U, Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin, Glia., 29, 154-165, 2000.
44. Powell, L, I-type lectins, In Essentials of Glycobiology, Varki, A, Cummings, R, Esko, J, Freeze, H, Hart, G, Marth, J, Eds., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp. 363-378, 1999.
45. Bartsch, U, Bandtlow, C E, Schnell, L, Bartsch, S, Spillmann, A A, Rubin, B P, Hillenbrand, R, Montag, D, Schwab, M E, Schachner, M, Lack of evidence that myelin-associated glycoprotein is a major inhibitor of axonal regeneration in the CNS, Neuron., 15, 1375-1381, 1995.
46. Crocker, P R, Kelm, S, Hartnell, A, Freeman, S, Nath, D, Vinson, M, Mucklow, S, Sialoadhesin and related cellular recognition molecules of the immunoglobulin superfamily, Biochem. Soc. Trans., 24, 150-156, 1996.
47. Schnaar, R L, Glycobiology of the nervous system. In Carbohydrates in Chemistry and Biology, Part II: Biology of Saccharides, Wiley-VCH, Weinheim, pp. 1013-1027, 2000.
48. Yamashita, T, Higuchi, H, Tohyama, M, The p75 receptor transduces the signal from myelinassociated glycoprotein to Rho, J. Cell. Biol., 157, 565-570, 2002.
49. Lehmann, M, Fournier, A, Selles-Navarro, I, Dergham, P, Sebok, A, Leclerc, N, Tigyi, G, McKerracher, L, Inactivation of Rho signaling pathway promotes CNS axon regeneration, J. Neurosci., 19, 7537-7547, 1999.
50. Lang, P, Gesbert, F, Delespine-Carmagnat, M, Stancou, R, Pouchelet, M, Bertoglio, J, Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes, EMBO J., 15, 510-519, 1996.
51. Qiu, J, Cai, D, Dai, H, McAtee, M, Hoffman, P N, Bregman, B S, Filbin, M T, Spinal axon regeneration induced by elevation of cyclic AMP, Neuron., 34, 895-903, 2002.
52. Neumann, S, Bradke, F, Tessier-Lavigne, M, Basbaum, A I, Regeneration of sensory axons within the injured spinal cord induced by intraganglionic cAMP elevation, Neuron., 34, 885-893, 2002.
53. Vinson, M, van der Merwe, P A, Kelm, S, May, A, Jones, E Y, Crocker, P R, Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis, J. Biol. Chem., 271, 9267-9272, 1996.
54. van der Merwe, P A, Crocker, P R, Vinson, M, Barclay, A N, Schauer, R, Kelm, S, Localization of the putative sialic acid-binding site on the immunoglobulin superfamily cell-surface molecule CD22, J. Biol. Chem., 271, 9273-9280, 1996.
55. May, A P, Robinson, R C, Vinson, M, Crocker, P R, Jones, E Y, Crystal structure of the N-terminal domain of sialoadhesin in complex with 30-sialyllactose at 1.85 Å resolution, Mol. Cell., 1, 719-728, 1998.
56. Collins, B E, Ito, H, Sawada, N, Ishida, H, Kiso, M, Schnaar, R L, Enhanced binding of the neural siglecs, myelin-associated glycoprotein and Schwann cell myelin protein, to Chol-1 (a-series) gangliosides and novel sulfated Chol-1 analogs, J. Biol. Chem., 274, 37637-37643, 1999.
57. Vyas, A A, Schnaar, R L, Brain gangliosides: functional ligands for myelin stability and the control of nerve regeneration, Biochimie, 83, 677-682, 2001.
58. Vyas, A A, Patel, H V, Fromholt, S E, Heffer-Lauc, M, Vyas, K A, Dang, J, Schachner, M, Schnaar, R L, From the cover: gangliosides are functional nerve cell ligands for myelin-associated glycoprotein (MAG), an inhibitor of nerve regeneration, Proc. Natl. Acad. Sci. USA, 99, 8412-8417, 2002.
59. Yang, L J S, Zeller, C B, Shaper, N L, Kiso, M, Hasegawa, A, Shapiro, R E, Schnaar, R L, Gangliosides are neuronal ligands for myelin-associated glycoprotein, Proc. Natl. Acad. Sci. USA, 93, 814-818, 1996.
60. Collins, B E, Kiso, M, Hasegawa, A, Tropak, M B, Roder, J C, Crocker, P R, Schnaar, R L, Binding specificities of the sialoadhesin family of I-type lectins. Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin, J. Biol. Chem., 272, 16889-16895, 1997.
61. Sheikh, K A, Sun, J, Liu, Y, Kawai, H, Crawford, T O, Proia, R L, Griffin, J W, Schnaar, R L, Mice lacking complex gangliosides develop Wallerian degeneration and myelination defects, Proc. Natl. Acad. Sci. USA, 96, 7532-7537, 1999.
62. Prabhanjan, H, Kameyama, A, Ishida, H, Kiso, M, Hasegawa, A, Regio-and stereo-selective synthesis of ganglioside GM1b and some positional analogs, Carbohydr. Res., 220, 127-143, 1991.
63. Prabhanjan, H, Aoyama, K, Kiso, M, Hasegawa, A, Synthesis of disialoganglioside GD1 and its positional isomer, Carbohydr. Res., 233, 87-99, 1992.
64. Hotta, K, Ishida, H, Kiso, M, Hasegawa, A, Synthetic studies on sialoglycoconjugates 66: first total synthesis of a cholinergic neuron-specific ganglioside GQ1ba, J. Carbohydr. Chem., 14, 491-506, 1995.
65. x ganglioside analogs modified at C-6 of the galactose residue to elucidate the mechanism of selection recognition, Carbohydr. Res., 306, 581-585, 1998.
66. Richardson, P J, Walker, J H, Jones, R T, Whittaker, V P, Identification of a cholinergic-specific antigen Chol-1 as a ganglioside, J. Neurochem., 38, 1605-1614, 1982.
67. Hirabayashi, Y, Nakao, T, Irie, F, Whittaker, V P, Kon, K, Ando, S, Structural characterization of a novel cholinergic neuron-specific ganglioside in bovine brain, J. Biol. Chem., 267, 12973-12978, 1992.
68. Strenge, K, Schauer, R, Bovin, N, Hasegawa, A, Ishida, H, Kiso, M, Kelm, S, Glycan specificity of myelin-associated glycoprotein and sialoadhesin deduced from interactions with synthetic oligosaccharides, Eur. J. Biochem., 258, 677-685, 1998.
69. Kelm, S, Brossmer, R, Isecke, R, Gross, H J, Strenge, K, Schauer, R, Functional groups of sialic acids involved in binding to siglecs (sialoadhesins) deduced from interactions with synthetic analogues, Eur. J. Biochem., 255, 663-672, 1998.
70. Sjoberg, E R, Powell, L D, Klein, A, Varki, A, Natural ligands of the B cell adhesion molecule CD22 beta can be masked by 9-O-acetylation of sialic acids, J. Cell. Biol., 126, 549-562, 1994.
71. Legler, G, Glycoside hydrolases: mechanistic information from studies with reversible and irreversible inhibitors, Adv Carbohydr Chem Biochem, 48, 319-385, 1990.
72. Legler, G, Glycosidase inhibition by basic sugar analogs and the transition state of enzymatic glycoside hydrolysis, In Iminosugars as Glycosidase Inhibitors, Stütz, A E, Ed., Wiley-VCH, Weinheim, pp. 31-36, 1999.
73. Sinnott, M L, Catalytic mechanisms of enzymic glycosyl transfer, Chem. Rev., 90, 1171-1202, 1990.
74. Davies, G, Sinnott, M L, Withers, S G, Glycosyl transfer, In Comprehensive Biological Catalysis, Sinnott, M L, Ed., Academic Press, New York, pp. 119-208, 1998.
75. Namchuk, M N, Withers, S G, Mechanism of agrobacterium b-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions, Biochemistry, 34, 16194-16202, 1995.
76. Mosi, R, Sham, H, Uitdehaag, J C M, Ruiterkamp, R, Dijkstra, B W, Withers, S G, Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase, Biochemistry, 37, 17192-17198, 1998.
77. Withers, S G, Namchuk, M, Mosi, R, Potent glycosidase inhibitors: transition state mimics or simply fortuitous binders?, In Iminosugars as Glycosidase Inhibitors, Stütz, A E, Ed., Wiley-VCH, Weinheim, pp. 188-206, 1999.
78. Ly, H, Withers, S G, Mutagenesis of glycosidases, Annu. Rev. Biochem., 68, 487-522, 1999.
79. Zechel, D L, Withers, S G, Glycosidase mechanisms: anatomy of a finely tuned catalyst, Acc. Chem. Res., 33, 11-18, 2000.
80. Rye, C S, Withers, S G, Glycosidase mechanisms, Curr. Opin. Chem. Biol., 4, 573-580, 2000.
81. Davies, G, Henrissat, B, Structures and mechanisms of glycosyl hydrolases, Structure, 3, 853-859, 1995.
82. White, A, Rose, D R, Mechanism of catalysis by retaining beta-glycosyl hydrolases, Curr. Opin. Struct. Biol., 7, 645-651, 1997.
