Illustration Credits

Structural image for the front cover, crystal structure of a cytokine/receptor complex: x-ray diffraction image of IL-6 (beta sign) chain provided through the courtesy of Research Collaboratory for Structural Bioinformatics, 2003. H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat,

H. Weissing, I.N. Shindyalov, P.E. Bourne: The Protein Data Bank, Nucleic Acids Research 28 pp. 235-242 (2000).

Photograph of Dr. A. Wallace Conerly on dedication page furnished through the courtesy of Jay Ferchaud, Department of Public Relations, University of Mississippi Medical Center, Jackson.

Figures 1.1, 1.5, 1.8, 1.11, 1.12, 1.14, 1.15, 1.18,

I.19, 1.20, 1.21, 1.40, 1.41, 1.42, 1.46, and 1.49 reprinted from U.S. National Library of Medicine.

Figures 1.2, 1.3, 1.4, 1.6, 1.9, 1.10, 1.13, 1.16, 1.17, 1.22 through 1.30, 1.32 through 1.39, 1.43, 1.44, 1.45, 1.47, 1.48 and 1.50 through 1.54 reprinted from Whitcomb, D., Immunology to 1980. University of Wisconsin, Center of Health Sciences Library, Madison, 1985.

Figure 1.8 courtesy of the Cruse collection; adapted from Hemmelweit, F., Collected Papers of Paul Ehrlich, Pergamon Press, Tarrytown, NY, 19561960.

Figure 1.55 reprinted with permission of Jerry Berndt.

Figure 1.56 compliments of Professor Dr. Rolf Zinkernagel, Institute of Pathology, University of Zurich.

Figure 2.4 adapted from Lachman, P.J., Keith, P.S., Rosen, F.S., and Walport, M.J., Clinical Aspects of Immunology, 5th ed., Vol. 1993, p. 203, Fig. 112. With permission.

Figures 2.4, 7.85, and 11.18 redrawn from Lachmann, P.J., Clinical Aspects of Immunology. Blackwell Scientific Publications, Cambridge, MA, 1993. Reprinted by permission of Blackwell Science, Inc.

Figures 2.5, 2.6, 2.9, 2.19, 2.52, 4.4, 4.14, 4.17, 7.80, 7.83, 9.24, 9.25, 9.26, 9.29, 9.30, 9.37, 10.4, 10.5, 10.6, 10.10, 10.19, 10.24, 10.26, 10.30, 10.35, 10.37, 10.39, 10.40, 19.8, 19.9, 19.10, 20.16, 20.19, 20.22, 21.4, 21.5, 21.6, 21.7, 22.25, 23.25, 23.29, 23.40, and 23.41 reprinted from Protein Data Bank. Abola, E.E., Bernstein, F.C., Bryant, S.H., Koetzle, T.F., and Weng, J., In: Crystallographic Database:

Information Content, Software Systems, Scientific Applications. Allen, F.H., Bergerhoff, G., and Wievers, R., Eds. Data Commission of the International Union of Crystallography, Bonn/Cambridge/Chester, 1987, pp. 107-132. Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F. Jr., Bride, M.D., Rogers, J.R., Kennard, O., Simanouchi, T., and Tasumi, M., The protein data bank: a computer-based archival file for macromolecular structures, Journal of Molecular Biology, 112:535-542, 1977. These images are part of the Swiss-3D Image Collection. Manuel C. Peitsch, Geneva Biomedical Research Institute, Glaxo Wellcome R&D, Geneva, Switzerland.

Figures 2.16, 2.39, 2.78, 2.85, 4.18, 4.19, 9.22, 9.23, 9.28, 9.38, and 9.39 redrawn from Barclay, A.N., Birkeland, M.L., Brown, M.H., Beyers, A.D., Davis, S.J., Somoza, C., and Williams, A.F., The Leucocyte Antigen Facts Book, Academic Press, Orlando, FL, 1993.

Figures 2.30, 2.31, 2.41, 2.50, 2.68, 2.69, 2.71, 2.75, 2.76, 2.84, 2.85, 2.90, 2.94, 2.95, 2.98, 2.99, 2.103, 9.7, and 21.33 through 21.47 compliments of Marsha L. Eigenbrodt, MD, MPH, formerly assistant professor, Department of Medicine, and Edwin H. Eigenbrodt, MD, formerly professor of pathology, University of Mississippi Medical Center.

