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Volumn 34, Issue , 2016, Pages 151-172

Regulation of Immunity by Butyrophilins

Author keywords

B30.2; BTN1A; BTN2A; BTN3A; PRYSPRY

Indexed keywords

BUTYROPHILIN; CD3 ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MYELIN OLIGODENDROCYTE GLYCOPROTEIN; PERIPLAKIN; PLAKIN; PROTEIN; PROTEIN KINASE ZAP 70; T LYMPHOCYTE RECEPTOR ALPHA CHAIN; T LYMPHOCYTE RECEPTOR BETA CHAIN; UNCLASSIFIED DRUG; B7 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR;

EID: 84969792498     PISSN: 07320582     EISSN: 15453278     Source Type: Book Series    
DOI: 10.1146/annurev-immunol-041015-055435     Document Type: Article
Times cited : (129)

References (135)
  • 1
    • 84927130807 scopus 로고    scopus 로고
    • Immune checkpoint targeting in cancer therapy: Toward combination strategies with curative potential
    • Sharma P, Allison JP. 2015. Immune checkpoint targeting in cancer therapy: toward combination strategies with curative potential. Cell 161:205-14
    • (2015) Cell , vol.161 , pp. 205-214
    • Sharma, P.1    Allison, J.P.2
  • 2
    • 79954533158 scopus 로고    scopus 로고
    • Shifting the equilibrium in cancer immunoediting: From tumor tolerance to eradication
    • Quezada SA, Peggs KS, Simpson TR,Allison JP. 2011. Shifting the equilibrium in cancer immunoediting: from tumor tolerance to eradication. Immunol. Rev. 241:104-18
    • (2011) Immunol. Rev , vol.241 , pp. 104-118
    • Quezada, S.A.1    Peggs, K.S.2    Simpson, T.R.3    Allison, J.P.4
  • 3
    • 84873396202 scopus 로고    scopus 로고
    • Targeting the B7 family of co-stimulatory molecules: Successes and challenges
    • Podojil JR, Miller SD. 2013. Targeting the B7 family of co-stimulatory molecules: successes and challenges. BioDrugs 27:1-13
    • (2013) BioDrugs , vol.27 , pp. 1-13
    • Podojil, J.R.1    Miller, S.D.2
  • 4
    • 84928774156 scopus 로고    scopus 로고
    • The future of immune checkpoint therapy
    • Sharma P, Allison JP. 2015. The future of immune checkpoint therapy. Science 348:56-61
    • (2015) Science , vol.348 , pp. 56-61
    • Sharma, P.1    Allison, J.P.2
  • 5
    • 67349259050 scopus 로고    scopus 로고
    • Regulation of costimulation in the era of butyrophilins
    • Arnett HA, Escobar SS, Viney JL. 2009. Regulation of costimulation in the era of butyrophilins. Cytokine 46:370-75
    • (2009) Cytokine , vol.46 , pp. 370-375
    • Arnett, H.A.1    Escobar, S.S.2    Viney, J.L.3
  • 7
    • 84867843325 scopus 로고    scopus 로고
    • The butyrophilin (BTN) gene family: From milk fat to the regulation of the immune response
    • Afrache H, Gouret P, Ainouche S, Pontarotti P, Olive D. 2012. The butyrophilin (BTN) gene family: from milk fat to the regulation of the immune response. Immunogenetics 64:781-94
    • (2012) Immunogenetics , vol.64 , pp. 781-794
    • Afrache, H.1    Gouret, P.2    Ainouche, S.3    Pontarotti, P.4    Olive, D.5
  • 8
    • 84904971095 scopus 로고    scopus 로고
    • Immune modulation by butyrophilins
    • Arnett HA, Viney JL. 2014. Immune modulation by butyrophilins. Nat. Rev. Immunol. 14:559-69
    • (2014) Nat. Rev. Immunol , vol.14 , pp. 559-569
    • Arnett, H.A.1    Viney, J.L.2
  • 9
    • 0033153443 scopus 로고    scopus 로고
    • Structure and evolution of the extended B7 family
    • Henry J, Miller MM, Pontarotti P. 1999. Structure and evolution of the extended B7 family. Immunol. Today 20:285-88
    • (1999) Immunol. Today , vol.20 , pp. 285-288
    • Henry, J.1    Miller, M.M.2    Pontarotti, P.3
  • 10
    • 0035251711 scopus 로고    scopus 로고
    • The cluster of BTN genes in the extended major histocompatibility complex
    • Rhodes DA, Stammers M, Malcherek G, Beck S, Trowsdale J. 2001. The cluster of BTN genes in the extended major histocompatibility complex. Genomics 71:351-62
    • (2001) Genomics , vol.71 , pp. 351-362
    • Rhodes, D.A.1    Stammers, M.2    Malcherek, G.3    Beck, S.4    Trowsdale, J.5
  • 11
    • 4444278347 scopus 로고    scopus 로고
