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Volumn 44, Issue 5, 2007, Pages 763-773

Mutagenesis, biochemical, and biophysical characterization of Mycoplasma arthritidis-derived mitogen

Author keywords

Analytical ultracentrifugation; CD; Cross linking; Dimerization; MAM; Sedimentation; Superantigen

Indexed keywords

ASPARTIC ACID; CASPASE 3; MITOGENIC AGENT; PENTAPEPTIDE;

EID: 33748919979     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.04.010     Document Type: Article
Times cited : (5)

References (53)
  • 1
    • 0026504297 scopus 로고
    • Selective expansion of T cells expressing T-cell receptor variable regions V beta 2 and V beta 8 in Kawasaki disease
    • Abe J., Kotzin B.L., Jujo K., Melish M.E., Glode M.P., Kohsaka T., and Leung D.Y. Selective expansion of T cells expressing T-cell receptor variable regions V beta 2 and V beta 8 in Kawasaki disease. Proc Natl Acad Sci USA 89 (1992) 4066-4070
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4066-4070
    • Abe, J.1    Kotzin, B.L.2    Jujo, K.3    Melish, M.E.4    Glode, M.P.5    Kohsaka, T.6    Leung, D.Y.7
  • 2
    • 0028766126 scopus 로고
    • Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1
    • Acharya K.R., Passalacqua E.F., Jones E.Y., Harlos K., Stuart D.I., Brehm R.D., and Tranter H.S. Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. Nature 367 (1994) 94-97
    • (1994) Nature , vol.367 , pp. 94-97
    • Acharya, K.R.1    Passalacqua, E.F.2    Jones, E.Y.3    Harlos, K.4    Stuart, D.I.5    Brehm, R.D.6    Tranter, H.S.7
  • 3
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler A.J., Greenfield N.J., and Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol 27 (1973) 675-735
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 5
    • 0037200073 scopus 로고    scopus 로고
    • The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome
    • Arcus V.L., Langley R., Proft T., Fraser J.D., and Baker E.N. The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome. J Biol Chem 277 (2002) 32274-32281
    • (2002) J Biol Chem , vol.277 , pp. 32274-32281
    • Arcus, V.L.1    Langley, R.2    Proft, T.3    Fraser, J.D.4    Baker, E.N.5
  • 6
    • 0034716945 scopus 로고    scopus 로고
    • Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes
    • Arcus V.L., Proft T., Sigrell J.A., Baker H.M., Fraser J.D., and Baker E.N. Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes. J Mol Biol 299 (2000) 157-168
    • (2000) J Mol Biol , vol.299 , pp. 157-168
    • Arcus, V.L.1    Proft, T.2    Sigrell, J.A.3    Baker, H.M.4    Fraser, J.D.5    Baker, E.N.6
  • 7
    • 4644303172 scopus 로고    scopus 로고
    • Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization
    • Baker H.M., Proft T., Webb P.D., Arcus V.L., Fraser J.D., and Baker E.N. Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization. J Biol Chem 279 (2004) 38571-38576
    • (2004) J Biol Chem , vol.279 , pp. 38571-38576
    • Baker, H.M.1    Proft, T.2    Webb, P.D.3    Arcus, V.L.4    Fraser, J.D.5    Baker, E.N.6
  • 8
    • 4344567024 scopus 로고    scopus 로고
    • Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1)
    • Baker M.D., Gendlina I., Collins C.M., and Acharya K.R. Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1). Protein Sci 13 (2004) 2285-2290
    • (2004) Protein Sci , vol.13 , pp. 2285-2290
    • Baker, M.D.1    Gendlina, I.2    Collins, C.M.3    Acharya, K.R.4
  • 9
    • 0030977285 scopus 로고    scopus 로고
    • Functional analysis of Mycoplasma arthritidis-derived mitogen interactions with class II molecules