83. Wolfenden, R, Lu, X, Young, G, Spontaneous hydrolysis of glycosides, J. Am. Chem. Soc., 120, 6814-6815, 1998.
84. Heightmann, T D, Vasella, A T, Recent insights into inhibition, structure, and mechanism of configurationretaining glycosidases, Angew. Chem. Int. Ed., 38, 750-770, 1999.
85. Vasella, A, Davies, G J, Böhm, M, Glycosidase mechanisms, Curr. Opin. Chem. Biol., 6, 619-629, 2002.
86. Truscheit, E, Frommer, W, Junge, B, Müller, L, Schmidt, D D, Wingender, W, Chemistry and biochemistry of microbial a-glucosidase inhibitors, Angew. Chem., 93, 738-755, 1981.
87. For recent reviews: see Laver, W G, Bischofberger, N, Webster, R G, Disarming flu viruses, Sci. Am., 280, 78-87, 1999.
88. Varghese, N, Development of neuraminidase inhibitors as anti-influenza virus drugs, Drug Dev. Res., 46, 176-196, 1999.
89. Gonzalez, L S, New neuraminidase inhibitors for influenza: current and potential therapeutic roles, Formulary, 35, 812-831, 2000.
90. Dreitlein, W B, Maratos, J, Brocavich, J, Zanamivir and oseltamivir: two new options for the treatment and prevention of influenza, Clin. Ther., 23, 327-355, 2001, and references cited.
91. Groopman, J E, Current advances in the diagnosis and treatment of AIDS: an introduction, Rev. Infect. Dis., 12, 908-911, 1990.
92. de Clercq, E, Antiviral drugs: current state of the art, J. Clin. Virol., 22, 73-89, 2001.
93. Zitzmann, N, Mehta, A S, Carrouée, S, Butters, T D, Platt, F M, McCauley, J, Blumberg, B S, Dwek, R A, Block, T M, Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus: implications for the development of broad spectrum antihepatitis virus agents, Proc. Natl. Acad. Sci. USA, 96, 11878-11882, 1999.
94. For the most recent reviews: see Asano, N, Nash, R J, Molyneux, R J, Fleet, G W J, Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application, Tetrahedron: Asymmetry, 11, 1645-1680, 2000.
95. Asano, N, Alkaloidal sugar mimetics: biological activities and therapeutic applications, J. Enzyme Inhib., 15, 215-234, 2000.
96. Wrodnigg, T M, From lianas to glycobiology tools: twenty-five years of 2,5-dideoxy-2,5-imino-D-mannitol, Monatshefte für Chemie, 133, 393-426, 2002.
97. Lillelund, V H, Jensen, H H, Liang, X, Bols, M, Recent developments of transition-state analogue inhibitors of non-natural product origin, Chem. Rev., 102, 515-553, 2002, and references cited.
98. Atkinson, M A, Eisenbarth, G S, Type 1 diabetes: new perspectives on disease pathogenesis and treatment, Lancet, 358, 221-229, 2001.
99. Charpentier, G, Oral combination therapy for type 2 diabetes, Diabetes Metab. Res. Rev., 18, S70-S76, 2002.
100. International Diabetes Center, http://www.parknicollet.com/diabetes (Accessed May 8, 2003).
101. Edelman, S V, Type II diabetes mellitus, Adv. Intern. Med., 43, 449-500, 1998.
102. Riddle, M, Combining sulfonylureas and other oral agents, Am. J. Med., 108, 15S-22S, 2000.
103. Yki-Järvinen, H, Combination therapy with insulin and oral agents: optimizing glycemic control in patients with type 2 diabetes mellitus, Diabetes Metab. Res. Rev., 18, S77-S81, 2002.
104. DeFronzo, R A, Pharmacologic therapy for type 2 diabetes mellitus, Ann. Intern. Med., 131, 281-303, 1999.
105. Creutzfeld, W, Effects of the a-glucosidase inhibitor acarbose on the development of long-term complications in diabetic animals: patho-physiological and therapeutic implications, Diabetes Metab. Res. Rev., 15, 289-296, 1999.
106. Schmidt, D D, Frommer, W, Müller, L, Junge, B, Wingender, W, Truscheit, E, Schäfer, D, a-Glucosidase inhibitors. New complex oligosaccharides of microbial origin, Naturwissenschaften, 64, 535-536, 1977.
107. Puls, W, Keup, U, Krause, H P, Thomas, G, Hoffmeister, F, Glucosidase inhibition. A new approach to the treatment of diabetes, obesity, and hyperlipoproteinemia, Naturwissenschaften, 64, 536-537, 1977.
108. Balfour, J A, McTavish, D, Acarbose-an update of its pharmacology and therapeutic use in diabetes mellitus, Drugs, 46, 1025-1054, 1993.
109. Hoffmann, J, Spengler, M, Efficacy of 24-week monotherapy with acarbose, glibenclamide or placebo in NIDDM patients, Diabetes Care, 6, 561-566, 1994.
110. Chiasson, J L, Josse, R G, Hunt, J A, Palmason, C, Rodger, N W, Ross, S A, Ryan, E A, Tan, M H, Wolever, T M, The efficacy of acarbose in the treatment of patients with noninsulin dependent diabetes mellitus, Ann. Intern. Med., 121, 928-935, 1994.
111. Kameda, Y, Asano, N, Yoshikawa, M, Takeuchi, M, Yamaguchi, T, Matsui, K, Horii, S, Fukase, H, Valiolamine, a new a-glucosidase inhibiting aminocyclitol produced by Streptomyces hygroscopicus, J. Antibiot., 37, 1301-1307, 1984.
112. Horii, S, Fukase, H, Matsuo, T, Kameda, Y, Asano, N, Matsui, K, Synthesis and a-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents, J. Med. Chem., 29, 1038-1046, 1986.
113. Yagi, M, Kuono, T, Aoyagi, Y, Murai, H, The structure of moranoline, a piperidine alkaloid from Morus species, Nippon Nog Kag Kaish, 50, 571-572, 1976.
114. Paulsen, H, Todt, K, Monosaccharides with a nitrogen-containing ring. XV. Nuclear magnetic resonance spectroscopic studies of hindered rotation of monosaccharides with a nitrogen-containing ring, Chem. Ber., 100, 3397-3404, 1967.
115. Inouye, S, Tsuruoka, T, Ito, T, Niida, T, Structure and synthesis of nojirimycin, Tetrahedron, 24, 2125-2144, 1968.
116. Inouye, S, Tsuruoka, T, Niida, T, Structure of nojirimycin, sugar antibiotic with nitrogen in the ring, J. Antibiot., 19, 288-292, 1966.
117. Yu, J, Choi, S Y, Moon, K D, Chung, H H, Youn, H J, Jeong, S, Park, H, Schultz, P G, A glycosidase antibody elicited against a chair-like transition state analog by in vitro immunization, Proc. Natl. Acad. Sci. USA, 95, 2880-2884, 1998.
118. Winchester, B, Fleet, G W J, Amino-sugar glycosidase inhibitors: versatile tools for glycobiologists, Glycobiology, 2, 199-210, 1992.
119. Lembcke, B, Folsch, U R, Creutzfeldt, W, Effect of 1-desoxynojirimycin derivatives on small intestinal disaccharide activities and on active transport in vitro, Digestion, 31, 120-127, 1985.
120. Taylor, R H, Barker, H M, Bowey, E A, Canfield, J E, Regulation of the absorption of dietary carbohydrate in man by two new glucosidase inhibitors, Gut, 27, 1471-1478, 1986.
121. Rhinehart, G L, Robinson, K M, Payne, A J, Wheately, M E, Fisher, J L, Liu, P S, Cheng, W, Castanospermine blocks the hyperglycemic response to carbohydrates in vivo: a result of intestinal disaccharidase inhibition, Life Sci., 41, 2325-2331, 1987.
122. Samulitis, B K, Goda, T, Lee, S M, Koldovski, O, Inhibitory mechanism of acarbose and 1-deoxynojirimycin derivatives on carbohydrases in rat small intestine, Drugs Exp. Clin. Res., 13, 517-524, 1987.
123. Robinson, K M, Begovic, M E, Rhinehart, G L, Heineke, E W, Ducep, J B, Kastner, P R, Marshall, F N, Danzin, C, New potent aglucohydrolase inhibitor MDL 73945 with long duration of action in rats, Diabetes, 40, 825-830, 1991.
124. Nojima, H, Kimura, I, Chen, F, Sugihara, Y, Haruno, M, Kato, A, Asano, N, Antihyperglycemic effects of N-containing sugars from Xanthocercis zambesiaca Morus bombycis, Aglaonema treubii, and Castanospermum australe in streptozotocin-diabetic mice, J. Nat. Prod., 61, 397-400, 1998.