    • Frontline: Characterization of BT3 molecules belonging to the B7 family expressed on immune cells
    • Compte E, Pontarotti P, Collette Y, Lopez M, Olive D. 2004. Frontline: characterization of BT3 molecules belonging to the B7 family expressed on immune cells. Eur. J. Immunol. 34:2089-99
    • (2004) Eur. J. Immunol , vol.34 , pp. 2089-2099
    • Compte, E.1    Pontarotti, P.2    Collette, Y.3    Lopez, M.4    Olive, D.5
  • 12
    • 33846491444 scopus 로고    scopus 로고
    • BTNL2, a butyrophilin/B7-like molecule, is a negative costimulatory molecule modulated in intestinal inflammation
    • Arnett HA, Escobar SS, Gonzalez-Suarez E, Budelsky AL, Steffen LA, et al. 2007. BTNL2, a butyrophilin/B7-like molecule, is a negative costimulatory molecule modulated in intestinal inflammation. J. Immunol. 178:1523-33
    • (2007) J. Immunol , vol.178 , pp. 1523-1533
    • Arnett, H.A.1    Escobar, S.S.2    Gonzalez-Suarez, E.3    Budelsky, A.L.4    Steffen, L.A.5
  • 13
    • 77951633576 scopus 로고    scopus 로고
    • BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of T cell activation
    • Smith IA, Knezevic BR, Ammann JU, Rhodes DA, Aw D, et al. 2010. BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of T cell activation. J. Immunol. 184:3514-25
    • (2010) J. Immunol , vol.184 , pp. 3514-3525
    • Smith, I.A.1    Knezevic, B.R.2    Ammann, J.U.3    Rhodes, D.A.4    Aw, D.5
  • 14
    • 84874239826 scopus 로고    scopus 로고
    • Butyrophilin-like 2 modulates B7 costimulation to induce Foxp3 expression and regulatory T cell development in mature T cells
    • Swanson RM, GavinMA, Escobar SS, Rottman JB, Lipsky BP, et al. 2013. Butyrophilin-like 2 modulates B7 costimulation to induce Foxp3 expression and regulatory T cell development in mature T cells. J. Immunol. 190:2027-35
    • (2013) J. Immunol , vol.190 , pp. 2027-2035
    • Swanson, R.M.1    Gavin, M.A.2    Escobar, S.S.3    Rottman, J.B.4    Lipsky, B.P.5
  • 15
    • 84872930787 scopus 로고    scopus 로고
    • Six-of-The-best: Unique contributions of γδT cells to immunology
    • Vantourout P, Hayday A. 2013. Six-of-The-best: unique contributions of γδT cells to immunology. Nat. Rev. Immunol. 13:88-100
    • (2013) Nat. Rev. Immunol , vol.13 , pp. 88-100
    • Vantourout, P.1    Hayday, A.2
  • 16
    • 77954143558 scopus 로고    scopus 로고
    • γδTcell effector functions: A blend of innate programming and acquired plasticity
    • Bonneville M, O'Brien RL, Born WK. 2010. γδTcell effector functions: a blend of innate programming and acquired plasticity. Nat. Rev. Immunol. 10:467-78
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 467-478
    • Bonneville, M.1    O'Brien, R.L.2    Born, W.K.3
  • 17
    • 68649104004 scopus 로고    scopus 로고
    • γδT cells and the lymphoid stress-surveillance response
    • Hayday AC. 2009. γδT cells and the lymphoid stress-surveillance response. Immunity 31:184-96
    • (2009) Immunity , vol.31 , pp. 184-196
    • Hayday, A.C.1
  • 18
  • 20
    • 79960954029 scopus 로고    scopus 로고
    • Searching for "signal 2": Costimulation requirements of γδ T cells
    • Ribot JC, Debarros A, Silva-Santos B. 2011. Searching for "signal 2": costimulation requirements of γδ T cells. Cell Mol. Life Sci. 68:2345-55
    • (2011) Cell Mol. Life Sci , vol.68 , pp. 2345-2355
    • Ribot, J.C.1    Debarros, A.2    Silva-Santos, B.3
  • 21
    • 84864130583 scopus 로고    scopus 로고
    • B7-CD28 costimulatory signals control the survival and proliferation of murine and human γδ T cells via IL-2 production
    • Ribot JC, Debarros A, Mancio-Silva L, Pamplona A, Silva-Santos B. 2012. B7-CD28 costimulatory signals control the survival and proliferation of murine and human γδ T cells via IL-2 production. J. Immunol. 189:1202-8
    • (2012) J. Immunol , vol.189 , pp. 1202-1208
    • Ribot, J.C.1    Debarros, A.2    Mancio-Silva, L.3    Pamplona, A.4    Silva-Santos, B.5
  • 22
    • 42649092113 scopus 로고    scopus 로고
    • Skint1, the prototype of a newly identified immunoglobulin superfamily gene cluster, positively selects epidermal γδT cells