    • Bernatchez C., Al-Daccak R., Mayer P.E., Mehindate K., Rink L., Mecheri S., and Mourad W. Functional analysis of Mycoplasma arthritidis-derived mitogen interactions with class II molecules. Infect Immun 65 (1997) 2000-2005
    • (1997) Infect Immun , vol.65 , pp. 2000-2005
    • Bernatchez, C.1    Al-Daccak, R.2    Mayer, P.E.3    Mehindate, K.4    Rink, L.5    Mecheri, S.6    Mourad, W.7
  • 10
    • 0032563116 scopus 로고    scopus 로고
    • Structural and energetic factors of the increased thermal stability in a genetically engineered Escherichia coli adenylate kinase
    • Burlacu-Miron S., Perrier V., Gilles A.M., Pistotnik E., and Craescu C.T. Structural and energetic factors of the increased thermal stability in a genetically engineered Escherichia coli adenylate kinase. J Biol Chem 273 (1998) 19102-19107
    • (1998) J Biol Chem , vol.273 , pp. 19102-19107
    • Burlacu-Miron, S.1    Perrier, V.2    Gilles, A.M.3    Pistotnik, E.4    Craescu, C.T.5
  • 11
    • 0034695588 scopus 로고    scopus 로고
    • The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function
    • Cavallin A., Arozenius H., Kristensson K., Antonsson P., Otzen D.E., Bjork P., and Forsberg G. The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. J Biol Chem 275 (2000) 1665-1672
    • (2000) J Biol Chem , vol.275 , pp. 1665-1672
    • Cavallin, A.1    Arozenius, H.2    Kristensson, K.3    Antonsson, P.4    Otzen, D.E.5    Bjork, P.6    Forsberg, G.7
  • 12
    • 1842668061 scopus 로고    scopus 로고
    • Spectrophotometric methods for the determination of superantigen structure and stability
    • Cavallin A., Petersson K., and Forsberg G. Spectrophotometric methods for the determination of superantigen structure and stability. Methods Mol Biol 214 (2003) 55-63
    • (2003) Methods Mol Biol , vol.214 , pp. 55-63
    • Cavallin, A.1    Petersson, K.2    Forsberg, G.3
  • 13
    • 0029991018 scopus 로고    scopus 로고
    • The sequence of the Mycoplasma arthritidis superantigen, MAM: identification of functional domains and comparison with microbial superantigens and plant lectin mitogens
    • Cole B.C., Knudtson K.L., Oliphant A., Sawitzke A.D., Pole A., Manohar M., Benson L.S., Ahmed E., and Atkin C.L. The sequence of the Mycoplasma arthritidis superantigen, MAM: identification of functional domains and comparison with microbial superantigens and plant lectin mitogens. J Exp Med 183 (1996) 1105-1110
    • (1996) J Exp Med , vol.183 , pp. 1105-1110
    • Cole, B.C.1    Knudtson, K.L.2    Oliphant, A.3    Sawitzke, A.D.4    Pole, A.5    Manohar, M.6    Benson, L.S.7    Ahmed, E.8    Atkin, C.L.9
  • 15
    • 0347382594 scopus 로고    scopus 로고
    • Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)
    • Dam J., Guan R., Natarajan K., Dimasi N., Chlewicki L.K., Kranz D.M., Schuck P., Margulies D.H., and Mariuzza R.A. Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b). Nat Immunol 4 (2003) 1213-1222
    • (2003) Nat Immunol , vol.4 , pp. 1213-1222
    • Dam, J.1    Guan, R.2    Natarajan, K.3    Dimasi, N.4    Chlewicki, L.K.5    Kranz, D.M.6    Schuck, P.7    Margulies, D.H.8    Mariuzza, R.A.9
  • 16
    • 1642493665 scopus 로고    scopus 로고
    • Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold
    • Donadini R., Liew C.W., Kwan A.H., Mackay J.P., and Fields B.A. Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold. Structure (Camb) 12 (2004) 145-156
    • (2004) Structure (Camb) , vol.12 , pp. 145-156
    • Donadini, R.1    Liew, C.W.2    Kwan, A.H.3    Mackay, J.P.4    Fields, B.A.5
  • 17
    • 0028831120 scopus 로고
    • Divergent effects of zinc on different bacterial pathogenic agents
