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Volumn 52, Issue 3, 2012, Pages 176-181

Evolution of immunity: No development without risk

Author keywords

Cell receptors; Multichain; Protein intrinsic disorder; Signal transduction; Single chain receptors

Indexed keywords

CELL SURFACE RECEPTOR; IMMUNE RECOGNITION RECEPTOR; UNCLASSIFIED DRUG;

EID: 84864276631     PISSN: 0257277X     EISSN: 15590755     Source Type: Journal    
DOI: 10.1007/s12026-011-8256-4     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0026540751 scopus 로고
    • Multichain immune recognition receptors: Similarities in structure and signaling pathways
    • Keegan AD, Paul WE. Multichain immune recognition receptors: similarities in structure and signaling pathways. Immunol Today. 1992;13:63-8.
    • (1992) Immunol Today , vol.13 , pp. 63-68
    • Keegan, A.D.1    Paul, W.E.2
  • 2
    • 5644293225 scopus 로고    scopus 로고
    • Multichain immune recognition receptor signaling: Different players, same game?
    • Sigalov AB. Multichain immune recognition receptor signaling: different players, same game? Trends Immunol. 2004;25:583-9.
    • (2004) Trends Immunol , vol.25 , pp. 583-589
    • Sigalov, A.B.1
  • 3
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature. 1989;338:383-4.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 4
    • 0034596890 scopus 로고    scopus 로고
    • DAP10 and DAP12 form distinct, but functionally cooperative, receptor complexes in natural killer cells
    • Wu J, Cherwinski H, Spies T, Phillips JH, Lanier LL. DAP10 and DAP12 form distinct, but functionally cooperative, receptor complexes in natural killer cells. J Exp Med. 2000;192:1059-68.
    • (2000) J Exp Med , vol.192 , pp. 1059-1068
    • Wu, J.1    Cherwinski, H.2    Spies, T.3    Phillips, J.H.4    Lanier, L.L.5
  • 5
    • 1242307780 scopus 로고    scopus 로고
    • Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif
    • Sigalov A, Aivazian D, Stern L. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry. 2004;43:2049-61.
    • (2004) Biochemistry , vol.43 , pp. 2049-2061
    • Sigalov, A.1    Aivazian, D.2    Stern, L.3
  • 6
    • 33845925345 scopus 로고    scopus 로고
    • Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits
    • Sigalov AB, Aivazian DA, Uversky VN, Stern LJ. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry. 2006;45:15731-9.
    • (2006) Biochemistry , vol.45 , pp. 15731-15739
    • Sigalov, A.B.1    Aivazian, D.A.2    Uversky, V.N.3    Stern, L.J.4
  • 7
    • 79960371484 scopus 로고    scopus 로고
    • Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors
    • Sigalov AB, Uversky VN. Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors. Self Nonself. 2011;2:55-72.
    • (2011) Self Nonself , vol.2 , pp. 55-72
    • Sigalov, A.B.1    Uversky, V.N.2
  • 8
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem. 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 9
    • 70349311250 scopus 로고    scopus 로고
    • Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition
    • Sigalov AB, Hendricks GM. Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition. Biochem Biophys Res Commun. 2009;389:388-93.
    • (2009) Biochem Biophys Res Commun , vol.389 , pp. 388-393
    • Sigalov, A.B.1    Hendricks, G.M.2
  • 10
    • 57449091330 scopus 로고    scopus 로고
    • The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition
    • Sigalov AB, Kim WM, Saline M, Stern LJ. The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition. Biochemistry. 2008;47: 12942-4.
    • (2008) Biochemistry , vol.47 , pp. 12942-12944
    • Sigalov, A.B.1    Kim, W.M.2    Saline, M.3    Stern, L.J.4
  • 11
    • 33947254923 scopus 로고    scopus 로고
    • Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form
    • Sigalov AB, Zhuravleva AV, Orekhov VY. Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie. 2007;89: 419-21.
    • (2007) Biochimie , vol.89 , pp. 419-421
    • Sigalov, A.B.1    Zhuravleva, A.V.2    Orekhov, V.Y.3
  • 12
    • 77956288834 scopus 로고    scopus 로고
    • The SCHOOL of nature. I. Transmembrane signaling
