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Document 104. Bradshaw D, Dodge BB, Franz PH, Lee SC, Wilson SE. Abstracts, 3rd Interscience World Conference on Inflammation. Monte-Carlo, 1989, 183. 105. Sedgwick AD. Abstracts, 3rd Interscience World Conference on Inflammation. Monte-Carlo; 1989:183. 106. Kraulis PJ, MOLSCRIPT: a program to produce both detailed and schematic plots of protein Structures. J Appl Cryst 1991; 24:946–950. 107. Merrit EM, M RASTER 3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr 1994; D50:869–873. Page 434 108. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991; 11:281–296. 109. Russell RB, Barton CJ, Proteins, 1992; 14:309–323. 110. Barton CJ, Protein Engineering, 1989; 6:37–40. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_434.html [4/9/2004 12:10:26 AM]
Document 17 Structure and Functional Studies of Interferon: A Solid Foundation for Rational Drug Design Michael A. Jarpe Cambridge NeuroScience, Inc., Cambridge, Massachusetts Carol H. Pontzer University of Maryland, College Park, Maryland Brian E. Szente * and Howard M. Johnson University of Florida, Gainesville, Florida I. Introduction The interferons (IFNs) were discovered in 1957 by Isaacs and Lindenman when they observed that a substance secreted by virally infected cells could protect other cells from viral infection [1a]. They called this substance interferon and found that it was a protein that caused uninfected cells to produce other proteins that made them resistant. Page 435 Researchers since then have been finding a growing family of structurally related molecules: the interferons. Through the years, the interferons have been given many different names including immune, fibroblast, leukocyte, Type I, and Type II interferons. The recognized nomenclature includes alpha, beta, omega, tau, and gamma (α, β, ω, τ, and γ) interferons. Alpha, beta, omega, and tau all belong to the similar Type I subclass. Gamma is the sole member of the Type II or immune interferon class. The Type I interferons all share a greater sequence homology to each other than they do to IFN-γ (for a recent general review of the IFNs, see Reference 1b). The IFNs exert their actions on cells via cell surface receptors. Type I IFNs share the IFN Type I receptor (IFN-R1) while IFN-γ has its own unique Type II receptor. The signal transduction pathways of Type I and Type II * Current affiliation: Brigham and Women's Hospital, Boston, Massachusetts. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_435.html [4/9/2004 12:10:29 AM]
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Page 543 and 544: Document Table 1 Approval Indicatio
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