    • Driessen C., Hirv K., Kirchner H., and Rink L. Divergent effects of zinc on different bacterial pathogenic agents. J Infect Dis 171 (1995) 486-489
    • (1995) J Infect Dis , vol.171 , pp. 486-489
    • Driessen, C.1    Hirv, K.2    Kirchner, H.3    Rink, L.4
  • 18
    • 0036150022 scopus 로고    scopus 로고
    • Involvement of zinc in the binding of mycoplasma arthritidis-derived mitogen to the proximity of the HLA-DR binding groove regardless of histidine 81 of the beta chain
    • Etongue-Mayer P., Langlois M.A., Ouellette M., Li H., Younes S., Al-Daccak R., and Mourad W. Involvement of zinc in the binding of mycoplasma arthritidis-derived mitogen to the proximity of the HLA-DR binding groove regardless of histidine 81 of the beta chain. Eur J Immunol 32 (2002) 50-58
    • (2002) Eur J Immunol , vol.32 , pp. 50-58
    • Etongue-Mayer, P.1    Langlois, M.A.2    Ouellette, M.3    Li, H.4    Younes, S.5    Al-Daccak, R.6    Mourad, W.7
  • 19
    • 0032403177 scopus 로고    scopus 로고
    • Antigen-specific T-cell receptor V beta expression in Porphyromonas gingivalis-specific T-cell lines
    • Gemmell E., Grieco D.A., Cullinan M.P., Westerman B., and Seymour G.J. Antigen-specific T-cell receptor V beta expression in Porphyromonas gingivalis-specific T-cell lines. Oral Microbiol Immunol 13 (1998) 355-361
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 355-361
    • Gemmell, E.1    Grieco, D.A.2    Cullinan, M.P.3    Westerman, B.4    Seymour, G.J.5
  • 20
    • 3843067734 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal peptidogly can-binding domain of human peptidoglycan recognition protein Ialpha
    • Guan R., Malchiodi E.L., Wang Q., Schuck P., and Mariuzza R.A. Crystal structure of the C-terminal peptidogly can-binding domain of human peptidoglycan recognition protein Ialpha. J Biol Chem 279 (2004) 31873-31882
    • (2004) J Biol Chem , vol.279 , pp. 31873-31882
    • Guan, R.1    Malchiodi, E.L.2    Wang, Q.3    Schuck, P.4    Mariuzza, R.A.5
  • 21
    • 0034703273 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules
    • Hakansson M., Petersson K., Nilsson H., Forsberg G., Bjork P., Antonsson P., and Svensson L.A. The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules. J Mol Biol 302 (2000) 527-537
    • (2000) J Mol Biol , vol.302 , pp. 527-537
    • Hakansson, M.1    Petersson, K.2    Nilsson, H.3    Forsberg, G.4    Bjork, P.5    Antonsson, P.6    Svensson, L.A.7
  • 22
    • 0029147099 scopus 로고
    • Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II
    • Hudson K.R., Tiedemann R.E., Urban R.G., Lowe S.C., Strominger J.L., and Fraser J.D. Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II. J Exp Med 182 (1995) 711-720
    • (1995) J Exp Med , vol.182 , pp. 711-720
    • Hudson, K.R.1    Tiedemann, R.E.2    Urban, R.G.3    Lowe, S.C.4    Strominger, J.L.5    Fraser, J.D.6
  • 23
    • 0030460727 scopus 로고    scopus 로고
    • 2+ ion. Proposal of a novel catalytic role for Glu48
    • 2+ ion. Proposal of a novel catalytic role for Glu48. J Biol Chem 271 (1996) 32729-32736
    • (1996) J Biol Chem , vol.271 , pp. 32729-32736
    • Kanaya, S.1    Oobatake, M.2    Liu, Y.3
  • 24
    • 0037480943 scopus 로고    scopus 로고
    • Molecular genetics, structure, and immunobiology of streptococcal pyrogenic exotoxins A and C
    • Leung D.Y.M., Huber B.T., and Schlievert P.M. (Eds)
    • Kim M.H., and Schlievert P. Molecular genetics, structure, and immunobiology of streptococcal pyrogenic exotoxins A and C. In: Leung D.Y.M., Huber B.T., and Schlievert P.M. (Eds). Superantigens: Molecular Biology, Immunology, and Relevance to Human Disease (1997) 257-280
