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Document 90. Baltz T, Baltz D, Giroud C, Crockett J. Cultivation in a semi-defined medium of animal infective forms of Trypanosoma brucei, T. equiperdum, T. evansi, T. rhodesiense and T. gambiense. EMBO J 1985; 4:1273–1277. Page 394 91. Opperdoes FR, personal communication. 92. Whelan JS, Davis CL, Rule S, Ransom M, Smith OP, Metha AB, Catovsky D, Rohatiner AZ, Lister TA. Fludarabine phosphate for the treatment of low grade lymphoid malignancy. Br J Cancer 1991; 64:120–123. 93. Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallography 1991; 24:946–950. 94. Bernstein BE, Michels PAM, Hol WGJ. Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 1997; 385:275–278. 95. Michels PAM. Biology of the Cell 1988; 64:157–164. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_394.html [4/5/2004 5:43:59 PM]
Document 16 Progress in the <strong>Design</strong> of Immunomodulators Based on the <strong>Structure</strong> of Interleukin-1 Glen Spraggon University of California, San Diego, La Jolla, California Pandi Veerapandian Axiom Biotechnologies, Inc., San Diego, California, and La Jolla Institute for Experimental Medicine, La Jolla, California I. Introduction Page 395 The interleukin-1 (IL-1) family of cytokines exhibit both normal and pathological effects in almost every tissue and organ system and, as such, have been associated with cells engaged in the immune response, inflammatory cells, and cells engaged in development, differentiation, and repair processes [1–4]. Interleukin-1 can produce either a direct response on one specific target cell or act as an indirect effector molecule, inducing the expression of a variety of genes and synthesis of several proteins such as IL-2–IL-8, tumor necrosis factor (TNF), colony-stimulating factors (CSF), platelet-derived factors (PDFs), and other cytokines. Pathologically uncontrolled, IL-1 activity can induce disease states and has been linked to septic shock, the growth of acute and chronic myelogenous leukemia cells, inflammation associated with arthritis and colitis, development of atherosclerotic plaques, insulin-dependent diabetes, osteoporosis, parsitemia, and cancer [1,5,6]. Strategies to treat such diseases are being developed and usually involve the inhibition of IL-1 synthesis or the blocking of its activity [7]. The therapeutic advantage of reducing the activity of IL-1 resides in preventing its deleterious biological effects without interfering with homeostasis. In order to achieve such a goal, an understanding of the structure-function relationship of the IL-1 family of proteins at the molecular level is important. Such a knowledge could lead to the design and development of http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_395.html [4/5/2004 5:44:01 PM]
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Document 6 Structural Implications
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Page 519 and 520: Document Figure 13 The identified p
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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