Where to Start

Nossal, G. J. V. 1993. Life, death, and the immune system. Sci. Am. 269(3):53–62.

Tonegawa, S. 1985. The molecules of the immune system. Sci. Am. 253(4):122–131.

Leder, P. 1982. The genetics of antibody diversity. Sci. Am. 246(5):102–115.

Bromley, S. K., Burack, W. R., Johnson, K. G., Somersalo, K., Sims, T. N., Sumen, C., Davis, M. M., Shaw, A. S., Allen, P. M., and Dustin, M. L. 2001. The immunological synapse. Annu. Rev. Immunol. 19:375–396.

Owen, J. A., Punt, J., and Stranford, S. A. 2013. Kuby Immunology (7th ed.). W. H. Freeman and Company.

Abbas, A. K., Lichtman, A. H. H., and Pillai, S. 2014. Cellular and Molecular Immunology (8th ed.). Saunders.

Cold Spring Harbor Symposia on Quantitative Biology. 1989. Volume 54. Immunological Recognition. Cold Spring Harbor Laboratory Press.

Weir, D. M. (Ed.). 1996. Handbook of Experimental Immunology (5th ed.). Oxford University Press.

Murphy, K. 2011. Janeway’s Immunobiology (8th ed.). Garland Science.

Janeway, C. A., Jr., and Medzhitov, R. 2002. Innate immune recognition. Annu. Rev. Immunol. 20:197–216.

Khalturin, K., Panzer, Z., Cooper, M. D., and Bosch, T. C. 2004. Recognition strategies in the innate immune system of ancestral chordates. Mol. Immunol. 41:1077–1087.

Beutler, B., and Rietschel, E. T. 2003. Innate immune sensing and its roots: The story of endotoxin. Nat. Rev. Immunol. 3:169–176.

Xu, Y., Tao, X., Shen, B., Horng, T., Medzhitov, R., Manley, J. L., and Tong, L. 2000. Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 408:111–115.

Botos, I., Segal, D. M., and Davies, D. R. 2011. The structural biology of the Toll-like receptors. Structure 19:447–459.

Davies, D. R., Padlan, E. A., and Sheriff, S. 1990. Antibody-antigen complexes. Annu. Rev. Biochem. 59:439–473.

Poljak, R. J. 1991. Structure of antibodies and their complexes with antigens. Mol. Immunol. 28:1341–1345.

Davies, D. R., and Cohen, G. H. 1996. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. U.S.A. 93:7–12.

Marquart, M., Deisenhofer, J., Huber, R., and Palm, W. 1980. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution. J. Mol. Biol. 141:369–391.

Silverton, E. W., Navia, M. A., and Davies, D. R. 1977. Three-dimensional structure of an intact human immunoglobulin. Proc. Natl. Acad. Sci. U.S.A. 74:5140–5144.

Padlan, E. A., Silverton, E. W., Sheriff, S., Cohen, G. H., Smith, G. S., and Davies, D. R. 1989. Structure of an antibody-antigen complex: Crystal structure of the HyHEL-10 Fab lysozyme complex. Proc. Natl. Acad. Sci. U.S.A. 86:5938–5942.

Rini, J., Schultze-Gahmen, U., and Wilson, I. A. 1992. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255:959–965.

Fischmann, T. O., Bentley, G. A., Bhat, T. N., Boulot, G., Mariuzza, R. A., Phillips, S. E., Tello, D., and Poljak, R. J. 1991. Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-Å resolution. J. Biol. Chem. 266: 12915–12920.

Burton, D. R. 1990. Antibody: The flexible adaptor molecule. Trends Biochem. Sci. 15:64–69.

Saphire, E. O., Parren P. W., Pantophlet, R., Zwick, M. B., Morris, G. M., Rudd, P. M., Dwek, R. A., Stanfield, R. L., Burton, D. R., and Wilson, I. A. 2001. Crystal structure of a neutralizing human IgG against HIV-1: A template for vaccine design. Science 293:1155–1159.