    • (1997) Superantigens: Molecular Biology, Immunology, and Relevance to Human Disease , pp. 257-280
    • Kim, M.H.1    Schlievert, P.2
  • 25
    • 0030729213 scopus 로고    scopus 로고
    • Expression of the superantigen Mycoplasma arthritidis mitogen in Escherichia coli and characterization of the recombinant protein
    • Knudtson K.L., Manohar M., Joyner D.E., Ahmed E.A., and Cole B.C. Expression of the superantigen Mycoplasma arthritidis mitogen in Escherichia coli and characterization of the recombinant protein. Infect Immun 65 (1997) 4965-4971
    • (1997) Infect Immun , vol.65 , pp. 4965-4971
    • Knudtson, K.L.1    Manohar, M.2    Joyner, D.E.3    Ahmed, E.A.4    Cole, B.C.5
  • 26
    • 0027370384 scopus 로고
    • Superantigens and their potential role in human disease
    • Kotzin B.L., Leung D.Y., Kappler J., and Marrack P. Superantigens and their potential role in human disease. Adv Immunol 54 (1993) 99-166
    • (1993) Adv Immunol , vol.54 , pp. 99-166
    • Kotzin, B.L.1    Leung, D.Y.2    Kappler, J.3    Marrack, P.4
  • 27
    • 0029153035 scopus 로고
    • Multiple binding sites for bacterial superantigens on soluble class II MHC molecules
    • Kozono H., Parker D., White J., Marrack P., and Kappler J. Multiple binding sites for bacterial superantigens on soluble class II MHC molecules. Immunity 3 (1995) 187-196
    • (1995) Immunity , vol.3 , pp. 187-196
    • Kozono, H.1    Parker, D.2    White, J.3    Marrack, P.4    Kappler, J.5
  • 28
    • 0037591186 scopus 로고    scopus 로고
    • Zinc-binding sites in the N terminus of Mycoplasma arthritidis-derived mitogen permit the dimer formation required for high affinity binding to HLA-DR and for T cell activation
    • Langlois M.A., El Fakhry Y., and Mourad W. Zinc-binding sites in the N terminus of Mycoplasma arthritidis-derived mitogen permit the dimer formation required for high affinity binding to HLA-DR and for T cell activation. J Biol Chem 278 (2003) 22309-22315
    • (2003) J Biol Chem , vol.278 , pp. 22309-22315
    • Langlois, M.A.1    El Fakhry, Y.2    Mourad, W.3
  • 29
    • 0343618440 scopus 로고    scopus 로고
    • Binding of Mycoplasma arthritidis-derived mitogen to human MHC class II molecules via its N terminus is modulated by invariant chain expression and its C terminus is required for T cell activation
    • Langlois M.A., Etongue-Mayer P., Ouellette M., and Mourad W. Binding of Mycoplasma arthritidis-derived mitogen to human MHC class II molecules via its N terminus is modulated by invariant chain expression and its C terminus is required for T cell activation. Eur J Immunol 30 (2000) 1748-1756
    • (2000) Eur J Immunol , vol.30 , pp. 1748-1756
    • Langlois, M.A.1    Etongue-Mayer, P.2    Ouellette, M.3    Mourad, W.4
  • 30
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz J., Lewis M.S., and Schuck P. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci 11 (2002) 2067
    • (2002) Protein Sci , vol.11 , pp. 2067
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 31
    • 0033008083 scopus 로고    scopus 로고
    • The structural basis of T cell activation by superantigens
    • Li H., Llera A., Malchiodi E.L., and Mariuzza R.A. The structural basis of T cell activation by superantigens. Annu Rev Immunol 17 (1999) 435-466
    • (1999) Annu Rev Immunol , vol.17 , pp. 435-466
    • Li, H.1    Llera, A.2    Malchiodi, E.L.3    Mariuzza, R.A.4
  • 32
    • 0030761504 scopus 로고    scopus 로고
    • The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action
    • Li P.L., Tiedemann R.E., Moffat S.L., and Fraser J.D. The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action. J Exp Med 186 (1997) 375-383