Figure 2.33 reprinted from Deutsch, M. and Weinreb, A., Apparatus for high-precision repetitive sequential optical measurement of lifting cells, Cytometry 16:214-226, 1994. Adapted by permission of Wiley-Liss, Inc., a subsidiary of John Wiley & Sons, Inc., and Marder, O., et al., Effect of interleukin-1a, interleukin-1ß, and tumor necrosis factor-a on the intercellular fluorescein fluorescence polarization of human lung fibroblasts, Pathobiology 64(3):123-130.

Figure 2.44 redrawn from Ravetch, J.V. and Kinet, J.P., Fc receptors, Annual Review of Immunology 9:462, 1991.

Figures 2.79, 7.23, 7.25, 7.28, 12.2, 12.18, 12.22, 12.28 and 15.9 redrawn from Murray, P.R., Medical Microbiology, Mosby-Yearbook, St. Louis, MO, 1994.

Figure 2.86 redrawn from Tedder, T.F., Structure of the gene encoding the human B lymphocyte differentiation antigen CD20(B1), Journal of Immunology 142(7):2567, 1989.

Figures 3.2, 6.19, 21.20, and 22.5. Redrawn from Bellanti, J.A., Immunology II. W.B. Saunders Co., Philadelphia, PA, 1978.

Figure 24.04 ©1997 by Facts and Comparisons. Adapted with permission from Immunofacts: Vaccines and Immunologic Drugs. Facts and Comparisons, St. Louis, MO, a Wolters Kluwer Company, 1996.

Figure 4.12 reprinted from Janeway, C.A. Jr. and Travers, P., Immunobiology: The Immune System in Health and Disease. 3rd ed., pp. 4-5, 1997. Reprinted by permission of Routledge/Taylor & Francis Books, Inc.

Figure 4.22 reprinted with permission from Nature. Bjorkmam, P.J., Saper, M.A., Samraoui, B., Bennet, W.A.S., Strominger, J.L., and Wiley, D.C., Structure of the human class I histocompatibility antigen, HLA-A2, 329:506-512. ©1987 Macmillan Magazines, Ltd.

Figures 6.6, 6.9, and 27.50 redrawn from Paul, W.E., Fundamental Immunology, 3rd ed., Raven Press, New York, 1993.

Figure 7.1 redrawn from Hunkapiller, T. and Hood, L., Diversity of the immunoglobulin gene super-family, Advances in Immunology 44:1-62, 1989.

Figure 7.11 courtesy of Mike Clark, PhD, Division of Immunology, Cambridge University.

Figure 7.12 reprinted with permission from Nature. Harris, L.F., Larson, S.E., Hasel, K.W., Day, J., Greenwood, A., and McPherson, A., The three-dimensional structure of an intact monoclonal antibody for canine lymphoma, 360(6402):369-372. ©1992 Macmillan Magazines Ltd.

Figures 7.20, 7.22 through 7.25, 7.30 through 7.32, and 6.52 for immunoglobulins redrawn from Oppenheim, J., Rosenstreich, D.L., and Peter, M., Cellular Function Immunity and Inflammation, Elsevier Science, New York, 1984.

Figure 7.35 redrawn from Capra, J.D. and Edmundson, A.B., The antibody combining site, Scientific American 236:50-54, 1977. ©George V. Kelvin/ Scientific American.

Figure 7.43 courtesy of Dr. Leon Carayannopoulos, Department of Microbiology, University of Texas, Southwestern Medical School, Dallas.

Figure 7.48 adapted from Kang, C. and Kohler, H., Immunoregulation and Autoimmunity, Vol. 3, Cruse, J.M. and Lewis, R.E. Eds., 226 S Karger, Basel, Switzerland, 1986.

Figure 7.66 reprinted with permission from Ragha-van, M., et al., Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants,

Biochemistry 34:14,469-14,657. ©1995 American Chemical Society; and from Junghans, R.P., Finally, the Brambell receptor (FcRB), Immunologic Research 16:29-57.