    • Boyden LM, Lewis JM, Barbee SD, Bas A, Girardi M, et al. 2008. Skint1, the prototype of a newly identified immunoglobulin superfamily gene cluster, positively selects epidermal γδT cells. Nat. Genet. 40:656-62
    • (2008) Nat. Genet , vol.40 , pp. 656-662
    • Boyden, L.M.1    Lewis, J.M.2    Barbee, S.D.3    Bas, A.4    Girardi, M.5
  • 23
    • 84866308872 scopus 로고    scopus 로고
    • Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing by a major human γδ T-cell subset
    • Harly C, Guillaume Y, Nedellec S, Peigne CM, Monkkonen H, et al. 2012. Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing by a major human γδ T-cell subset. Blood 120:2269-79
    • (2012) Blood , vol.120 , pp. 2269-2279
    • Harly, C.1    Guillaume, Y.2    Nedellec, S.3    Peigne, C.M.4    Monkkonen, H.5
  • 25
    • 0031461574 scopus 로고    scopus 로고
    • Cloning, localization, and structure of new members of the butyrophilin gene family in the juxta-telomeric region of the major histocompatibility complex
    • Tazi-Ahnini R, Henry J, Offer C, Bouissou-Bouchouata C, Mather IH, Pontarotti P. 1997. Cloning, localization, and structure of new members of the butyrophilin gene family in the juxta-telomeric region of the major histocompatibility complex. Immunogenetics 47:55-63
    • (1997) Immunogenetics , vol.47 , pp. 55-63
    • Tazi-Ahnini, R.1    Henry, J.2    Offer, C.3    Bouissou-Bouchouata, C.4    Mather, I.H.5    Pontarotti, P.6
  • 26
    • 0030792643 scopus 로고    scopus 로고
    • Cloning, structural analysis, and mapping of the B30 and B7 multigenic families to the major histocompatibility complex (MHC) and other chromosomal regions
    • Henry J, Ribouchon M, Depetris D, Mattei M, Offer C, et al. 1997. Cloning, structural analysis, and mapping of the B30 and B7 multigenic families to the major histocompatibility complex (MHC) and other chromosomal regions. Immunogenetics 46:383-95
    • (1997) Immunogenetics , vol.46 , pp. 383-395
    • Henry, J.1    Ribouchon, M.2    Depetris, D.3    Mattei, M.4    Offer, C.5
  • 27
    • 67349233519 scopus 로고    scopus 로고
    • Reproducible association with type 1 diabetes in the extended class i region of the major histocompatibility complex
    • Viken MK, Blomhoff A, Olsson M, Akselsen HE, Pociot F, et al. 2009. Reproducible association with type 1 diabetes in the extended class I region of the major histocompatibility complex. Genes Immun. 10:323-33
    • (2009) Genes Immun , vol.10 , pp. 323-333
    • Viken, M.K.1    Blomhoff, A.2    Olsson, M.3    Akselsen, H.E.4    Pociot, F.5
  • 28
    • 20144388906 scopus 로고    scopus 로고
    • Sarcoidosis is associated with a truncating splice site mutation in BTNL2
    • Valentonyte R, Hampe J, Huse K, Rosenstiel P, Albrecht M, et al. 2005. Sarcoidosis is associated with a truncating splice site mutation in BTNL2. Nat. Genet. 37:357-64
    • (2005) Nat. Genet , vol.37 , pp. 357-364
    • Valentonyte, R.1    Hampe, J.2    Huse, K.3    Rosenstiel, P.4    Albrecht, M.5
  • 29
    • 70349334518 scopus 로고    scopus 로고
    • Confirmation of the novel association at the BTNL2 locus with ulcerative colitis
    • Pathan S, GowdyRE, Cooney R, Beckly JB,Hancock L, et al. 2009. Confirmation of the novel association at the BTNL2 locus with ulcerative colitis. Tissue Antigens 74:322-29
    • (2009) Tissue Antigens , vol.74 , pp. 322-329
    • Pathan, S.1    Gowdy, R.E.2    Cooney, R.3    Beckly, J.B.4    Hancock, L.5
  • 30
    • 84924423137 scopus 로고    scopus 로고
    • Pooled sequencing of 531 genes in inflammatory bowel disease identifies an associated rare variant in BTNL2 and implicates other immune related genes
    • Prescott NJ, Lehne B, Stone K, Lee JC, Taylor K, et al. 2015. Pooled sequencing of 531 genes in inflammatory bowel disease identifies an associated rare variant in BTNL2 and implicates other immune related genes. PLOS Genet. 11:e1004955
    • (2015) PLOS Genet , vol.11 , pp. e1004955
    • Prescott, N.J.1    Lehne, B.2    Stone, K.3    Lee, J.C.4    Taylor, K.5