    • (1997) J Exp Med , vol.186 , pp. 375-383
    • Li, P.L.1    Tiedemann, R.E.2    Moffat, S.L.3    Fraser, J.D.4
  • 34
    • 0028784436 scopus 로고
    • Cross-linking of major histocompatibility complex class II molecules by staphylococcal enterotoxin A superantigen is a requirement for inflammatory cytokine gene expression
    • Mehindate K., Thibodeau J., Dohlsten M., Kalland T., Sekaly R.P., and Mourad W. Cross-linking of major histocompatibility complex class II molecules by staphylococcal enterotoxin A superantigen is a requirement for inflammatory cytokine gene expression. J Exp Med 182 (1995) 1573-1577
    • (1995) J Exp Med , vol.182 , pp. 1573-1577
    • Mehindate, K.1    Thibodeau, J.2    Dohlsten, M.3    Kalland, T.4    Sekaly, R.P.5    Mourad, W.6
  • 35
    • 0034541702 scopus 로고    scopus 로고
    • Structural evidence for the evolution of pyrogenic toxin superantigens
    • Mitchell D.T., Levitt D.G., Schlievert P.M., and Ohlendorf D.H. Structural evidence for the evolution of pyrogenic toxin superantigens. J Mol Evol 51 (2000) 520-531
    • (2000) J Mol Evol , vol.51 , pp. 520-531
    • Mitchell, D.T.1    Levitt, D.G.2    Schlievert, P.M.3    Ohlendorf, D.H.4
  • 36
    • 0029645282 scopus 로고
    • Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site
    • Papageorgiou A.C., Acharya K.R., Shapiro R., Passalacqua E.F., Brehm R.D., and Tranter H.S. Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure 3 (1995) 769-779
    • (1995) Structure , vol.3 , pp. 769-779
    • Papageorgiou, A.C.1    Acharya, K.R.2    Shapiro, R.3    Passalacqua, E.F.4    Brehm, R.D.5    Tranter, H.S.6
  • 38
    • 0033521685 scopus 로고    scopus 로고
    • Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeAl) by MHC class II molecules and T-cell receptors
    • Papageorgiou A.C., Collins C.M., Gutman D.M., Kline J.B., O'Brien S.M., Tranter H.S., and Acharya K.R. Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeAl) by MHC class II molecules and T-cell receptors. Embo J 18 (1999) 9-21
    • (1999) Embo J , vol.18 , pp. 9-21
    • Papageorgiou, A.C.1    Collins, C.M.2    Gutman, D.M.3    Kline, J.B.4    O'Brien, S.M.5    Tranter, H.S.6    Acharya, K.R.7
  • 39
    • 0035796399 scopus 로고    scopus 로고
    • Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
    • Petersson K., Hakansson M., Nilsson H., Forsberg G., Svensson L.A., Liljas A., and Walse B. Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence. Embo J 20 (2001) 3306-3312
    • (2001) Embo J , vol.20 , pp. 3306-3312
    • Petersson, K.1    Hakansson, M.2    Nilsson, H.3    Forsberg, G.4    Svensson, L.A.5    Liljas, A.6    Walse, B.7
  • 41
    • 0030299903 scopus 로고    scopus 로고
    • Superantigens in autoimmune diseases: still more shades of gray
    • Renno T., and Acha-Orbea H. Superantigens in autoimmune diseases: still more shades of gray. Immunol Rev 154 (1996) 175-191
    • (1996) Immunol Rev , vol.154 , pp. 175-191
    • Renno, T.1    Acha-Orbea, H.2
  • 42
    • 0030798632 scopus 로고    scopus 로고
    • Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules
    • Roussel A., Anderson B.F., Baker H.M., Fraser J.D., and Baker E.N. Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules. Nat Struct Biol 4 (1997) 635-643
    • (1997) Nat Struct Biol , vol.4 , pp. 635-643
    • Roussel, A.1    Anderson, B.F.2    Baker, H.M.3    Fraser, J.D.4    Baker, E.N.5
  • 43
    • 0033965823 scopus 로고    scopus 로고
    • Anti-MAM antibodies in rheumatic disease: evidence for a MAM-like superantigen in rheumatoid arthritis?