125. Asano, N, Oseki, K, Kizu, H, Matsui, K, Nitrogen-in-the-ring pyranoses and furanoses: structural basis of inhibition of mammalian glycosidases, J. Med. Chem., 37, 3701-3706, 1994.
126. Asano, N, Nishida, M, Kato, A, Kizu, H, Matsui, K, Shimada, Y, Itoh, T, Baba, M, Watson, A A, Nash, R J, de Q Lilley, P M, Watkin, D J, Fleet, G W J, Homonojirimycin isomers and N-alkylated homonojirimycins: structural and conformational basis of inhibition of glycosidases, J. Med. Chem., 41, 2565-2571, 1998.
127. Johnston, P S, Feig, P U, Coniff, R F, Krol, A, Davidson, J A, Haffner, S M, Long-term titrated-dose alpha-glucosidase inhibition in non-insulin-requiring Hispanic NIDDM patients, Diabetes Care, 21, 409-415, 1998.
128. Johnston, P S, Feig, P U, Coniff, R F, Krol, A, Kelley, D E, Mooradian, A D, Chronic treatment of African-American type 2 diabetic patients with alpha-glucosidase inhibition, Diabetes Care, 21, 416-422, 1998.
129. Mitrakou, A, Tountas, N, Raptis, A E, Bauer, R J, Schulz, H, Raptis, S A, Long-term effectiveness of a new alphaglucosidase inhibitor (BAY m1099-miglitol) in insulin-treated type 2 diabetes mellitus, Diabet. Med., 15, 657-660, 1998.
130. Ahr, H J, Boberg, M, Brendel, E, Krause, H P, Steinke, W, Pharmacokinetics of miglitol. Absorption, distribution, metabolism, and excretion following administration to rats, dogs, and man, Arzneimittel-Forschung, 47, 734-745, 1997.
131. Betts, R F, Influenza virus, In Mandell, Douglas, and Bennett’s Principles and Practice of Infectious Diseases, Mandell, G L, Bennett, J E, Dolin, R, Eds., Churchill Livingstone, New York, pp. 1546-1567, 1995.
132. Hwang, M Y, Do you have the flu?, JAMA, 281, 962, 1999.
133. Palese, P, Schulman, J L, Bodo, G, Meindl, P, Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA), Virology, 59, 490-498, 1974.
134. Palese, P, Tobita, K, Ueda, M, Compans, R W, Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase, Virology, 61, 397-410, 1974.
135. Palese, P, Compans, R W, Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action, J. Gen. Virol., 33, 159-163, 1976.
136. Colman, P M, Influenza virus neuraminidase: structure, antibodies, and inhibitors, Protein Sci., 3, 1687-1696, 1994.
137. Calfee, D P, Hayden, F G, New approaches to influenza chemotherapy: neuraminidase inhibitors, Drugs, 56, 537-553, 1998.
138. Air, G M, Ghate, A A, Stray, S J, Influenza neuraminidase as target for antivirals, Adv. Virus Res., 54, 375-402, 1999.
139. Finley, J B, Atigadda, V R, Duarte, F, Zhao, J J, Brouillette, W J, Air, G M, Luo, M, Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site, J. Mol. Biol., 293, 1107-1119, 1999.
140. Houde, M, Arora, D J, Stimulation of tumor necrosis factor secretion by purified influenza virus neuraminidase, Cell Immunol., 129, 104-111, 1990.
141. Woods, J M, Bethell, R C, Coates, J A V, Healy, N, Hiscox, S A, Pearson, B A, Ryan, D M, Ticehurst, J, Tilling, J, 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro, Antimicrob. Agents Chemother., 37, 1473-1479, 1993.
142. von Itzstein, M, Dyason, J C, Oliver, S W, White, H F, Wu, W Y, Kok, G B, Pegg, M S, A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs, J. Med. Chem., 39, 388-391, 1996.
143. Coleman, P M, Varghese, J N, Laver, W G, Structure of the catalytic and antigenic sites in influenza virus neuraminidase, Nature, 303, 41-44, 1983.
144. Varghese, N, Colman, P M, Threedimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution, J. Mol. Biol., 221, 473-486, 1991.
145. Burmeister, W P, Ruigrok, R W H, Cusack, S, The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid, EMBO J., 11, 49-56, 1992.
146. von Itzstein, M, Wu, W Y, Kok, G B, Pegg, M S, Dyason, J C, Jin, B, Phan, T V, Smythe, M L, White, H F, Oliver, S W, Colman, P M, Varghese, J N, Ryan, D M, Wood, J M, Bethell, R C, Hotham, V J, Cameron, J M, Penn, C R, Rational design of potent sialidase-based inhibitors of influenza virus replication, Nature, 363, 418-423, 1993.
147. Holzer, C T, von Itzstein, M, Jin, B, Pegg, M S, Stewart, W P, Wu, W Y, Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position, Glycoconjugate J., 10, 40-44, 1993.
148. Taylor, N R, von Itzstein, M, Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis, J. Med. Chem., 37, 616-624, 1994.
149. von Itzstein, M, Wu, W Y, Jin, B, The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-Nacetylneuraminic acid: a potent influenza virus sialidase inhibitor, Carbohydr. Res., 259, 301-305, 1994.
150. Kiefel, M J, von Itzstein, M, Influenza virus sialidase: a target for drug discovery, Prog. Med. Chem., 36, 1-28, 1999.
151. Kiefel, M J, von Itzstein, M, Recent advances in the synthesis of sialic acid derivatives and sialylmimetics as biological probes, Chem. Rev., 102, 471-490, 2002.
152. Saito, M, Yu, R K, Biochemistry and function of sialidases, In Biology of the Sialic Acids, Rosenberg, A, Ed., Plenum Press, New York, pp. 261-318, 1995.
153. Dowle, M D, Howes, P D, Recent advances in sialidase inhibitors, Expert Opin. Ther. Pat., 8, 1461-1478, 1998.
154. Meindl, P, Bodo, G, Palese, P, Schulman, J, Tuppy, H, Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid, Virology, 58, 457-463, 1974.
155. Kamerling, J P, Schauer, R, Shukla, A K, Stoll, S, van Beek, H, Vliegenthart, J F G, Migration of O-acetyl groups in N, O-acetylneuraminic acids, Eur. J. Biochem., 162, 601-607, 1987.
156. Hiramatsu, Y, Tsukida, T, Nakai, Y, Inoue, Y, Kondo, H, Study on selectin blocker. 8. Lead discovery of a non-sugar antagonist using a 3D-pharmacophore model, J. Med. Chem., 43, 1476-1483, 2000.
157. Ryan, D M, Ticehurst, J, Dempsey, M H, Penn, C R, Inhibition of influenza virus replication in mice by GG 167 is consistent with extracellular activity of viral neuraminidase, Antimicrob. Agents Chemother., 38, 2270-2275, 1994.
158. Chandler, M, Bamford, M J, Conroy, R, Lamont, B, Patel, B, Patel, V K, Steeples, I P, Storer, R, Weir, N G, Wright, M, Williamson, C, Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino-Neu5Ac2en. X-ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-D-erythro-L-gluco-nonionic acid, J. Chem. Soc., Perkin. Trans. 1, 1173-1180, 1995.
159. Smith, P W, Starkey, I D, Howes, P D, Sollis, S L, Keeling, S P, Cherry, P C, von Itzstein, M, Wu, W Y, Jin, B, Synthesis and influenza virus sialidase inhibitory activity of analogs of 4-guanidino-Neu5Ac2en (GG167) with modified 5-substituents, Eur. J. Med. Chem., 31, 143-150, 1996.
160. Bamford, M J, Pichel, J C, Husman, W, Patel, B, Storer, R, Weir, N G, Synthesis of 6-, 7-and 8-carbon sugar analogs of potent anti-influenza 2,3-didehydro-2,3-dideoxy-N-acetylneuraminic acid derivatives, J. Chem. Soc., Perkin. Trans. 1, 1181-1187, 1995.
161. Smith, P W, Sollis, S L, Howes, P D, Cherry, P C, Starkey, I D, Cobley, K N, Weston, H, Scicinski, J, Merritt, A, Whittington, A, Wyatt, P, Taylor, N, Green, D, Bethell, R, Madar, S, Fenton, R J, Morley, P J, Pateman, T, Beresford, A, Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 1. Discovery, synthesis, biological activity, and structureactivity relationships of 4-guanidino-and 4-amino-4H-pyran-6-carboxamides, J. Med. Chem., 41, 787-797, 1998.
162. Wyatt, P G, Coomber, B A, Evans, D N, Jack, T I, Fulton, H E, Wonacott, A J, Colman, P, Varghese, J, Sialidase inhibitors related to zanamivir. Further SAR studies of 4-amino-4H-pyran-2-carboxylic acid-6-propylamides, Bioorg. Med. Chem. Lett., 11, 669-673, 2001.
163. Masuda, T, Shibuya, S, Arai, M, Yoshida, S, Tomozawa, T, Ohno, A, Yamashita, M, Honda, T, Synthesis and anti-influenza evaluation of orally active bicyclic ether derivatives related to zanamivir, Bioorg. Med. Chem. Lett., 13, 669-673, 2003.