Calarese, D. A., Scanlan, C. N., Zwick, M. B., Deechongkit, S., Mimura, Y., Kunert R., Zhu, P., Wormald, M. R., Stanfield, R. L., Roux, K. H., et al. 2003. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065–2071.

Tonegawa, S. 1988. Somatic generation of immune diversity. Biosci. Rep. 8:3–26.

Honjo, T., and Habu, S. 1985. Origin of immune diversity: Genetic variation and selection. Annu. Rev. Biochem. 54:803–830.

Gellert, M., and McBlane, J. F. 1995. Steps along the pathway of VDJ recombination. Philos. Trans. R. Soc. Lond. B Biol. Sci. 347:43–47.

Harris, R. S., Kong, Q., and Maizels, N. 1999. Somatic hypermutation and the three R’s: Repair, replication and recombination. Mutat. Res. 436:157–178.

Lewis, S. M., and Wu, G. E. 1997. The origins of V(D)J recombination. Cell 88:159–162.

Ramsden, D. A., van Gent, D. C., and Gellert, M. 1997. Specificity in V(D)J recombination: New lessons from biochemistry and genetics. Curr. Opin. Immunol. 9:114–120.

Roth, D. B., and Craig, N. L. 1998. VDJ recombination: A transposase goes to work. Cell 94:411–414.

Sadofsky, M. J. 2001. The RAG proteins in V(D)J recombination: More than just a nuclease. Nucleic Acids Res. 29:1399–1409.

Bjorkman, P. J., and Parham, P. 1990. Structure, function, and diversity of class I major histocompatibility complex molecules. Annu. Rev. Biochem. 59:253–288.

Goldberg, A. L., and Rock, K. L. 1992. Proteolysis, proteasomes, and antigen presentation. Nature 357:375–379.

Madden, D. R., Gorga, J. C., Strominger, J. L., and Wiley, D. C. 1992. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight binding to MHC. Cell 70:1035–1048.

Fremont, D. H., Matsumura, M., Stura, E. A., Peterson, P. A., and Wilson, I. A. 1992. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 257: 880–881.

Matsumura, M., Fremont, D. H., Peterson, P. A., and Wilson, I. A. 1992. Emerging principles for the recognition of peptide antigens by MHC class I. Science 257:927–934.

Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., and Wiley, D. C. 1993. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 364:33–39.

Saper, M. A., Bjorkman, P. J., and Wiley, D. C. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:277–319.

Madden, D. R., Gorga, J. C., Strominger, J. L., and Wiley, D. C. 1991. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353:321–325.

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Cresswell, P., Bangia, N., Dick, T., and Diedrich, G. 1999. The nature of the MHC class I peptide loading complex. Immunol. Rev. 172:21–28.

Madden, D. R., Garboczi, D. N., and Wiley, D. C. 1993. The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693–708.

Hennecke, J., and Wiley, D. C. 2001. T-cell receptor-MHC interactions up close. Cell 104:1–4.

Ding, Y. H., Smith, K. J., Garboczi, D. N., Utz, U., Biddison, W. E., and Wiley, D. C. 1998. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 8:403–411.

Reinherz, E. L., Tan, K., Tang, L., Kern, P., Liu, J., Xiong, Y., Hussey, R. E., Smolyar, A., Hare, B., Zhang, R., et al. 1999. The crystal structure of a T-cell receptor in complex with peptide and MHC class II. Science 286:1913–1921.

Davis, M. M., and Bjorkman, P. J. 1988. T-cell antigen receptor genes and T-cell recognition. Nature 334:395–402.

Cochran, J. R., Cameron, T. O., and Stern, L. J. 2000. The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers. Immunity 12:241–250.

Garcia, K. C., Teyton, L., and Wilson, I. A. 1999. Structural basis of T cell recognition. Annu. Rev. Immunol. 17:369–397.

Garcia, K. C., Degano, M., Stanfield, R. L., Brunmark, A., Jackson, M. R., Peterson, P. A., Teyton, L. A., and Wilson, I. A. 1996. An αβ T-cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. Science 274:209–219.