    • Sawitzke A., Joyner D., Knudtson K., Mu H.H., and Cole B. Anti-MAM antibodies in rheumatic disease: evidence for a MAM-like superantigen in rheumatoid arthritis?. J Rheumatol 27 (2000) 358-364
    • (2000) J Rheumatol , vol.27 , pp. 358-364
    • Sawitzke, A.1    Joyner, D.2    Knudtson, K.3    Mu, H.H.4    Cole, B.5
  • 44
    • 0031556023 scopus 로고    scopus 로고
    • A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity
    • Schad E.M., Papageorgiou A.C., Svensson L.A., and Acharya K.R. A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity. J Mol Biol 269 (1997) 270-280
    • (1997) J Mol Biol , vol.269 , pp. 270-280
    • Schad, E.M.1    Papageorgiou, A.C.2    Svensson, L.A.3    Acharya, K.R.4
  • 45
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems
    • Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., and Schubert D. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J 82 (2002) 1096-1111
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 46
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTENT, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTENT, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287 (2000) 252-260
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 47
    • 0032962084 scopus 로고    scopus 로고
    • Structural basis for HLA-DQ binding by the streptococcal superantigen SSA
    • Sundberg E., and Jardetzky T.S. Structural basis for HLA-DQ binding by the streptococcal superantigen SSA. Nat Struct Biol 6 (1999) 123-129
    • (1999) Nat Struct Biol , vol.6 , pp. 123-129
    • Sundberg, E.1    Jardetzky, T.S.2
  • 48
    • 0036467503 scopus 로고    scopus 로고
    • So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes
    • Sundberg E.J., Li Y., and Mariuzza R.A. So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes. Curr Opin Immunol 14 (2002) 36-44
    • (2002) Curr Opin Immunol , vol.14 , pp. 36-44
    • Sundberg, E.J.1    Li, Y.2    Mariuzza, R.A.3
  • 50
    • 0026437573 scopus 로고
    • Crystal structure of staphylococcal enterotoxin B, a superantigen
    • Swaminathan S., Furey W., Pletcher J., and Sax M. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature 359 (1992) 801-806
    • (1992) Nature , vol.359 , pp. 801-806
    • Swaminathan, S.1    Furey, W.2    Pletcher, J.3    Sax, M.4
  • 51
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica J., Dam J., Balbo A., Yikilmaz E., Mariuzza R.A., Rouault T.A., and Schuck P. Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal Biochem 326 (2004) 234-256
    • (2004) Anal Biochem , vol.326 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7
  • 52
    • 1242306188 scopus 로고    scopus 로고
    • Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex
    • Zhao Y., Li Z., Drozd S., Guo Y., Mourad W., and Li H. Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex. Structure 12 (2004) 277-288
    • (2004) Structure , vol.12 , pp. 277-288
    • Zhao, Y.1    Li, Z.2    Drozd, S.3    Guo, Y.4    Mourad, W.5    Li, H.6
  • 53
    • 4644304168 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of Mycoplasma arthritidis-derived mitogen complexed with peptide/MHC class II antigen
    • Zhao Y., Li Z., Drozd S., Guo Y., Stack R., Hauer C., and Li H. Crystallization and preliminary crystallographic analysis of Mycoplasma arthritidis-derived mitogen complexed with peptide/MHC class II antigen. Acta Crystallogr D Biol Crystallogr 60 (2004) 353-356
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 353-356
    • Zhao, Y.1    Li, Z.2    Drozd, S.3    Guo, Y.4    Stack, R.5    Hauer, C.6    Li, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.