Figure 7.67 reprinted with permission from Nature. Brambel, F.W.R., Hemmings, W.A., and Morris, I.G., A theoretical model of gamma globulin catabolism, 203:1352-1355. © 1987 Macmillan Magazines, Ltd.

Figure 7.68 reprinted from Brambell, F.W.R., The transmission of immunity from mother to young and the catabolism of immunoglobulins, The Lancet, ii:1087-1093, 1966.

Figure 7.74 adapted from Haber, E., Quertermous, T., Matsueda, G.R., and Runge, M.S., Innovative approaches to plasminogen activator therapy, Science 243:52-56. ©1989 American Association for the Advancement of Science.

Figure 7.84 redrawn from Conrad, D.H., Keegan, A.D., Kalli, K.R., Van Dusen, R., Rao, M., and Levine, A.D., Superinduction of low affinity IgE receptors on murine B lymphocytes by LPS and interleukin-4, Journal of Immunology 141:10911097, 1988.

Figures 8.7, 8.13, 8.16, 8.18, and 8.21 redrawn from Eisen, H., Immunology, Lippincott-Raven Publishers, New York, pp. 371, 373, 385-386, 1974.

Figures 8.23 and 8.24 reprinted from Kabat, E.A.,

Structural Concepts in Immunology and Immu-nochemistry, Holt, Rinehart & Winston, New York, 1968.

Figure 9.2 reprinted from Atlas of Tumor Pathology, 2nd Series, Fascicle 13, Armed Forces Institute of Pathology.

Figures 9.3 and 9.8 reprinted from Atlas of Tumor Pathology, 3rd Series, Fascicle 21, Armed Forces Institute of Pathology.

Figures 9.4, 9.5, and 9.6 reprinted from Muller-Hermelink, H.K., Marina, M., and Palestra, G., Pathology of thymic epithelial tumors. In: The Human Thymus. Current Topics in Pathology. Muller-Hermelink, H.K., Ed. 1986; 75:207268.

Figure 9.10 reprinted from van Wijingaert, F.P., Kendall, M.D., Schuurmann, H.J., Rademakers, L.H., Kater, L., Heterogeneity of epithelial cells in the human thymus. An ultrastructural study, Cell and Tissue Research 227-237, 1984.

Figure 9.13 reprinted from Lo, D., Reilly, C.R., DeKoning, J., Laufer, T.M., and Glimcher, L.H., Thymic stromal cell specialization of the T cell receptor repertoire, Immunologic Research 16(1):3-14, 1997.

Figure 9.27 adapted from Werner, K. and Ferrara, J., Immunologic Research 15(1), 1996, p.52.

Figures 9.33 and 17.90 redrawn from Davis, M.M., T cell receptor gene diversity and selection, Annual Review of Biochemistry 59:477, 1990.

Figure 10.28 redrawn from Ealick, S.E., Cook, W.J., and Vijay-Kumar, S., Three-dimensional structure of recombinant human interferon-y, Science 252:698-702. ©1991 American Association for the Advancement of Science.

Figure 10.39 adapted from Rifkin, D.B. et al., Thrombosis and Haemostasis 1993:70, 177-179.

Figure 11.4 redrawn from Arlaud, G.J., Colomb, M.G., and Gagnon, J., A functional model of the human C1 complex. Immunology Today 8:107-109, 1987.

Figures 11.9 and 11.11 redrawn from Podack, E.R., Molecular mechanisms of cytolysis by complement and cytolytic lymphocytes, Journal of Cellular Biochemistry 30:133-70, 1986.

Figure 11.12 redrawn from Rooney, I.A., Oglesby, T.J., and Atkinson, J.P., Complement in human reproduction: activation and control, Immuno-logic Research 12(3): 276-294, 1993.

Figure 11.19 redrawn from Kinoshita, T., Complement Today. Cruse, J.M. and Lewis, R.E., Eds., 48 S. Karger, Basel Switzerland, 1993.

Figure 12.26 reprinted from Shwartzman, G. Phenomenon of Local Tissue Reactivity and Its Immunological, Pathological, and Clinical Significance, Paul B. Hoeber, Publisher (LippincottRaven Publishers), New York, 1937, p. 275.