  • 31
    • 33646272188 scopus 로고    scopus 로고
    • Analysis of a functional BTNL2 polymorphism in type 1 diabetes, rheumatoid arthritis, and systemic lupus erythematosus
    • Orozco G, Eerligh P, Sanchez E, Zhernakova S, Roep BO, et al. 2005. Analysis of a functional BTNL2 polymorphism in type 1 diabetes, rheumatoid arthritis, and systemic lupus erythematosus. Hum. Immunol. 66:1235-41
    • (2005) Hum. Immunol , vol.66 , pp. 1235-1241
    • Orozco, G.1    Eerligh, P.2    Sanchez, E.3    Zhernakova, S.4    Roep, B.O.5
  • 32
    • 29644442440 scopus 로고    scopus 로고
    • Association of the truncating splice site mutation in BTNL2 with multiple sclerosis is secondary to HLA-DRB1 and z ast 15
    • Traherne JA, Barcellos LF, Sawcer SJ,Compston A,Ramsay PP, et al. 2006. Association of the truncating splice site mutation in BTNL2 with multiple sclerosis is secondary to HLA-DRB1 and z ast 15. Hum. Mol. Genet. 15:155-61
    • (2006) Hum. Mol. Genet , vol.15 , pp. 155-161
    • Traherne, J.A.1    Barcellos, L.F.2    Sawcer, S.J.3    Compston, A.4    Ramsay, P.P.5
  • 34
    • 0035967146 scopus 로고    scopus 로고
    • Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses
    • Stamper CC, Zhang Y,Tobin JF, Erbe DV, Ikemizu S, et al. 2001. Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses. Nature 410:608-11
    • (2001) Nature , vol.410 , pp. 608-611
    • Stamper, C.C.1    Zhang, Y.2    Tobin, J.F.3    Erbe, D.V.4    Ikemizu, S.5
  • 36
  • 37
    • 34447335278 scopus 로고    scopus 로고
    • Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function
    • James LC, Keeble AH,Khan Z, Rhodes DA, Trowsdale J. 2007. Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function. PNAS 104:6200-5
    • (2007) PNAS , vol.104 , pp. 6200-6205
    • James, L.C.1    Keeble, A.H.2    Khan, Z.3    Rhodes, D.A.4    Trowsdale, J.5
  • 38
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
    • Xu H, Yang J, GaoW, Li L, Li P, et al. 2014. Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 513:237-41
    • (2014) Nature , vol.513 , pp. 237-241
    • Xu, H.1    Yang, J.2    Gao, W.3    Li, L.4    Li, P.5
  • 39
    • 84908604511 scopus 로고    scopus 로고
    • Detecting "different": Pyrin senses modifiedGTPases
    • de ZoeteMR, Flavell RA. 2014. Detecting "different": Pyrin senses modifiedGTPases. Cell Res. 24:1286-87
    • (2014) Cell Res , vol.24 , pp. 1286-1287
    • De Zoete, M.R.1    Flavell, R.A.2
  • 40
    • 84918535219 scopus 로고    scopus 로고
    • NOD1 and NOD2: Signaling, host defense, and inflammatory disease
    • Caruso R, Warner N, Inohara N, Nunez G. 2014. NOD1 and NOD2: signaling, host defense, and inflammatory disease. Immunity 41:898-908
    • (2014) Immunity , vol.41 , pp. 898-908
    • Caruso, R.1    Warner, N.2    Inohara, N.3    Nunez, G.4
  • 41
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, et al. 2001. The tripartite motif family identifies cell compartments. EMBO J. 20:2140-51
    • (2001) EMBO J , vol.20 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3    Merla, G.4    Cairo, S.5
  • 42
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: Retroviral restriction and antiviral defence
    • Nisole S, Stoye JP, Saib A. 2005. TRIM family proteins: retroviral restriction and antiviral defence. Nat. Rev. Microbiol. 3:799-808
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 43
    • 54949126675 scopus 로고    scopus 로고
    • TRIM family proteins and their emerging roles in innate immunity
    • Ozato K, Shin DM, Chang TH, Morse HC. 2008. TRIM family proteins and their emerging roles in innate immunity. Nat. Rev. Immunol. 8:849-60
    • (2008) Nat. Rev. Immunol , vol.8 , pp. 849-860
    • Ozato, K.1    Shin, D.M.2    Chang, T.H.3    Morse, H.C.4
  • 44
    • 33846220331 scopus 로고    scopus 로고
    • TRIM21 is a trimeric protein that binds IgG Fc via the B30.2 domain
    • Rhodes DA, Trowsdale J. 2007. TRIM21 is a trimeric protein that binds IgG Fc via the B30.2 domain. Mol. Immunol. 44:2406-14