164. Kim, C U, Lew, W, Williams, M A, Liu, H, Zhang, L, Swaminathan, S, Bischofberger, N, Chen, M S, Mendel, D B, Tai, C Y, Laver, W G, Stevens, R C, Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity, J. Am. Chem. Soc., 119, 681-690, 1997.
165. Kim, C U, Lew, W, Williams, M A, Wu, H, Zhang, L, Chen, X, Mendel, D B, Laver, W G, Stevens, R C, Structure-activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors, J. Med. Chem., 41, 2451-2460, 1998.
166. Mendel, D B, Tai, C Y, Escarpe, P A, Li, W, Sidwell, R W, Huffman, J H, Sweet, C, Jakeman, K J, Merson, J, Lacy, S A, Lew, W, Williams, M A, Zhang, L, Chen, M S, Bischofberger, N, Kim, C U, Oral administration of a prodrug of the influenza virus neuraminidase inhibitor GS 4071 protects mice and ferrets against influenza infection, Antimicrob. Agents Chemother., 42, 640-646, 1998.
167. Lew, W, Chen, X W, Kim, C U, Discovery and development of GS 4104 (oseltamivir): an orally active influenza neuraminidase inhibitor, Curr. Med. Chem., 7, 663-672, 2000.
168. McClellan, K, Perry, C M, Oseltamivir: a review of its use in influenza, Drugs, 61, 261-283, 2001.
169. Kerrigan, S A, Smith, P W, Stoodley, R J, (4R,5R)-4-acetylamino-5-diethylcarbamoylcyclohex-1-ene-1-carboxylic acid and (3R,4R)-4-acetylamino-3-diethylcarbamoylcyclohex-1-ene-1-carboxylic acid: new inhibitors of influenza virus sialidases, Tetrahedron Lett., 42, 4709-4712, 2001.
170. Bianco, A, Brufani, M, Manna, F, Melchioni, C, Synthesis of a carbocyclic sialic acid analogue for the inhibition of influenza virus neuraminidase, Carbohydr. Res., 332, 23-31, 2001.
171. Lew, W, Wu, H, Chen, X, Graves, B J, Escarpe, P A, MacArthur, H L, Mendel, D B, Kim, C U, Carbocyclic influenza neuraminidase inhibitors possessing a C3-cyclic amine side chain: synthesis and inhibitory activity, Bioorg. Med. Chem. Lett., 10, 1257-1260, 2000.
172. Hochgürtel, M, Biesinger, R, Kroth, H, Piecha, D, Hofmann, M W, Krause, S, Schaaf, O, Nicolau, C, Eliseev, A E, Ketones as building blocks for dynamic combinatorial libraries: highly active neuraminidase inhibitors generated via selection pressure of the biological target, J. Med. Chem., 46, 356-358, 2003.
173. Babu, Y S, Chand, P, Bantia, S, Kotian, P, Dehghani, A, El-Kattan, Y, Lin, T H, Hutchison, T L, Elliot, A J, Parker, C D, Ananth, S L, Horn, L L, Laver, G W, Montgomery, J A, BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design, J. Med. Chem., 43, 3482-3486, 2000.
174. Bantia, S, Parker, C D, Ananth, S L, Horn, L L, Andries, K, Chand, P, Kotian, P L, Dehghani, A, El-Kattan, Y, Lin, T, Hutchison, T L, Montgomery, J A, Kellog, D L, Babu, Y S, Comparison of the anti-influenza virus activity of RWJ-270201 with those of oseltamivir and zanamivir, Antimicrob. Agents Chemother., 45, 1162-1167, 2001.
175. Jedrzejas, M J, Singh, S, Brouillette, W J, Laver, W G, Air, G M, Luo, M, Structures of aromatic inhibitors of influenza virus neuraminidase, Biochemistry, 34, 3144-3151, 1995.
176. Singh, S, Jedrzejas, M J, Air, G M, Luo, M, Laver, W G, Brouillette, W J, Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction, J. Med. Chem., 38, 3217-3225, 1995.
177. Atigadda, V R, Brouillette, W J, Duarte, F, Babu, Y S, Bantia, S, Chand, P, Chu, N, Montgomery, J A, Walsh, D A, Sudbeck, E, Finley, J, Air, G M, Luo, M, Laver, G W, Hydrophobic benzoic acids as inhibitors of influenza neuraminidases, Bioorg. Med. Chem., 7, 2487-2497, 1999.
178. Finley, J B, Atigadda, V R, Duarte, F, Zhao, J J, Brouillette, W J, Air, G M, Luo, M, Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site, J. Mol. Biol., 293, 1107-1119, 1999.
179. Atigadda, V R, Brouillette, W J, Duarte, F, Ali, S M, Babu, Y S, Bantia, S, Chand, P, Chu, N, Montgomery, J A, Walsh, D A, Sudbeck, E A, Finley, J, Luo, M, Air, G M, Laver, G W, Potent inhibition of influenza sialidase by a benzoic acid containing a 2-pyrrolidinone substituent, J. Med. Chem., 42, 2332-2343, 1999.
180. Varghese, J N, Epa, V C, Colman, P M, Three-dimensional structure of the complex of 4-guanidino-Neu5ac2en and influenza virus neuraminidase, Protein Sci., 4, 1081-1087, 1995.
181. Mousa, S A, Recent advances in cell adhesion molecule (CAM) research and development: targeting CAMs for therapeutic and diagnostic applications, Drugs Fut., 21, 283-289, 1996.
182. Mousa, S A, Cheresh, D A, Recent advances in cell adhesion molecules and extracellular matrix proteins: potential clinical implications, Drug Discov. Today, 2, 187-199, 1997.
183. Cines, D B, Pollak, E S, Buck, C A, Loscalzo, J, Zimmermann, G A, McEver, R P, Pober, J S, Wick, T M, Konkle, B A, Schwartz, B S, Barnathan, E S, McCrae, K R, Hug, B A, Schmidt, A.-M., Stern, D M, Endothelial cells in physiology and in the pathophysiology of vascular disorders, Blood, 91, 3527-3561, 1998.
184. Lobb, R R, Adhesion. Its Role in Inflammatory Disease, Harlan, J M, Liu, D Y, Eds., W.H. Freeman, New York, p. 1, 1992, chap. 1.
185. Paulson, J C, Adhesion. Its Role in Inflammatory Disease, Harlan, J M, Liu, D Y, Eds., W.H. Freeman, New York, p. 19, 1992, chap. 2.
186. Kansas, G S, Selectins and their ligands: current concepts and controversies, Blood, 88, 3259-3287, 1996.
187. Varki, A, Selectin ligands, Proc. Natl. Acad. Sci. USA, 91, 7390-7397, 1994.
188. Geng, J G, Bevilacqua, M P, Moore, K L, McIntyre, T M, Prescott, S M, Kim, J M, Bliss, G A, Zimmermann, G A, McEver, R E, Rapid neutrophil adhesion to activated endothelium mediated by GMP-140, Nature, 343, 757-760, 1990.
189. Hattori, R, Hamilton, K K, Fugate, R D, McEver, R P, Sims, P J, Stimulated secretion of endothelial von Willebrand factor is accompanied by rapid redistribution to the cell surface of the intracellular granule membrane protein GMP-140, J. Biol. Chem., 264, 7768-7771, 1989.
190. Bevilacqua, M P, Pober, J S, Mendrick, D L, Cotran, R S, Gimbrone, M A Jr, Identification of an inducible endothelial-leukocyte adhesion molecule, Proc. Natl. Acad. Sci. USA, 84, 9238-9242, 1987.
191. Gallatin, W M, Weissman, I L, Butcher, E C, A cell-surface molecule involved in organ-specific homing of lymphocytes, Nature, 304, 30-34, 1983.
192. Lewinsohn, D M, Bargatze, R F, Butcher, E C, Leukocyte-endothelial cell recognition: evidence of a common molecular mechanism shared by neutrophils, lymphocytes, and other leukocytes, J. Immunol., 138, 4313-4321, 1987.
193. Lawrence, M B, Springer, T A, Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins, Cell, 65, 859-873, 1991.
194. Alon, R, Hammer, D A, Springer, T A, Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow, Nature, 374, 539-542, 1995.
195. Nicholson, M W, Barclay, A N, Singer, M S, Rosen, S D, van der Merwe, P A, Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1, J. Biol. Chem., 273, 763-770, 1998.
196. Mehta, P, Cummings, R D, McEver, R P, Affinity and kinetic analysis of P-selectin binding to P-selectin glycoprotein ligand-1, J. Biol. Chem., 273, 32506-32513, 1998.
197. Wild, M K, Huang, M.-C., Schulze-Horsel, U, van der Merwe, P A, Vestweber, D, Affinity, kinetics and thermodynamics of E-selectin binding to E-selectin ligand-1, J. Biol. Chem., 276, 31602-31612, 2001.