Figures 14.2, 14.3, and 14.6 through 14.53 are furnished courtesy of INOVA Corp. and Ms. Carol Peebles, San Diego, CA.

Figures 16.5 and 16.22 adapted from Vengelen-Tyler, V., Ed., Technical Manual, 12th ed., American Association of Blood Banks, Bethesda, MD, 1996, pp. 231, 282.

Figures 16.12, 16.24 and 16.26 reprinted from Daniels, G., Human Blood Groups, Blackwell Science Ltd., Oxford, UK, pp.13, 271, 432, 1995.

Figures 16.33 and 16.11 adapted from Walker, R.H., Ed., Technical Manual, 11th ed., American Association of Blood Banks, Bethesda, MD, 1993, pp 242, 281.

Figures 17.8 and 17.69 redrawn from Cotran, R.S., Kumar, V., and Robbins, S.L., Robbins Pathologic Basis of Disease, B. Saunders Co., Philadelphia, PA, 1989.

Figures 17.23 and 17.87 reprinted from Valenzuela, R., Bergfeld, W.F., and Deodhar, S.D., Immuno-fluorescent Patterns in Skin Diseases, American Society of Clinical Pathologists Press, Chicago, IL, 1984. With permission of the ASCP Press.

Figures 17.27 and 17.28 adapted from Edmundson, A.B., Ely, K.R., Abola, E.E., Schiffer, M., and Panagotopoulos, N., Rotational allomerism and divergent evolution of domains in immunoglobulin light chains, Biochemistry 14:3953-3961. ©1975 American Chemical Society.

Figure 16.33 reprinted from Clemetson, K.J., Glycoproteins of the platelet plasma membrane, in Platelet Membrane Glycoproteins, George, J.N., Norden, A.T., and Philips, D.R., Eds., Plenum Press, New York, 1985, pp. 61-86, with permission.

Figure 17.46 redrawn from Stites, D.P., Basic and Clinical Immunology, Appleton & Lange, East Norwalk, CT, 1991.

Figure 17.112 redrawn from Dieppe, P.A., Bacon, P.A., Bamji, A.N., and Watt, I., Atlas of Clinical Rheumatology, Lea & Febiger, Philadelphia, PA, 1986.

Figure 21.17 adapted from Splits, Associated Antigens and Inclusions, PEL-FREEZE Clinical Systems, Brown Deer, WI, 1992.

Figures 21.48 through 21.62 compliments of Howard M. Shulman, MD, professor of pathology, University of Washington, Member Fred Hutchinson Cancer Research Center, Seattle.

Figures 22.1 through 22.3 reprinted from Monoclonal Antiadhesion Molecules, Nov. 8, 1994. Seikagaku Corp.

Figure 23.17 reproduced from Journal of Cell Biology. Tilney, L.G. and Portnoy, D.A., Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes, 1989, 109:1597-1608, with permission of the Rockefeller University Press.

Figure 22.23 adapted from Immunoscintigraphy (nude mouse) with a 131I-labelled monoclonal antibody, photographs prepared by Hachmann, H. and Steinstraesser, A., Radiochemical Laboratory, Hrechst, Frankfort, Germany. With permission.

Figures 22.31 and 23.32 reprinted from Seifer, M. and Standring, D.N., Assembly and antigenicity of hepatitis B virus core particles, Intervirology 38:47-62, 1995.

Figure 23.36 courtesy of Farr-Jones, S., University of California at San Francisco.

Figures 27.3 and 27.4 redrawn from Hudson, L. and Hay, F.C., Practical Immunology, Blackwell Scientific Publications, Cambridge, MA, 1989.

Figure 27.10 redrawn from Miller, L.E., Manual of Laboratory Immunology, Lea & Febiger, Mal-vern, PA, 1991.

Figure 27.19 redrawn from Elek, S.D., Staphylo-ccocus Pyogenes and its Relation to Disease, E&S Livingstone Ltd., Edinburgh and London, 1959.

Figures 28.1 through 28.33 are furnished courtesy of Cell Marque Corp. and Dr. Michael Lacey, Hot Springs, AR.

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