    • (2007) Mol. Immunol , vol.44 , pp. 2406-2414
    • Rhodes, D.A.1    Trowsdale, J.2
  • 47
    • 84871946152 scopus 로고    scopus 로고
    • TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity
    • Uchil PD, Hinz A, Siegel S, Coenen-Stass A, Pertel T, et al. 2013. TRIM protein-mediated regulation of inflammatory and innate immune signaling and its association with antiretroviral activity. J. Virol. 87:257-72
    • (2013) J. Virol , vol.87 , pp. 257-272
    • Uchil, P.D.1    Hinz, A.2    Siegel, S.3    Coenen-Stass, A.4    Pertel, T.5
  • 48
    • 79955377543 scopus 로고    scopus 로고
    • TRIM5 is an innate immune sensor for the retrovirus capsid lattice
    • Pertel T, Hausmann S, Morger D, Zuger S, Guerra J, et al. 2011. TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 472:361-65
    • (2011) Nature , vol.472 , pp. 361-365
    • Pertel, T.1    Hausmann, S.2    Morger, D.3    Zuger, S.4    Guerra, J.5
  • 49
    • 33744914590 scopus 로고    scopus 로고
    • BTNL2, a butyrophilin-like molecule that functions to inhibit T cell activation
    • Nguyen T, Liu XK, Zhang Y, Dong C. 2006. BTNL2, a butyrophilin-like molecule that functions to inhibit T cell activation. J. Immunol. 176:7354-60
    • (2006) J. Immunol , vol.176 , pp. 7354-7360
    • Nguyen, T.1    Liu, X.K.2    Zhang, Y.3    Dong, C.4
  • 50
    • 84877826452 scopus 로고    scopus 로고
    • Butyrophilin Btn2a2 inhibits TCR activation and phosphatidylinositol 3-kinase/Akt pathway signaling and induces Foxp3 expression in T lymphocytes
    • Ammann JU, Cooke A, Trowsdale J. 2013. Butyrophilin Btn2a2 inhibits TCR activation and phosphatidylinositol 3-kinase/Akt pathway signaling and induces Foxp3 expression in T lymphocytes. J. Immunol. 190:5030-6
    • (2013) J. Immunol , vol.190 , pp. 5030-5036
    • Ammann, J.U.1    Cooke, A.2    Trowsdale, J.3
  • 51
    • 84961159630 scopus 로고    scopus 로고
    • Btn2a2, a T-cell immunomodulatory molecule coregulated with MHC class II genes
    • Sarter K, Leimgruber E, Gobet F, Agrawal V, Dunand-Sauthier I, et al. 2016. Btn2a2, a T-cell immunomodulatory molecule coregulated with MHC class II genes. J. Exp. Med. 213:177-87
    • (2016) J. Exp. Med , vol.213 , pp. 177-187
    • Sarter, K.1    Leimgruber, E.2    Gobet, F.3    Agrawal, V.4    Dunand-Sauthier, I.5
  • 53
    • 25844499012 scopus 로고    scopus 로고
    • Regulation ofMHCclass II gene expression by the class II transactivator
    • ReithW, LeibundGut-Landmann S,Waldburger JM. 2005. Regulation ofMHCclass II gene expression by the class II transactivator. Nat. Rev. Immunol. 5:793-806
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 793-806
    • Reith, W.1    LeibundGut-Landmann, S.2    Waldburger, J.M.3
  • 54
    • 79851504402 scopus 로고    scopus 로고
    • CD277 is a negative co-stimulatory molecule universally expressed by ovarian cancer microenvironmental cells
    • Cubillos-Ruiz JR,MartinezD, Scarlett UK,Rutkowski MR,Nesbeth YC, et al. 2010. CD277 is a negative co-stimulatory molecule universally expressed by ovarian cancer microenvironmental cells. Oncotarget 1:329-38
    • (2010) Oncotarget , vol.1 , pp. 329-338
    • Cubillos-Ruiz, J.R.1    Martinez, D.2    Scarlett, U.K.3    Rutkowski, M.R.4    Nesbeth, Y.C.5
  • 55
    • 84862023293 scopus 로고    scopus 로고
    • BTN3A2 expression in epithelial ovarian cancer is associated with higher tumor infiltrating T cells and a better prognosis
    • Le Page C, Marineau A, Bonza PK, Rahimi K, Cyr L, et al. 2012. BTN3A2 expression in epithelial ovarian cancer is associated with higher tumor infiltrating T cells and a better prognosis. PLOS ONE 7:e38541
    • (2012) PLOS ONE , vol.7 , pp. e38541
    • Le Page, C.1    Marineau, A.2    Bonza, P.K.3    Rahimi, K.4    Cyr, L.5
  • 56
    • 79952714881 scopus 로고    scopus 로고
    • Butyrophilin-like 1 encodes an enterocyte protein that selectively regulates functional interactions with T lymphocytes