198. Moore, K L, Patel, K D, Bruehl, R E, Li, F, Johnson, D A, Lichtenstein, H S, Cummings, R D, Bainton, D F, McEver, R P, P-selectin glycoprotein ligand-1 mediates rolling of human neutrophils on P-selectin, J. Cell. Biol., 128, 661-671, 1995.
199. Patel, K D, McEver, R P, Comparison of tethering and rolling of eosinophils and neutrophils through selectins and P-selectin glycoprotein ligand-1, J. Immunol., 159, 4555-4565, 1997.
200. Norman, K E, Moore, K L, McEver, R P, Ley, K, Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1, Blood, 86, 4417-4421, 1995.
201. Tedder, T F, Steeber, D A, Chen, A, Engel, P, The selectins: vascular adhesion molecules, FASEB J, 9, 866-873, 1995.
202. McEver, R P, Moore, K L, Cummings, R D, Leukocyte trafficking mediated by selectin-carbohydrate interactions, J. Biol. Chem., 270, 11025-11028, 1995.
203. Lasky, L, Selectin-carbohydrate interactions and the initiation of the inflammatory response, Annu. Rev. Biochem., 64, 113-139, 1995.
204. von Andrian, U H, Berger, E M, Ramezani, L, Chambers, J D, Ochs, H D, Harlan, J M, Paulson, J C, Etzioni, A, Arfors, K-E, In vivo behavior of neutrophils from two patients with distinct inherited leukocyte adhesion deficiency syndromes, J. Clin. Invest., 91, 2893-2897, 1993.
205. X, Science, 250, 1130-1132, 1990.
206. X determinant on myeloid and tumor cells, Science, 250, 1132-1135, 1990.
207. a is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1, J. Biol. Chem., 266, 14869-14872, 1991.
208. Mihelcic, D, Schleiffenbaum, B, Tedder, T F, Sharar, S R, Harlan, J M, Winn, R K, Inhibition of leukocyte L-selectin function with a monoclonal antibody attenuates reperfusion injury to the rabbit ear, Blood, 84, 2322-2328, 1994.
209. x-containing carbohydrate reduces infarct size: role of selectins in myocardial reperfusion injury, Am. J. Physiol., 271, H2086-H2096, 1996.
210. x analog inhibits eosinophil accumulation and late asthmatic response in a guinea-pig model of asthma, Int. Arch. Allergy Immunol., 111, 32-36, 1996.
211. Park, I Y, Lee, D S, Song, M H, Kim, W, Won, J M, Cylexin: a P-selectin inhibitor prolongs heart allograft survival in hypersensitized rat recipients, Transplant. Proc., 30, 2927-2928, 1998.
212. For reviews, see. Simanek, E E, McGarvey, G J, Jablonowski, J A, Wong, C-H, Selectincarbohydrate interactions: from natural ligands to designed mimics, Chem. Rev., 98, 833-862, 1998.
213. Bertozzi, C R, Cracking the carbohydrate code for selectin recognition, Chem. Biol., 2, 703-708, 1995.
214. Musser, J H, Anderson, M B, Levy, D E, Glycomimetics as selectin inhibitors, Curr. Pharm. Des., 1, 221-232, 1995.
215. x group and its analogues as ligands for selectins: chemoenzymatic syntheses and biological functions, Angew. Chem. Int. Ed., 33, 178-190, 1994.
216. Role of hydroxyls of L-Fuc moiety. Ramphal, J Y, Zheng, Z.-L., Perez, C, Walker, L E, DeFrees, S A, Gaeta, F C A, Structure-activity relationships of sialyl Lewis X-containing oligosaccharides.1. Effect of modifications of the fucose moiety, J. Med. Chem., 37, 3459-3463, 1994.
217. Brandley, B K, Kiso, M, Abbas, S, Nikrad, P, Srivasatava, O, Foxall, C, Oda, Y, Hasegawa, A, Structure-function studies on selectin carbohydrate ligands. Modifications to fucose, sialyl acid and sulphate as sialyl acid replacement, Glycobiology, 3, 633-639, 1993.
218. x analogs. Potential selectin antagonists, Angew. Chem. Int. Ed., 33, 2096-2098, 1994. Role of the hydroxyls of D-Gal moiety.
219. x mimetics. 2. Modification of the 6-position of galactose, Bioorg. Med. Chem. Lett., 11, 459-462, 2001. Role of the substituent of the Neu5Ac moiety.
220. Tyrrell, D, James, P, Rao, N, Foxall, C, Abbas, S, Dasgupta, F, Nashed, M, Hasegawa, A, Kiso, M, Asa, D, Kidd, J, Brandley, B K, Structural requirements for the carbohydrate ligand of E-selectin, Proc. Natl. Acad. Sci. USA, 88, 10372-10376, 1991.
221. Ohmoto, H, Nakamura, K, Inoue, T, Kondo, N, Inoue, Y, Yoshino, K, Kondo, H, Ishida, H, Kiso, M, Hasegawa, A, Studies on selectin blocker. 1. Structure-activity relationships of sialyl Lewis X analogs, J. Med. Chem., 39, 1339-1343, 1996. Role of the substituents of the GlcNAc moiety.
222. DeFrees, S A, Gaeta, F C A, Lin, Y C, Ichikawa, Y, Wong, C.-H., Ligand recognition by E-selectin: analysis of conformation and activity of synthetic monomeric and bivalent sialyl Lewis X analogs, J. Am. Chem. Soc., 115, 7549-7550, 1993.
223. x recognition site of P-selectin, J. Med. Chem., 39, 4547-4553, 1996.
224. Wada, Y, Saito, T, Matsuda, N, Ihmoto, H, Yoshino, K, Ohashi, M, Kondo, H, Ishida, H, Kiso, M, Hasegawa, A, Studies on selectin blockers. 2. Novel selectin blocker as potential therapeutics for inflammatory disorders, J. Med. Chem., 39, 2055-2059, 1996.
225. x bound to E-selectin using saturation transfer difference NMR experiments, Glycobiology, 13, 435-443, 2003.
226. Siegelman, M H, Cheng, I C, Weissman, I L, Wakeland, E K, The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: role of the EGF domain in endothelial binding, Cell., 61, 611-622, 1990.
227. Watson, S R, Imai, Y, Fennie, C, Geoffrey, J, Singer, M, Rosen, S D, Lasky, L A, The complement binding-like domains of the murine homing receptor facilitate lectin activity, J. Cell. Biol., 115, 235-243, 1991.
228. Kansas, G S, Saunders, K B, Ley, K, Zakrzewics, A, Gibson, R M, Furie, B C, Tedder, T F, A role for the epidermal growth factor-like domain of P-selectin in ligand recognition and cell adhesion, J. Cell. Biol., 124, 609-618, 1994.
229. Li, S H, Burns, D K, Rumberger, J M, Presky, D H, Wilkinson, V L, Anostario, M Jr., Wolitzky, B A, Norton, C R, Familleti, P C, Kim, K J, Goldstein, A L, Cox, D C, Huang, K.-S., Consensus repeat domains of E-selectin enhance ligand binding, J. Biol. Chem., 269, 4431-4437, 1994.
230. Bargatze, R F, Kurk, S, Watts, G, Kishimoto, T K, Speer, C A, Jutila, M A, In vivo and in vitro functional examination of a conserved epitope of L-and E-selectin crucial for leukocyte-endothelial cell interactions, J. Immunol., 152, 5814-5825, 1994.
231. Gibson, R M, Kansas, G S, Tedder, T F, Furie, B, Furie, B C, Lectin and epidermal growth factor domains of P-selectin at physiologic density are the recognition unit for leukocyte binding, Blood, 85, 151-158, 1995.
232. Kolbinger, F, Patton, J T, Geisenhoff, G, Aenis, A, Li, X, Katopodis, A G, The carbohydrate-recognition domain of E-selectin is sufficient for ligand binding under both static and flow conditions, Biochemistry, 35, 6385-6392, 1996.
233. Weis, W I, Drickamer, K, Hendrickson, W A, Structure of a C-type mannose-binding protein complexed with an oligosaccharide, Nature, 360, 127-134, 1992.
234. Wright, C S, Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 Å resolution, J. Mol. Biol., 194, 501-529, 1987.
235. Bourne, Y, Rouge, P, Cambillau, C, X-Ray Structure of a (a-Man(1-3)b-Man(1-4)GlcNAc)-lectin complex at 2.1-Å resolution. The role of water in sugar-lectin interaction, J. Biol. Chem., 265, 18161-18165, 1990.
236. Shaanan, B, Lis, H, Sharon, N, Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose, Science, 254, 862-866, 1991.
237. Naismith, J H, Emmerich, C, Habash, J, Harop, S J, Hellewell, J R, Hunter, W N, Rafetery, J, Kalb, A J, Yariv, J, Refined structure of concanavalin a complexed with methyl a-D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure, Acta Crystallogr., D50, 847-858, 1994.
238. Ng, K. K.-S., Weis, W I, Structure of a selectin-like mutant of mannose-binding protein complexed with sialylated and sulfated Lewis oligosaccharides, Biochemistry, 36, 979-988, 1997.
