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rote the paper: DN AD. 9 Structural Studies of a Bacterial a2-Macroglobulin References 1. 2. 3. Armstrong PB Proteases and protease inhibitors: a balance of activities in hostpathogen interaction. Immunobiology 211: 263281. Sottrup-Jensen L Alpha macroglobulins: structure, shape, and mechanism of proteinase complex formation. J Biol Chem 264: 1153911542. Kolodziej SJ, Wagenknecht T, Strickland DK, Stoops JK The threedimensional structure of the human a2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin a 2macroglobulin complexes. J Biol Chem 277: 2803128037. Qazi U, Kolodziej SJ, Gettins PGW, Stoops JK The structure of the C949S mutant human a2-macroglobulin demonstrates the critical role of the internal thiol esters in its proteinase-entrapping structural transformation. J Struct Biol 131: 1926. Boisset N, Taveau J-C, Ponchon F, Lamy J Similar architectures of native and transformed human a2-macroglobulin suggest the transformation mechanism. J Biol Chem 271: 2576225769. Arakawa H, Nishigai M, Ikai A a2-macroglobulin traps a proteinase in the midregion of its arms. J Biol Chem 264: 23502356. Delain E, Barray M, Trapon-Bretaudiere J, Ponchon F, Maryen P, et al. The molecular organization of human a2-macroglobulin. J Biol Chem 263: 29812989. Delain E, Pochon F, Barray M, van Leuven F Ultrastructure of alpha 2macroglobulins. Electron Microsc “7834183 Rev 5: 231281. purchase PP-242 Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J Crystal structure of the receptor-binding domain of a2-macroglobulin. Structure 6: 595604. Boisset N, Penczek P, Ponchon F, Frank J, Lamy J Three-dimensional architecture of human a2-macroglobulin transformed with methylamine. J Mol Biol 232: 522529. Osterberg R, Malmensten B Methylamine-induced conformational change of a2-macroglobulin and its zinc binding capacity. Eur J Biochem 143: 541544. Branegard B, Osterberg R, Sjoberg B Small-angle X-ray scattering study of the interaction between human a2-macroglobulin and trypsin. Eur J Biochem 122: 663666. Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, et al. The crystal structure of human a2-macroglobulin reveals a unique molecular cage. Angew Chem Int Ed Engl e-print. Gros P, Milder FJ, Janssen BJC Complement driven by conformational changes. Nat Rev Immunol 8: 4858. Sahu A, Lambris JD Structure and biology of complement protein C3, a connecting link between innate and acquired immunity. Immun Rev 180: 3548. Kirkitadze MD, Barlow PN Structure and flexibility of the multiple domain proteins that regulate complement activation. Immun Rev 180: 146161. Janssen BJ, Huizinga EG, Raaijmakers HC, Roos A, Daha MR, et al. Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437: 505511. Freslund F, Jenner L, Husted LB, Nyborg J, Andersen GR, et al. The structure of bovine complement component 3 reveals the basis for thioester function. J Mol Biol 361: 115127. Alcorlo M, Martinez-Barricarte R, Fernandez FJ, Rodriguez-Gallego C, Round A, et al. ” Unique structure of iC3b resolved at a resolution of 24 A by 3D-electron microscopy. Proc Natl Acad Sci USA 108: 1323613240. Janssen BJC, Christodoulidou A, McCarthy A, Lambris JD, Gros P Structure of C3b reveals conformational changes that underlie complement activity. Nature 444: 213216. Nishida N, Walz T, Springer TA Structural transitions of complement component C3 and its activation products. Proc Natl Acad Sci USA 103: 1973719742. 22. Wiesm

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