    • Bas A, Swamy M, Abeler-Dorner L,WilliamsG, Pang DJ, et al. 2011. Butyrophilin-like 1 encodes an enterocyte protein that selectively regulates functional interactions with T lymphocytes. PNAS 108:4376-81
    • (2011) PNAS , vol.108 , pp. 4376-4381
    • Bas, A.1    Swamy, M.2    Abeler-Dorner, L.3    Williams, G.4    Pang, D.J.5
  • 58
    • 84884146085 scopus 로고    scopus 로고
    • BTNL8, a butyrophilin-like molecule that costimulates the primary immune response
    • Chapoval AI, Smithson G, Brunick L, Mesri M, Boldog FL, et al. 2013. BTNL8, a butyrophilin-like molecule that costimulates the primary immune response. Mol. Immunol. 56:819-28
    • (2013) Mol. Immunol , vol.56 , pp. 819-828
    • Chapoval, A.I.1    Smithson, G.2    Brunick, L.3    Mesri, M.4    Boldog, F.L.5
  • 59
    • 33746178062 scopus 로고    scopus 로고
    • Selection of the cutaneous intraepithelial γδ+ T cell repertoire by a thymic stromal determinant
    • Lewis JM, GirardiM, Roberts SJ, Barbee SD,Hayday AC, Tigelaar RE. 2006. Selection of the cutaneous intraepithelial γδ+ T cell repertoire by a thymic stromal determinant. Nat. Immunol. 7:843-50
    • (2006) Nat. Immunol , vol.7 , pp. 843-850
    • Lewis, J.M.1    Girardi, M.2    Roberts, S.J.3    Barbee, S.D.4    Hayday, A.C.5    Tigelaar, R.E.6
  • 60
    • 79952752806 scopus 로고    scopus 로고
    • Skint-1 is a highly specific, unique selecting component for epidermal T cells
    • Barbee SD, Woodward MJ, Turchinovich G, Mention JJ, Lewis JM, et al. 2011. Skint-1 is a highly specific, unique selecting component for epidermal T cells. PNAS 108:3330-35
    • (2011) PNAS , vol.108 , pp. 3330-3335
    • Barbee, S.D.1    Woodward, M.J.2    Turchinovich, G.3    Mention, J.J.4    Lewis, J.M.5
  • 61
    • 79960447248 scopus 로고    scopus 로고
    • Skint-1 identifies a common molecular mechanism for the development of interferon-γ-secreting versus interleukin-17-secreting γδT cells
    • Turchinovich G, Hayday AC. 2011. Skint-1 identifies a common molecular mechanism for the development of interferon-γ-secreting versus interleukin-17-secreting γδT cells. Immunity 35:59-68
    • (2011) Immunity , vol.35 , pp. 59-68
    • Turchinovich, G.1    Hayday, A.C.2
  • 62
    • 33746171691 scopus 로고    scopus 로고
    • Selection of intraepithelial γδcells: The Holy GrIEL at last?
    • Bonneville M. 2006. Selection of intraepithelial γδcells: the Holy GrIEL at last? Nat. Immunol. 7:791-92
    • (2006) Nat. Immunol , vol.7 , pp. 791-792
    • Bonneville, M.1
  • 64
    • 84899121545 scopus 로고    scopus 로고
    • The intracellular B30.2 domain of butyrophilin 3a1 binds phosphoantigens to mediate activation of human Vγ9Vδ2 T cells
    • Sandstrom A, Peigne CM, Leger A, Crooks JE, Konczak F, et al. 2014. The intracellular B30.2 domain of butyrophilin 3a1 binds phosphoantigens to mediate activation of human Vγ9Vδ2 T cells. Immunity 40:490-500
    • (2014) Immunity , vol.40 , pp. 490-500
    • Sandstrom, A.1    Peigne, C.M.2    Leger, A.3    Crooks, J.E.4    Konczak, F.5
  • 65
    • 84921894883 scopus 로고    scopus 로고
    • Synthesis of a phosphoantigen prodrug that potently activates Vγ9Vδ2 T-lymphocytes
    • Hsiao CH, Lin X, Barney RJ, Shippy RR, Li J, et al. 2014. Synthesis of a phosphoantigen prodrug that potently activates Vγ9Vδ2 T-lymphocytes. Chem. Biol. 21:945-54
    • (2014) Chem. Biol , vol.21 , pp. 945-954
    • Hsiao, C.H.1    Lin, X.2    Barney, R.J.3    Shippy, R.R.4    Li, J.5
  • 66
    • 84924388810 scopus 로고    scopus 로고
    • Activation of human γδT cells by cytosolic interactions of BTN3A1 with soluble phosphoantigens and the cytoskeletal adaptor periplakin
    • Rhodes DA, Chen HC, Price AJ, Keeble AH, Davey MS, et al. 2015. Activation of human γδT cells by cytosolic interactions of BTN3A1 with soluble phosphoantigens and the cytoskeletal adaptor periplakin. J. Immunol. 194:2390-98
    • (2015) J. Immunol , vol.194 , pp. 2390-2398
    • Rhodes, D.A.1    Chen, H.C.2    Price, A.J.3    Keeble, A.H.4    Davey, M.S.5
  • 67
    • 84883147590 scopus 로고    scopus 로고
    • Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδT cells