239. Hiramatsu, Y, Tsujishita, H, Kondo, H, Studies on selectin blocker. 3. Investigation of the carbohydrate ligand sialyl Lewis X recognition site of P-selectin, J. Med. Chem., 39, 4547-4553, 1996.
240. Kogan, T P, Revelle, B M, Tapp, S, Scott, D, Beck, P J, A single amino acid residue can determine the ligand specificity of E-selectin, J. Biol. Chem., 270, 14047-14055, 1995.
241. Cooke, R M, Hale, R S, Lister, S G, Shah, G, Weir, M P, The conformation of the sialyl Lewis X ligand changes upon binding to E-selectin, Biochemistry, 33, 10591-10596, 1994.
242. Rutherford, T J, Spackman, D G, Simpson, P J, Homans, S W, 5 Nanosecond molecular dynamics and NMR study of conformational transitions in the sialyl-Lewis X antigen, Glycobiology, 4, 59-68, 1994.
243. x tetrasaccharide, free in solution and bound to E-, P-, and L-selectin, J. Am. Chem. Soc., 119, 1727-1736, 1997.
244. x in solution and bound to E-selectin, J. Am. Chem. Soc., 121, 2546-2551, 1999.
245. Ernst, B, Dragic, Z, Marti, S, Müller, C, Wagner, B, Jahnke, W, Magnani, J L, Norman, K E, Oehrlein, R, Peters, T, Kolb, H C, Design and synthesis of E-selectin antagonists, Chimia, 55, 268-274, 2001.
246. Thoma, G, Magnani, J L, Patton, J T, Synthesis and biological evaluation of a sialyl Lewis X mimic with significantly improved E-selectin inhibition, Bioorg. Med. Chem. Lett., 11, 923-925, 2001.
247. Graves, B J, Crowther, R L, Chandran, C, Rumberger, J M, Li, S, Huang, K-S, Presky, D H, Familletti, P C, Wolitzky, B A, Burns, B K, Insight into E-Selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains, Nature, 367, 532-538, 1994.
248. X and PSGL-1, Cell, 103, 467-479, 2000.
249. x: a molecular orbital study with insights into its binding properties toward the carbohydrate recognition domain of E-selectin, Bioorg. Med. Chem. Lett., 10, 2751-2757, 2002.
250. x) oligosaccharides: ligands related to E-selectin [ELAM-1] binding, J. Am. Chem. Soc., 114, 5449-5545, 1992.
251. Ishikawa, Y, Lin, C-Y, Dumas, D P, Shen, G-J, Garcia-Junceda, E, Williams, M A, Bayer, R, Ketcham, C, Walker, L E, Paulson, J C, Wong, C-H, Chemical-enzymic synthesis and conformational analysis of sialyl Lewis X and derivatives, J. Am. Chem. Soc., 114, 9283-9298, 1992.
252. Lin, C-Y, Hummel, C W, Huang, D-H, Ishikawa, Y, Nicolaou, K C, Wong, CH, Conformational studies of sialyl Lewis X in aqueous solution, J. Am. Chem. Soc., 114, 5452-5454, 1992.
253. Kolb, H C, Ernst, B, Development of tools for the design of selectin antagonists, Chem Eur J, 3, 1571-1578, 1997.
254. Kolb, H C, Ernst, B, Recent progresses in the glycodrug area, Pure Appl. Chem., 69, 1879-1884, 1997.
255. Hensley, P, McDervitt, P J, Brooks, I, Trill, J J, Field, J A, McNulty, D E, Connor, J R, Griswold, D E, Kumar, N V, Kopple, K D, Carr, S A, Dalton, B J, Johanson, K J, The soluble form of E-selectin is an asymmetric monomer. Expression, purification, and characterization of the recombinant protein, J. Biol. Chem., 269, 23949-23958, 1994.
256. x complex, Angew. Chem. Int. Ed., 34, 1841-1844, 1995.
257. x bound to E-selectin, Biomol. NMR, 9, 423-436, 1997.
258. x analog blocker of the selectin adhesion molecules, on infarct size and no-reflow in the rabbit model of acute myocardial infarction/reperfusion, J. Mol. Cell. Cardiol., 29, 2013-2025, 1997.
259. x analog does not reduce myocardial infarct size after ischemia and reperfusion in dogs, Circulation., 94, 542-546, 1996.
260. x analog attenuates neutrophil accumulation and myocardial necrosis after ischemia and reperfusion, Circulation, 90, 2390-2401, 1994.
261. x analogue) Phase II/III clinical trials (treatment of reperfusion injury in infants undergoing corrective surgery for congenital heart disease), which indicated that Cylexin showed no benefit over the placebo.
262. Koenig, A, Jain, R, Vig, R, Norgard-Sumnicht, K E, Matta, K L, Varki, A, Selectin inhibition: synthesis and evaluation of novel sialylated, sulfated and fucosylated oligosaccharides, including the major capping group of GlyCAM-1, Glycobiology, 7, 79-93, 1997.
263. Kameyama, A, Ishida, H, Kiso, M, Hasegawa, A, Synthetic studies on sialoglycoconjugates. Part 21. Total synthesis of sialyl Lewis X, Carbohydr. Res., 209, C1-C4, 1991.
264. X, J. Am. Chem. Soc., 114, 3126-3128, 1992.
265. Danishefsky, S J, Gervay, J, Peterson, J M, McDonald, F E, Koseki, K, Oriyama, T, Griffith, D A, Wong, C H, Dumas, D P, Remarkable regioselectivity in the chemical glycosylation of glycal acceptors: a concise solution to the synthesis of sialyl-Lewis X glycal, J. Am. Chem. Soc., 114, 8329-8331, 1992.
266. Hiramatsu, Y, Tsukida, T, Nakai, Y, Inoue, Y, Kondo, H, Study on selectin blocker. 8. Lead discovery of a non-sugar antagonist using a 3D-pharmacophore model, J. Med. Chem., 43, 1476-1483, 2000.
267. x, J. Org. Chem., 61, 514-524, 1996.
268. x analogues correlates with their affinity to E-selectin, Angew. Chem. Int. Ed., 40, 1941-1945, 2001.
269. Kolb, H C, Design and synthesis of a macrocyclic E-selectin antagonist, Bioorg. Med. Chem. Lett., 7, 2629-2634, 1997.
270. x mimics derived from a pharmacophore search are selectin inhibitors with antiinflammatory activity, J. Biol. Chem., 269, 19663-19666, 1994.
271. Kogan, T P, Dupre, B, Keller, K M, Scott, I L, Bui, H, Market, R V, Beck, P J, Voytus, J A, Revelle, B M, Scott, D, Rational design and synthesis of small molecule, non-oligosaccharide selectin inhibitors: (a-D-mannopyranosyloxy) biphenyl-substituted carboxylic acids, J. Med. Chem., 38, 4976-4984, 1995.
272. Kogan, T P, Dupre, B, Bui, H, McAbee, K L, Kassir, J A, Scott, I L, Hu, X, Vanderslice, P, Beck, P J, Dixon, R A F, Novel synthetic inhibitors of selectin-mediated cell adhesion: synthesis of 1,6-bis[3-(3-carboxymethylphenyl)-4-(2-a-D-mannopyranosyloxy) phenyl]-hexane (TBC1269), J. Med. Chem., 41, 1099-1111, 1998.
273. Dupre, B, Bui, H, Scott, I L, Market, R V, Keller, K M, Beck, P J, Kogan, T P, Glycomimetic selectin inhibitors: (a-D-mannopyranosyloxy) methylbiphenyls, Bioorg. Med. Chem. Lett., 6, 569-572, 1996.
274. Patel, T P, Goelz, S E, Lobb, R R, Parekh, R B, Isolation and characterization of natural proteinassociated carbohydrates for E-selectin, Biochemistry, 33, 14815-14824, 1994.
275. Miyauchi, H, Yuri, M, Tanaka, M, Kawamura, N, Hayashi, M, Synthesis and inhibitory effects of bivalent sialyl Lewis X analogs at preventing cell adhesion, Bioorg. Med. Chem. Lett., 7, 989-992, 1997.
276. Palma-Vargas, J M, Toledo-Pereyra, L, Dean, R E, Harkema, J M, Dixon, R A F, Kogan, T P, Smallmolecule selectin inhibitor protects against liver inflammatory response after ischemia and reperfusion, J. Am. Coll. Surg., 185, 365-372, 1997.
277. Press releases by Revotar Biopharmaceuticals AG and Texas Biotechnology Corporation, February 6 and August 5, 2003.
278. x, Bioorg. Med. Chem. Lett., 41, 2421-2439, 1998.
279. De Vleeschauwer, M, Vaillancourt, M, Goudreau, N, Guindon, Y, Gravel, D, Design and synthesis of a new sialyl Lewis X mimetic: how selective are the selectin receptors? Bioorg. Med. Chem. Lett., 11, 1109-1112, 2001.