    • Sigalov AB. The SCHOOL of nature. I. Transmembrane signaling. Self Nonself. 2010;1:4-39.
    • (2010) Self Nonself , vol.1 , pp. 4-39
    • Sigalov, A.B.1
  • 13
    • 77953588437 scopus 로고    scopus 로고
    • New therapeutic strategies targeting transmembrane signal transduction in the immune system
    • Sigalov AB. New therapeutic strategies targeting transmembrane signal transduction in the immune system. Cell Adh Migr. 2010; 4:255-67.
    • (2010) Cell Adh Migr , vol.4 , pp. 255-267
    • Sigalov, A.B.1
  • 14
    • 80053110777 scopus 로고    scopus 로고
    • Cells diversify transmembrane signaling through the controlled chaos of protein disorder
    • Sigalov AB. Cells diversify transmembrane signaling through the controlled chaos of protein disorder. Self Nonself. 2011;2:75-9.
    • (2011) Self Nonself , vol.2 , pp. 75-79
    • Sigalov, A.B.1
  • 15
    • 0037388679 scopus 로고    scopus 로고
    • Protein-protein interactions as a target for drugs in proteomics
    • Archakov AI, et al. Protein-protein interactions as a target for drugs in proteomics. Proteomics. 2003;3:380-91.
    • (2003) Proteomics , vol.3 , pp. 380-391
    • Archakov, A.I.1
  • 16
    • 3342908718 scopus 로고    scopus 로고
    • Emerging classes of protein-protein interaction inhibitors and new tools for their development
    • Pagliaro L, et al. Emerging classes of protein-protein interaction inhibitors and new tools for their development. Curr Opin Chem Biol. 2004;8:442-9.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 442-449
    • Pagliaro, L.1
  • 17
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov. 2004;3:301-17.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 18
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • Berg T. Modulation of protein-protein interactions with small organic molecules. Angew Chem Int Ed Engl. 2003;42:2462-81.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 2462-2481
    • Berg, T.1
  • 19
    • 34447290874 scopus 로고    scopus 로고
    • Protein-protein interaction inhibitors: Small molecules from screening techniques
    • Fletcher S, Hamilton AD. Protein-protein interaction inhibitors: small molecules from screening techniques. Curr Top Med Chem. 2007;7:922-7.
    • (2007) Curr Top Med Chem , vol.7 , pp. 922-927
    • Fletcher, S.1    Hamilton, A.D.2
  • 20
    • 70049097909 scopus 로고    scopus 로고
    • Novel mechanistic insights into viral modulation of immune receptor signaling
    • Sigalov AB. Novel mechanistic insights into viral modulation of immune receptor signaling. PLoS Pathog. 2009;5:e1000404.
    • (2009) PLoS Pathog , vol.5
    • Sigalov, A.B.1
  • 21
    • 78149301312 scopus 로고    scopus 로고
    • HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferation
    • Cohen T, Cohen SJ, Antonovsky N, Cohen IR, Shai Y. HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferation. PLoS Pathog. 2010;6:e1001085.
    • (2010) PLoS Pathog , vol.6
    • Cohen, T.1    Cohen, S.J.2    Antonovsky, N.3    Cohen, I.R.4    Shai, Y.5
  • 23
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol. 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 25
    • 34047113297 scopus 로고    scopus 로고
    • Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment
    • Minezaki Y, Homma K, Nishikawa K. Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment. J Mol Biol. 2007;368:902-13.
    • (2007) J Mol Biol , vol.368 , pp. 902-913
    • Minezaki, Y.1    Homma, K.2    Nishikawa, K.3
  • 26
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The database of disordered proteins
    • Sickmeier M, et al. DisProt: the database of disordered proteins. Nucleic Acids Res. 2007;35:D786-93.
    • (2007) Nucleic Acids Res , vol.35
    • Sickmeier, M.1
  • 27
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A, Nakamura H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett. 2006;580:2041-5.
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 28
    • 0141447817 scopus 로고    scopus 로고
    • T-cell receptor signal transmission: Who gives an ITAM?