Garboczi, D. N., Ghosh, P., Utz, U., Fan, Q. R., Biddison, W. E., Wiley, D. C. 1996. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134–141.

Gaul, B. S., Harrison, M. L., Geahlen, R. L., Burton, R. A., and Post, C. B. 2000. Substrate recognition by the Lyn protein-tyrosine kinase: NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. J. Biol. Chem. 275:16174–16182.

Kern, P. S., Teng, M. K., Smolyar, A., Liu, J. H., Liu, J., Hussey, R. E., Spoerl, R., Chang, H. C., Reinherz, E. L., and Wang, J. H. 1998. Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8 αβ ectodomain fragment in complex with H-2Kb. Immunity 9:519–530.

Konig, R., Fleury, S., and Germain, R. N. 1996. The structural basis of CD4-MHC class II interactions: Coreceptor contributions to T cell receptor antigen recognition and oligomerization-dependent signal transduction. Curr. Top. Microbiol. Immunol. 205:19–46.

Davis, M. M., Boniface, J. J., Reich, Z., Lyons, D., Hampl, J., Arden, B., and Chien, Y. 1998. Ligand recognition by αβ T-cell receptors. Annu. Rev. Immunol. 16:523–544.

Janeway, C. J. 1992. The T cell receptor as a multicomponent signalling machine: CD4/CD8 coreceptors and CD45 in T cell activation. Annu. Rev. Immunol. 10:645–674.

Podack, E. R., and Kupfer, A. 1991. T-cell effector functions: Mechanisms for delivery of cytotoxicity and help. Annu. Rev. Cell Biol. 7:479–504.

Davis, M. M. 1990. T cell receptor gene diversity and selection. Annu. Rev. Biochem. 59:475–496.

Leahy, D. J., Axel, R., and Hendrickson, W. A. 1992. Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution. Cell 68:1145–1162.

Bots, M., and Medema, J. P. 2006. Granzymes at a glance. J. Cell. Sci. 119:5011–5014.

Lowin, B., Hahne, M., Mattmann, C., and Tschopp, J. 1994. Cytolytic T-cell cytotoxicity is mediated through perforin and Fas lytic pathways. Nature 370:650–652.

Rudolph, M. G., and Wilson, I. A. 2002. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14:52–65.

Fauci, A. S. 1988. The human immunodeficiency virus: Infectivity and mechanisms of pathogenesis. Science 239:617–622.

Gallo, R. C., and Montagnier, L. 1988. AIDS in 1988. Sci. Am. 259(4): 41–48.

Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J., and Hendrickson, W. A. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648–659.

Johnston, M. I. and Fauci, A. S. 2007. An HIV vaccine—evolving concepts. New Engl. J. Med. 356:2073–2081.

Burton, D. R., Desrosiers, R. C., Doms, R. W., Koff, W. C., Kwong, P. D., Moore, J. P., Nabel, G. J., Sodroski, J., Wilson, I. A., and Wyatt, R. T. 2004. HIV vaccine design and the neutralizing antibody problem. Nature Immunol. 5:233–236.

Ada, G. 2001. Vaccines and vaccination. New Engl. J. Med. 345: 1042–1053.

Behbehani, A. M. 1983. The smallpox story: Life and death of an old disease. Microbiol. Rev. 47:455–509.

Ada, G. L., and Nossal, G. 1987. The clonal selection theory. Sci. Am. 257(2):62–69.

Porter, R. R. 1973. Structural studies of immunoglobulins. Science 180:713–716.

Edelman, G. M. 1973. Antibody structure and molecular immunology. Science 180:830–840.

Kohler, G. 1986. Derivation and diversification of monoclonal antibodies. Science 233:1281–1286.

Milstein, C. 1986. From antibody structure to immunological diversification of immune response. Science 231:1261–1268.

Janeway, C. A., Jr. 1989. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symp. Quant. Biol. 54:1–13.

Jerne, N. K. 1971. Somatic generation of immune recognition. Eur. J. Immunol. 1:1–9.