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Document 68. Robinson Jr WE, Reinecke MG, Abdel-Malek S, Jia Q, Chow SA. Inhibitors of HIV-1 replication that inhibit HIV integrase. Proc Natl Acad Sci USA 1996; 93:6326–6331. Page 118 69. Mazumder A, Wang S, Neamati N, Nicklaus M, Sunder S, Chen J, Milne GWA, Rice WG, Burke Jr TR, Pommier Y. Antiretroviral agents as inhibitors of both human immunodeficiency virus type 1 integrase and protease. J Med Chem 1996; 39;2472–2481. 70. Farnet CM, Wang B, Lipford JR, Bushman FD. Differential inhibition of HIV-1 preintegration complexes and purified integrase protein by small molecules. Proc Natl Acad Sci USA 1996; 93:9742–9747. 71. Mazumder A, Neamati N, Sommadossi J, Gosselin G, Schinazi RF, Imbach J, Pommier Y. Effects of nucleotide analogues on human immunodeficiency virus type 1 integrase. Mol Pharmacol 1996; 49:621–628. 72. Mazumder A, Neamati N, Ojwang JO, Sunder S, Rando RF, Pommier Y. Inhibition of the human immunodeficiency virus type 1 integrase by guanosine quartet structures. Biochem 1996; 35:13762–13771. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_118.html [4/5/2004 4:56:03 PM]
Document 4 Bradykinin Receptor Antagonists Donald J. Kyle Scios Nova Inc., Sunnyvale, California I. Introduction Page 119 The term “kinins” is generally made in reference to either the nonapeptide bradykinin (Arg1-Pro2-Pro3- Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) or the decapeptide kallidin (Lys1-Arg2-Pro3-Pro4-Gly5-Phe6-Ser7-Pro8- Phe9-Arg10). In rats another kinin, Ile1-Ser2-Arg3-Pro4-Pro5-Gly6-Phe7-Ser8-Pro9-Phe10-Arg11 (T-kinin) is produced under certain circumstances and binds to the same receptors as bradykinin [1,2]. A schematic of the human kinin-kallikrein system is shown in Figure 1. The release of kinins from precursor proteins (known as kininogens) is mediated by enzymes called kininogenases [3–5]. The predominant enzymes responsible are kallikreins, but others, which include trypsin, plasmin, and some snake venoms, also release kinins. Kininogens are primarily synthesized in the liver and represent an abundant source of the precursors that are required for kinin generation. These proteins are produced from alternative splicing of a single gene product and there are two forms: high molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK) [6]. Unlike HMWK, which exists in the circulation as a complex with plasma pre-kallikrein, LMWK circulates freely. During immunological reaction, charged surfaces—which may be derived from bacterial lipopolysaccharide, oligosaccharides, connective tissue proteoglycans, or damaged basement membranes—facilitate the conversion of factor XII to factor XIIa. Once factor XIIa is present, prekallikrein can be cleaved to its active form, known as plasma kallikrein. This enzyme acts upon its preferred substrate, HMWK, to release bradykinin. Plasma kallikrein is further able to convert inactive factor XII to active XIIa, thereby participating in a positive http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_119.html [4/5/2004 4:56:06 PM]
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Document Chris Tantillo. The work i
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Page 103 and 104: Document dine) and didanosine (dide
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Page 109 and 110: Document Figure 1 Retroviral lifecy
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Page 113 and 114: Document Page 88 transfer (Figure 3
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Page 117 and 118: Document Page 92 The role of the N-
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Page 139 and 140: Document cubation of phosphotyrosin
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Page 151 and 152: Document Page 121 Nearly all cells
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Page 171 and 172: Document Page 141 receptor with int
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Document Page 166 As predicated, th
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Document 6 Structural Implications
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Document All effects of the IL-1 fa
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Document Table 1 Approval Indicatio
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Document Page 438 proteins. One pot
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Document Page 443 that allowed for
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Document A. The Canyon Page 491 The
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Document Page 495 of the RNA and pr
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Document Figure 5 Some compounds wh
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Document D ddI, 152 tumour necrosis
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Document Phosphoglycerate kinase (P
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