280. Ramphal, J Y, Hiroshige, M, Lou, B, Gaudino, J J, Hayashi, M, Chen, S M, Chiang, L C, Gaeta, F C, DeFrees, S A, Ligand interactions with E-selectin. Identification of a new binding site for recognition of N-acyl aromatic glucosamine substituents of sialyl Lewis X, J. Med. Chem., 39, 1357-1360, 1996.
281. Graves, B J, Crowther, R L, Chandran, C, Rumberger, J M, Li, S, Huang, K-S., Presky, D H, Familletti, P C, Wolitzky, B A, Burns, D K, Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains, Nature, 367, 532-538, 1994.
282. Tsujishita, H, Hiramatsu, Y, Kondo, N, Ohmoto, H, Kondo, H, Kiso, M, Hasegawa, A, Selectin-ligand interactions revealed by molecular dynamics simulation in solution, J. Med. Chem., 40, 362-369, 1997.
283. x mimics as E-and P-selectin inhibitors, Med Res Rev, 22, 566-601, 2002.
284. Simanek, E E, McGarvey, G J, Jablonowski, J A, Wong, C.-H., Selectin-carbohydrate interactions: from natural ligands to designed mimics, Chem. Rev., 98, 833-862, 1998.
285. x determinant, Tetrahedron Lett., 36, 9161-9164, 1995.
286. X mimetics based on carbocyclic scaffolds derived from (-) quinic acid, Bioorg. Med. Chem. Lett., 7, 2729-2734, 1997.
287. Kolb, HC, Ernst, B, Unpublished results.
288. x mimetics and their relevance to P-selectin, Bioorg. Med. Chem. Lett., 8, 2803-2808, 1998.
289. x mimetics, J. Org. Chem., 60, 3100-3106, 1995.
290. x mimics, Tetrahedron Lett., 36, 5503-5506, 1995.
291. x ligand for E-selectin, Synlett, 868-870, 1994.
292. x analogues, J. Carbohydr. Chem., 15, 383-398, 1996.
293. Dasgupta, F, Musser, J H, Levy, D E, and Tang, P C, Preparation of Fucose-Containing Sialic Acids as Selectin Inhibitors, U.S. Patent 5658880, 1997.
294. Liu, A, Dillon, K, Campell, R M, Cox, D C, Huryn, D M, Synthesis of E-selectin inhibitors: use of an aryl-cyclohexyl ether as a disaccharide scaffold, Tetrahedron Lett., 37, 3785-3788, 1996.
295. x mimics: replacement of galactose by aromatic spacers, Tetrahedron Lett., 38, 4059-4062, 1997.
296. Wang, R, Wong, C-H, Synthesis of sialyl Lewis X mimetics: use of O-a-fucosyl-(1R,2R)-2-aminocyclohexanol as core structure, Tetrahedron Lett., 37, 5427-5430, 1996.
297. Lin, C-C, Shimazaki, M, Heck, M-P, Aoki, S, Wang, R, Kimura, T, Ritzen, H, Takayama, S, Wu, S-H, Weitz-Schmidt, G, Wong, C-H, Synthesis of sialyl Lewis X mimetics and related structures using the glycosyl phosphite methodology and evaluation of E-selectin inhibition, J. Am. Chem. Soc., 118, 6826-6840, 1996.
298. x mimetics, Bioorg. Med. Chem. Lett., 6, 2755-2760, 1996.
299. x mimetics, Angew. Chem. Int. Ed., 35, 88-90, 1996.
300. Lampe, T F J, Weitz-Schmidt, G, Wong, C-H, Parallel synthesis of sialyl Lewis X mimetics on a solid phase: access to a library of fucopeptides, Angew. Chem. Int. Ed., 37, 1707-1711, 1998.
301. x mimetics, J. Am. Chem. Soc., 117, 5395-5396, 1995.
302. Uchiyama, T, Woltering, T J, Wong, W, Lin, C-C, Kajimoto, T, Takebayashi, M, Weitz-Schmidt, G, Asakura, T, Noda, M, Wong, C-H, Design and synthesis of C-linked fucosides as inhibitors of E-selectin, Bioorg. Med. Chem., 4, 1149-1165, 1996.
303. x mimetics using the Ugi four-component reaction, Bioorg. Med. Chem. Lett., 8, 2333-2338, 1998.
304. Tsai, C-Y, Huang, X, Wong, C-H, Design and synthesis of cyclic sialyl Lewis X mimetics: a remarkable enhancement of inhibition by pre-organizing all essential functional groups, Tetrahedron Lett., 41, 9499-9503, 2000.
305. Martens, C L, Cwirla, S E, Lee, R Y-W, Whitehorn, E, Chen, E Y-F, Bakker, A, Martin, E L, Wagstrom, C, Gopalan, P, Smith, C W, Tate, E, Koller, K J, Schatz, P J, Dower, W J, Barrett, R W, Peptides which bind to E-selectin and block neutrophil adhesion, J. Biol. Chem., 270, 21129-21136, 1995.
306. x and E-selectin in metastasis assessed with peptide antagonists, Peptides, 23, 999-1010, 2002.
307. a with anti-inflammatory activity, Biochem. Biophys. Res. Commun., 268, 106-111, 2000.
308. x-dependent lung colonization of tumor cells, Cancer Res., 60, 450-456, 2000.
309. Renkonen, R, Fukuda, M N, Petrov, L, Paavonen, T, Renkonen, J, Häyry, P, Fukuda, M, A peptide mimic of selectin ligands abolishes in vivo inflammation but has no effect on the rat heart allograft survival, Transplantation, 74, 2-6, 2002.
310. Molenaar, T J M, Appeldoorn, C C M, de Haas, S A M, Michon, I N M, Bonnefoy, A, Hoylaerts, M F, Pannekoek, H, van Berkel, T J C, Kuiper, J, Biessen, E A L, Specific inhibition of P-selectin-mediated cell adhesion by phage display-derived peptide antagonists, Blood, 100, 3570-3577, 2002.
311. 2þ ions, J. Biol. Chem., 267, 19846-19853, 1992.
312. (2þ)-induced conformational change in the lectin domain of GMP-140, J. Biol. Chem., 266, 22313-22318, 1991.
313. Briggs, J B, Oda, Y, Gilbert, J H, Schaefer, M E, Macher, B A, Peptides inhibit selectin-mediated cell adhesion in vitro, and neutrophil influx into inflammatory sites in vivo, Glycobiology, 5, 583-588, 1995.
314. Briggs, J B, Larsen, R A, Harris, R B, Sekar, K V S, Macher, B A, Structure/activity studies of anti-inflammatory peptides based on a conserved peptide region of the lectin domain of E-, L-and P-selectin, Glycobiology, 6, 831-836, 1996.
315. Rozdzinski, E, Burnette, W N, Jones, T, Mar, V, Tuomanen, E, Prokaryotic peptides that block leukocyte adherence to selectins, J. Exp. Med., 178, 917-924, 1993.
316. Kruszynski, M, Nakada, M T, Tam, S H, Taylor, A H, Fieles, W E, Heavner, G A, Determination of the core sequence of an antagonist of selectin-dependent leukocyte adhesion and correlation of its structure with molecular modeling studies, Arch. Biochem. Biophys., 331, 23-30, 1996.
317. Tam, S H, Nakada, M T, Kruszynski, M, Fieles, W E, Taylor, A H, Mervic, M, Heavner, G A, Structure-function studies on synthetic peptides derived from the 109-118 lectin domain of selectins, Biochem. Biophys. Res. Commun., 227, 712-717, 1996.
318. Heerze, L D, Smith, R H, Wang, N, Armstrong, G D, Utilization of sialic acid-binding synthetic peptide sequences derived from pertussis toxin as novel anti-inflammatory agents, Glycobiology, 5, 427-433, 1995.
319. x mimetics as potential selectin antagonists, Tetrahedron, 53, 2485-2494, 1997.
320. x oligosaccharide, J. Cell. Biol., 117, 895-902, 1992.
321. Jacob, G S, Kirmaier, C, Abbas, S Z, Howard, S C, Steininger, C N, Welply, J K, Scudder, P, Binding of sialyl Lewis X to E-selectin as measured by fluorescence polarization, Biochemistry, 34, 1210-1217, 1995.
322. x types: relevance to anti-adhesion therapeutics, Biochemistry, 36, 5260-5266, 1997.
323. Marinier, A, Martel, A, Banville, J, Bachand, C, Remillard, R, Lapointe, P, Turmel, B, Menard, M, Harte, W E Jr., Wright, J J K, Todderud, G, Tramposch, K M, Bajorath, J, Hollenbaugh, D, Aruffo, A, Sulfated galactocerebrosides as potential antiinflammatory agents, J. Med. Chem., 40, 3234-3247, 1997.
324. Weitz-Schmidt, G, Stokmaier, D, Scheel, G, Nifant’ev, N E, Tuzikov, A B, Bovin, N V, An E-selectin binding assay based on a polyacrylamide-type glycoconjugate, Anal. Biochem., 238, 184-190, 1996.