    • Vavassori S, Kumar A, Wan GS, Ramanjaneyulu GS, Cavallari M, et al. 2013. Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδT cells. Nat. Immunol. 14:908-16
    • (2013) Nat. Immunol , vol.14 , pp. 908-916
    • Vavassori, S.1    Kumar, A.2    Wan, G.S.3    Ramanjaneyulu, G.S.4    Cavallari, M.5
  • 68
    • 0037455013 scopus 로고    scopus 로고
    • Human T cell receptor γδ cells recognize endogenous mevalonate metabolites in tumor cells
    • Gober HJ, Kistowska M, Angman L, Jeno P, Mori L, De Libero G. 2003. Human T cell receptor γδ cells recognize endogenous mevalonate metabolites in tumor cells. J. Exp. Med. 197:163-68
    • (2003) J. Exp. Med , vol.197 , pp. 163-168
    • Gober, H.J.1    Kistowska, M.2    Angman, L.3    Jeno, P.4    Mori, L.5    De Libero, G.6
  • 69
    • 84877145897 scopus 로고    scopus 로고
    • Selective role of mevalonate pathway in regulating perforin but not FasL and TNFαrelease in human natural killer cells
    • Poggi A, Boero S, Musso A, Zocchi MR. 2013. Selective role of mevalonate pathway in regulating perforin but not FasL and TNFαrelease in human natural killer cells. PLOS ONE 8:e62932
    • (2013) PLOS ONE , vol.8 , pp. e62932
    • Poggi, A.1    Boero, S.2    Musso, A.3    Zocchi, M.R.4
  • 71
    • 51149103549 scopus 로고    scopus 로고
    • Dysregulation of the host mevalonate pathway during early bacterial infection activates human TCR γδ cells
    • Kistowska M, Rossy E, Sansano S, Gober HJ, Landmann R, et al. 2008. Dysregulation of the host mevalonate pathway during early bacterial infection activates human TCR γδ cells. Eur. J. Immunol. 38:2200-9
    • (2008) Eur. J. Immunol , vol.38 , pp. 2200-2209
    • Kistowska, M.1    Rossy, E.2    Sansano, S.3    Gober, H.J.4    Landmann, R.5
  • 72
    • 79953699055 scopus 로고    scopus 로고
    • Host defense against viral infection involves interferon mediated down-regulation of sterol biosynthesis
    • BlancM,Hsieh WY,RobertsonKA, Watterson S, ShuiG, et al. 2011. Host defense against viral infection involves interferon mediated down-regulation of sterol biosynthesis. PLOS Biol. 9:e1000598
    • (2011) PLOS Biol , vol.9 , pp. e1000598
    • Blanc, M.1    Hsieh, W.Y.2    Robertson, K.A.3    Watterson, S.4    Shui, G.5
  • 73
    • 34547656276 scopus 로고    scopus 로고
    • The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts
    • Wang X, Hinson ER, Cresswell P. 2007. The interferon-inducible protein viperin inhibits influenza virus release by perturbing lipid rafts. Cell Host Microbe 2:96-105
    • (2007) Cell Host Microbe , vol.2 , pp. 96-105
    • Wang, X.1    Hinson, E.R.2    Cresswell, P.3
  • 74
    • 83655192651 scopus 로고    scopus 로고
    • Viperin: A multifunctional, interferon-inducible protein that regulates virus replication
    • Seo JY, Yaneva R, Cresswell P. 2011. Viperin: a multifunctional, interferon-inducible protein that regulates virus replication. Cell Host Microbe 10:534-39
    • (2011) Cell Host Microbe , vol.10 , pp. 534-539
    • Seo, J.Y.1    Yaneva, R.2    Cresswell, P.3
  • 75
    • 84862908644 scopus 로고    scopus 로고
    • Mutant p53 disruptsmammary tissue architecture via the mevalonate pathway
    • Freed-PastorWA, Mizuno H, Zhao X, Langerod A,MoonSH, et al. 2012. Mutant p53 disruptsmammary tissue architecture via the mevalonate pathway. Cell 148:244-58
    • (2012) Cell , vol.148 , pp. 244-258
    • Freed-Pastor, W.A.1    Mizuno, H.2    Zhao, X.3    Langerod, A.4    Moon, S.H.5
  • 76
    • 84902108855 scopus 로고    scopus 로고
    • Quantitative temporal viromics: An approach to investigate host-pathogen interaction
    • Weekes MP, Tomasec P, Huttlin EL, Fielding CA, Nusinow D, et al. 2014. Quantitative temporal viromics: an approach to investigate host-pathogen interaction. Cell 157:1460-72
    • (2014) Cell , vol.157 , pp. 1460-1472
    • Weekes, M.P.1    Tomasec, P.2    Huttlin, E.L.3    Fielding, C.A.4    Nusinow, D.5
  • 77
    • 84901647915 scopus 로고    scopus 로고
    • Two novel human cytomegalovirus NK cell evasion functions target MICA for lysosomal degradation