    • Pitcher LA, van Oers NS. T-cell receptor signal transmission: who gives an ITAM? Trends Immunol. 2003;24:554-60.
    • (2003) Trends Immunol , vol.24 , pp. 554-560
    • Pitcher, L.A.1    Van Oers, N.S.2
  • 29
    • 0942290446 scopus 로고    scopus 로고
    • The avian B-cell receptor complex: Distinct roles of Igalpha and Igbeta in B-cell development
    • Pike KA, Baig E, Ratcliffe MJ. The avian B-cell receptor complex: distinct roles of Igalpha and Igbeta in B-cell development. Immunol Rev. 2004;197:10-25.
    • (2004) Immunol Rev , vol.197 , pp. 10-25
    • Pike, K.A.1    Baig, E.2    Ratcliffe, M.J.3
  • 30
    • 33846342568 scopus 로고    scopus 로고
    • The Ig-alpha ITAM is required for efficient differentiation but not proliferation of pre-B cells
    • Storch B, Meixlsperger S, Jumaa H. The Ig-alpha ITAM is required for efficient differentiation but not proliferation of pre-B cells. Eur J Immunol. 2007;37:252-60.
    • (2007) Eur J Immunol , vol.37 , pp. 252-260
    • Storch, B.1    Meixlsperger, S.2    Jumaa, H.3
  • 31
    • 0038549478 scopus 로고    scopus 로고
    • Signal transduction by immunoglobulin Fc receptors
    • Sanchez-Mejorada G, Rosales C. Signal transduction by immunoglobulin Fc receptors. J Leukoc Biol. 1998;63:521-33.
    • (1998) J Leukoc Biol , vol.63 , pp. 521-533
    • Sanchez-Mejorada, G.1    Rosales, C.2
  • 33
    • 4544233317 scopus 로고    scopus 로고
    • Qualitatively differential regulation of T cell activation and apoptosis by T cell receptor zeta chain ITAMs and their tyrosine residues
    • Chae WJ, et al. Qualitatively differential regulation of T cell activation and apoptosis by T cell receptor zeta chain ITAMs and their tyrosine residues. Int Immunol. 2004;16:1225-36.
    • (2004) Int Immunol , vol.16 , pp. 1225-1236
    • Chae, W.J.1
  • 34
    • 34249280244 scopus 로고    scopus 로고
    • Innate versus adaptive immunity: A paradigm past its prime?
    • Borghesi L, Milcarek C. Innate versus adaptive immunity: a paradigm past its prime? Cancer Res. 2007;67:3989-93.
    • (2007) Cancer Res , vol.67 , pp. 3989-3993
    • Borghesi, L.1    Milcarek, C.2
  • 36
    • 0035321067 scopus 로고    scopus 로고
    • The evolution and genetics of innate immunity
    • Kimbrell DA, Beutler B. The evolution and genetics of innate immunity. Nat Rev Genet. 2001;2:256-67.
    • (2001) Nat Rev Genet , vol.2 , pp. 256-267
    • Kimbrell, D.A.1    Beutler, B.2
  • 37
    • 32944468017 scopus 로고    scopus 로고
    • The evolution of adaptive immune systems
    • Cooper MD, Alder MN. The evolution of adaptive immune systems. Cell. 2006;124:815-22.
    • (2006) Cell , vol.124 , pp. 815-822
    • Cooper, M.D.1    Alder, M.N.2
  • 38
    • 34249080854 scopus 로고    scopus 로고
    • Why study the evolution of immunity?
    • Litman GW, Cooper MD. Why study the evolution of immunity? Nat Immunol. 2007;8:547-8.
    • (2007) Nat Immunol , vol.8 , pp. 547-548
    • Litman, G.W.1    Cooper, M.D.2
  • 40
    • 70249111187 scopus 로고    scopus 로고
    • Natural killer cells remember: An evolutionary bridge between innate and adaptive immunity?
    • Sun JC, Lanier LL. Natural killer cells remember: an evolutionary bridge between innate and adaptive immunity? Eur J Immunol. 2009;39:2059-64.
    • (2009) Eur J Immunol , vol.39 , pp. 2059-2064
    • Sun, J.C.1    Lanier, L.L.2
  • 41
    • 5444259408 scopus 로고    scopus 로고
    • Phenomenon of life: Between equilibrium and nonlinearity
    • Galimov EM. Phenomenon of life: between equilibrium and nonlinearity. Orig Life Evol Biosph. 2004;34:599-613.
    • (2004) Orig Life Evol Biosph , vol.34 , pp. 599-613
    • Galimov, E.M.1
  • 42
    • 34249780115 scopus 로고    scopus 로고
    • Interaction between HIV gp41 fusion peptide and T cell receptor: Putting the puzzle pieces back together
    • author reply 1635
    • Sigalov AB. Interaction between HIV gp41 fusion peptide and T cell receptor: putting the puzzle pieces back together. Faseb J. 2007; 21:1633-1634; author reply 1635.
    • (2007) Faseb J , vol.21 , pp. 1633-1634
    • Sigalov, A.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.