Rolink, A.G. & Melchers, F. BAFFled B cells survive and thrive: roles of BAFF in B-cell development. Curr. Opin. Immunol. 14, 266–275 (2002).
Mackay, F. & Mackay, C.R. The role of BAFF in B-cell maturation, T-cell activation and autoimmunity. Trends Immunol. 23, 113–115 (2002).
Do, R.K. & Chen-Kiang, S. Mechanism of BLyS action in B cell immunity. Cytokine Growth Factor Rev. 13, 19–25 (2002).
Tribouley, C. et al. Characterization of a new member of the TNF family expressed on antigen-presenting cells. Biol. Chem. 380, 1443–1447 (1999).
Shu, H.B., Hu, W.H. & Johnson, H. TALL-1 is a novel member of the TNF family that is down-regulated by mitogens. J. Leukoc. Biol. 65, 680–683 (1999).
Mukhopadhyay, A., Ni, J., Zhai, Y., Yu, G.L. & Aggarwal, B.B. Identification and characterization of a novel cytokine, THANK, a TNF homologue that activates apoptosis, nuclear factor-κB, and c-Jun NH2-terminal kinase. J. Biol. Chem. 274, 15978–15981 (1999).
Hu, S., Tamada, K., Ni, J., Vincenz, C. & Chen, L. Characterization of TNFRSF19, a novel member of the tumor necrosis factor receptor superfamily. Genomics 62, 103–107 (1999).
Moore, P.A. et al. BLyS: member of the tumor necrosis factor family and B lymphocyte stimulator. Science 285, 260–263 (1999).
Schneider, P. et al. BAFF, a novel ligand of the tumor necrosis factor family, stimulates B cell growth. J. Exp. Med. 189, 1747–1756 (1999).
Gross, J.A. et al. TACI-Ig neutralizes molecules critical for B cell development and autoimmune disease. Impaired B cell maturation in mice lacking BLyS. Immunity 15, 289–302 (2001).
Schiemann, B. et al. An essential role for BAFF in the normal development of B cells through a BCMA-independent pathway. Science 293, 2111–2114 (2001).
Khare, S.D. et al. Severe B cell hyperplasia and autoimmune disease in TALL-1 transgenic mice. Proc. Natl. Acad. Sci. USA 97, 3370–3375 (2000).
Mackay, F. et al. Mice transgenic for BAFF develop lymphocytic disorders along with autoimmune manifestations. J. Exp. Med. 190, 1697–1710 (1999).
Groom, J. et al. Association of BAFF/BLyS overexpression and altered B cell differentiation with Sjogren's syndrome. J. Clin. Invest. 109, 59–68 (2002).
Gross, J.A. et al. TACI and BCMA are receptors for a TNF homologue implicated in B-cell autoimmune disease. Nature 404, 995–999 (2000).
Zhang, J. et al. Cutting edge: a role for B lymphocyte stimulator in systemic lupus erythematosus. J. Immunol. 166, 6–10 (2001).
Cheema, G.S., Roschke, V., Hilbert, D.M. & Stohl, W. Elevated serum B lymphocyte stimulator levels in patients with systemic immune-based rheumatic diseases. Arthritis Rheum. 44, 1313–1319 (2001).
Yan, M. et al. Identification of a receptor for BLyS demonstrates a crucial role in humoral immunity. Nat. Immunol. 1, 37–41 (2000).
Xia, X.Z. et al. TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation. J. Exp. Med. 192, 137–143 (2000).
Wang, H. et al. TACI-ligand interactions are required for T cell activation and collagen-induced arthritis in mice. Nat. Immunol. 2, 632–637 (2001).
Karpusas, M. et al. Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes. J. Mol. Biol. 315, 1145–1154 (2002).
Oren, D.A. et al. Structural basis of BLyS receptor recognition. Nat. Struct. Biol. 9, 288–292 (2002).
Liu, Y. et al. Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands. Cell 108, 383–394 (2002).
Yan, M. et al. Identification of a novel receptor for B lymphocyte stimulator that is mutated in a mouse strain with severe B cell deficiency. Curr. Biol. 11, 1547–1552 (2001).
Thompson, J.S. et al. BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF. Science 293, 2108–2111 (2001).
Thompson, J.S. et al. BAFF binds to the tumor necrosis factor receptor-like molecule B cell maturation antigen and is important for maintaining the peripheral B cell population. J. Exp. Med. 192, 129–135 (2000).
Marsters, S.A. et al. Interaction of the TNF homologues BLyS and APRIL with the TNF receptor homologues BCMA and TACI. Curr. Biol. 10, 785–788 (2000).
Seshasayee, D. et al. Loss of TACI causes fatal lymphoproliferation and autoimmunity, establishing TACI as an inhibitory BLyS receptor. Immunity 18, 279–288 (2003).
von Bulow, G.U., van Deursen, J.M. & Bram, R.J. Regulation of the T-independent humoral response by TACI. Immunity 14, 573–582 (2001).
Yan, M. et al. Activation and accumulation of B cells in TACI-deficient mice. Nat. Immunol. 2, 638–643 (2001).
Locksley, R.M., Killeen, N. & Lenardo, M.J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487–501 (2001).
Bodmer, J.L., Schneider, P. & Tschopp, J. The molecular architecture of the TNF superfamily. Trends Biochem. Sci. 27, 19–26 (2002).
Naismith, J.H., Devine, T.Q., Kohno, T. & Sprang, S.R. Structures of the extracellular domain of the type I tumor necrosis factor receptor. Structure 4, 1251–1262 (1996).
Naismith, J.H. & Sprang, S.R. Modularity in the TNF-receptor family. Trends Biochem. Sci. 23, 74–79 (1998).
Mongkolsapaya, J. et al. Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. Nat. Struct. Biol. 6, 1048–1053 (1999).
Hymowitz, S.G. et al. Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. Mol. Cell 4, 563–571 (1999).
Banner, D.W. et al. Crystal structure of the soluble human 55 kD TNF receptor-human TNF β-complex: implications for TNF receptor activation. Cell 73, 431–445 (1993).
Kayagaki, N. et al. BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-κB2. Immunity 17, 515–524 (2002).
Madry, C. et al. The characterization of murine BCMA gene defines it as a new member of the tumor necrosis factor receptor superfamily. Int. Immunol. 10, 1693–1702 (1998).
Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997).
Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. A 54, 905–921 (1998).
Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta. Crystallogr. A 47, 110–119 (1991).
Vriend, G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52–56 (1990).