325. Weitz-Schmidt, G, Gong, K W, Wong, C-H, Selectin/glycoconjugate binding assays for the identification and optimization of selectin antagonists, Anal. Biochem., 273, 81-88, 1999.
326. a polymer for ELISA, J. Am. Chem. Soc., 119, 7414-7415, 1997.
327. x analogs, J. Am. Chem. Soc., 117, 66-79, 1995.
328. Kretschmar, G, Sprengard, U, Kunz, H, Bartnik, E, Schmidt, W D, Toepfer, A, Hörsch, B, Krause, M, Seiffge, D, Oligosaccharide recognition by selectins: synthesis and biological activity of multivalent sialyl Lewis-X ligands, Tetrahedron, 51, 13015-13030, 1995.
329. Zhou, Q, Moore, K L, Smith, D F, Varki, A, McEver, R P, Cummings, R D, The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and nonmyeloid cells, J. Cell. Biol., 115, 557-564, 1991.
330. Ohnishi, M, Koike, H, Kawamura, N, Tojo, S J, Hayashi, M, Morooka, S, Role of P-selectin in the early stage of the arthus reaction, Immunopharmacology, 34, 161-170, 1996.
331. Norgard, K E, Moore, K L, Diaz, S, Stults, N L, Ushiyama, S, McEver, R P, Cummings, R D, Varki, A, Characterization of a specific ligand for P-selectin on myeloid cells. A minor glycoprotein with sialylated O-linked oligosaccharides, J. Biol. Chem., 268, 12764-12774, 1993.
332. Yokota, S, Nunn, M F, Morooka, S, Cross-linking of the ninth consensus repeat domain of P-selectin (GMP-140, CD62P) with a monoclonal antibody enhanced leukocyte adhesive activity, Biochem. Biophys. Res. Commun., 218, 709-713, 1996.
333. Revelle, B M, Scott, D, Beck, P J, Single amino acid residues in the E-and P-selectin epidermal growth factor domains can determine carbohydrate binding specificity, J. Biol. Chem., 271, 16160-16170, 1996.
334. Kansas, G S, Saunders, K B, Ley, K, Zakrzewicz, A, Gibson, R M, Furie, B C, Furie, B, Tedder, T F, A role for the epidermal growth factor-like domain of P-selectin in ligand recognition and cell adhesion, J. Cell. Biol., 124, 609-618, 1994.
335. Freedman, S J, Sanford, D G, Bachovchin, W W, Furie, B C, Baleja, J D, Furie, B, Structure and function of the epidermal growth factor domain of P-selectin, Biochemistry, 35, 13733-13744, 1996.
336. Ushiyama, S, Laue, T M, Moore, K L, Erickson, H P, McEver, R P, Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin, J. Biol. Chem., 268, 15229-15237, 1993.
337. Tyrell, D, James, P, Rao, N, Foxall, C, Abbas, S, Dasgupta, F, Nashed, M, Hasegawa, A, Kiso, M, Asa, D, Kidd, J, Brandley, B K, Structural requirements for the carbohydrate ligand of E-selectin, PNAS, 88, 10372-10376, 1991.
338. Patel, K D, Nollert, M U, McEver, R P, P-selectin must extend a sufficient length from the plasma membrane to mediate rolling of neutrophils, J. Cell. Biol., 131, 1893-1902, 1995.
339. Nelson, R M, Dolich, S, Aruffo, A, Cecconi, O, Bevilacqua, M P, Higher-affinity oligosaccharide ligands for E-selectin, J. Clin. Invest., 91, 1157-1166, 1993.
340. Elstad, M R, La Pine, T R, Cowley, F S, McEver, R P, McIntyre, T M, Prescott, S M, Zimmermann, G A, P-selectin regulates platelet-activating factor synthesis and phagocytosis by monocytes, J. Immunol., 155, 2109-2122, 1995.
341. Wein, M, Sterbinsky, S A, Bickel, C A, Schleiner, R P, Bochner, B S, Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin, Am. J. Respir. Cell. Mol., 12, 315-319, 1995.
342. Todderud, G, Alford, J, Millsap, K A, Aruffo, A, Tramposch, T K, PMN binding to P-selectin is inhibited by sulfatide, J. Leukocyte Biol., 52, 85-88, 1992.
343. Alon, R, Rossiter, H, Wang, X, Springer, T A, Kupper, T S, Distinct cell surface ligands mediate T lymphocyte attachment and rolling on P-and E-selectin under physiological flow, J. Cell. Biol., 127, 1485-1495, 1994.
344. Vachino, G, Chang, X-J, Veldman, G M, Kumar, R, Sako, D, Fouser, L A, Berndt, M C, Cumming, D A, P-selectin glycoprotein ligand-1 is the major counter-receptor for P-selectin on stimulated T cells and is widely distributed in non-functional form on many lymphocytic cells, J. Biol. Chem., 270, 21966-21974, 1995.
345. Aruffo, A, Kolanus, W, Walz, G, Fredman, P, Seed, B, CD62/P-selectin recognition of myeloid and tumor cell sulfatides, Cell., 67, 35-44, 1991.
346. Li, F, Wilkins, P P, Crawley, S, Weinstein, J, Cummings, R D, McEver, R P, Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P-and E-selectin, J. Biol. Chem., 271, 3255-3264, 1996.
347. Kumar, R, Camphausen, R T, Sullivan, F X, Cumming, D A, Core2 b-1,6-N-acetylglucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin, Blood, 88, 3872-3879, 1996.
348. Sako, D, Comess, K M, Barone, K M, Camphausen, R T, Cumming, D A, Shaw, G D, A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding, Cell., 83, 323-331, 1995.
349. Jutila, M A, Bargatze, R F, Kurk, S, Warnock, R A, Ehsani, N, Watson, S R, Walcheck, B, Cell surface P-and E-selectin support shear-dependent rolling of bovine g/d T cells, J. Immunol., 153, 3917-3928, 1994.
350. Puri, K D, Finger, E B, Springer, T A, The faster kinetics of L-selectin than of E-selectin and P-selectin rolling at comparable binding strength, J. Immunol., 158, 405-413, 1997.
351. Thoma, G, Patton, J T, Magnani, J L, Ernst, B, Öhrlein, R, Duthaler, R O, Versatile functionalization of polylysine: synthesis, characterization, and use of neoglycoconjugates, J. Am. Chem. Soc., 121, 5919-5929, 1999.
352. Bänteli, R, Herold, P, Bruns, C, Patton, J T, Magnani, J L, Thoma, G, Potent E-selectin antagonists, Helv. Chim. Acta, 83, 2893-2907, 2000.
353. Tempelman, L A, Hammer, D A, Receptor-mediated binding of IgE-sensitized rat basophilic leukemia cells to antigen-coated substrates under hydrodynamic flow, Biophys. J., 66, 1231-1243, 1994.
354. Alon, R, Hammer, D A, Springer, T A, Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flow, Nature, 374, 539-542, 1995.
355. Brunk, D K, Goetz, D J, Hammer, D A, Sialyl Lewis(X)/E-selectin-mediated rolling in a cell-free system, Biophys. J., 71, 2902-2907, 1996.
356. Olofsson, M, Arfors, K-E, Ramezani, L, Wolizky, B A, Butcher, E C, van Andrian, U H, Eselectin mediates leukocyte rolling in interleukin-1-treated rabbit mesentery venules, Blood, 84, 2749-2758, 1994.
357. Kubes, P, Jutila, M, Payne, D, Therapeutic potential of inhibiting leukocyte rolling in ischemia/reperfusion, J. Clin. Invest., 95, 2510-2519, 1995.
358. Norman, K E, Moore, K L, McEver, R P, Ley, K, Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1, Blood, 86, 4417-4421, 1995.
359. Damiano, E R, Westheider, J, Tözeren, A, Ley, K, Variation in the velocity, deformation, and adhesion energy density of leukocytes rolling within venules, Circ. Res., 79, 1122-1130, 1996.
360. 4-integrin, P-selectin, and E-selectin in an allergic model of inflammation, J. Exp. Med., 185, 1077-1087, 1997.
361. x mimetic, CGP69669A, disrupt E-selectin-dependent leukocyte rolling in vivo, Blood, 91, 475-483, 1998.
362. i-linked receptors, J. Immunol., 168, 1940-1949, 2002.
363. Bosse, R, Vestweber, D, Only simultaneous blocking of the L-and P-selectin completely inhibits neutrophil migration into mouse peritoneum, Eur. J. Immunol., 24, 3019-3024, 1994.
364. Harris, R R, Mackin, W M, Batt, D G, Rakich, S M, Collins, R J, Bruin, E M, Ackerman, N R, Cellular and biochemical characterization of the anti-inflammatory effects of DuP 654 in the arachidonic acid murine skin inflammation model, Skin Pharmacol., 3, 29-40, 1990.
365. Yawalkar, S, Wiesenberg-Boettcher, I, Gibson, J R, Siskin, S B, Pignat, W, Dermatopharmacologic investigation of halobetasol propionate in comparison with clobetasol 17-propionate, J. Am. Acad. Dermatol., 25, 1137-1144, 1991.