    • Fielding CA, Aicheler R, Stanton RJ, Wang EC, Han S, et al. 2014. Two novel human cytomegalovirus NK cell evasion functions target MICA for lysosomal degradation. PLOS Pathog. 10:e1004058
    • (2014) PLOS Pathog , vol.10 , pp. e1004058
    • Fielding, C.A.1    Aicheler, R.2    Stanton, R.J.3    Wang, E.C.4    Han, S.5
  • 78
    • 84929459975 scopus 로고    scopus 로고
    • Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation byHCMV US2 in cooperation with UL141
    • Hsu JL, van Boomen DJ, Tomasec P, Weekes MP, Antrobus R, et al. 2015. Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation byHCMV US2 in cooperation with UL141. PLOS Pathog. 11:e1004811
    • (2015) PLOS Pathog , vol.11 , pp. e1004811
    • Hsu, J.L.1    Van Boomen, D.J.2    Tomasec, P.3    Weekes, M.P.4    Antrobus, R.5
  • 79
    • 85015349205 scopus 로고    scopus 로고
    • Phosphoantigen presentation to TCR γδ cells, a conundrum getting less gray zones
    • De Libero G, Lau SY, Mori L. 2014. Phosphoantigen presentation to TCR γδ cells, a conundrum getting less gray zones. Front. Immunol. 5:679
    • (2014) Front. Immunol , vol.5 , pp. 679
    • De Libero, G.1    Lau, S.Y.2    Mori, L.3
  • 80
    • 85015355989 scopus 로고    scopus 로고
    • Molecules and mechanisms implicated in the peculiar antigenic activation process of human Vγ9Vδ2 T cells
    • Harly C, Peigne CM, Scotet E. 2014. Molecules and mechanisms implicated in the peculiar antigenic activation process of human Vγ9Vδ2 T cells. Front. Immunol. 5:657
    • (2014) Front. Immunol , vol.5 , pp. 657
    • Harly, C.1    Peigne, C.M.2    Scotet, E.3
  • 81
    • 84919467566 scopus 로고    scopus 로고
    • The Vγ9Vδ2 T cell antigen receptor and butyrophilin-3 A1: Models of interaction, the possibility of co-evolution, and the case of dendritic epidermal T cells
    • Karunakaran MM, Herrmann T. 2014. The Vγ9Vδ2 T cell antigen receptor and butyrophilin-3 A1: models of interaction, the possibility of co-evolution, and the case of dendritic epidermal T cells. Front. Immunol. 5:648
    • (2014) Front. Immunol , vol.5 , pp. 648
    • Karunakaran, M.M.1    Herrmann, T.2
  • 82
    • 84939513492 scopus 로고    scopus 로고
    • Sensing of pyrophosphate metabolites by Vγ9V and delta 2 T cells
    • Gu S, NawrockaW, Adams EJ. 2014. Sensing of pyrophosphate metabolites by Vγ9V and delta 2 T cells. Front. Immunol. 5:688
    • (2014) Front. Immunol , vol.5 , pp. 688
    • Gu, S.1    Nawrocka, W.2    Adams, E.J.3
  • 84
    • 84887281193 scopus 로고    scopus 로고
    • MAIT cells detect and efficiently lyse bacterially-infected epithelial cells
    • Le Bourhis L, Dusseaux M, Bohineust A, Bessoles S, Martin E, et al. 2013. MAIT cells detect and efficiently lyse bacterially-infected epithelial cells. PLOS Pathog. 9:e1003681
    • (2013) PLOS Pathog , vol.9 , pp. e1003681
    • Le Bourhis, L.1    Dusseaux, M.2    Bohineust, A.3    Bessoles, S.4    Martin, E.5
  • 85
    • 84871312235 scopus 로고    scopus 로고
    • Co-dependents: MR1-restricted MAIT cells and their antimicrobial function
    • Gold MC, Lewinsohn DM. 2013. Co-dependents: MR1-restricted MAIT cells and their antimicrobial function. Nat. Rev. Microbiol. 11:14-19
    • (2013) Nat. Rev. Microbiol , vol.11 , pp. 14-19
    • Gold, M.C.1    Lewinsohn, D.M.2
  • 86
    • 34447131000 scopus 로고    scopus 로고
    • CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor
    • Borg NA,Wun KS,Kjer-NielsenL,WilceMC,Pellicci DG, et al. 2007. CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor. Nature 448:44-49
    • (2007) Nature , vol.448 , pp. 44-49
    • Borg, N.A.1    Wun, K.S.2    Kjer-Nielsen, L.3    Wilce, M.C.4    Pellicci, D.G.5
  • 87
    • 84880647732 scopus 로고    scopus 로고
    • Butyrophilin 3A1 plays an essential role in prenyl pyrophosphate stimulation of human Vγ9Vδ2 T cells
    • Wang H, Henry O, Distefano MD, Wang YC, Raikkonen J, et al. 2013. Butyrophilin 3A1 plays an essential role in prenyl pyrophosphate stimulation of human Vγ9Vδ2 T cells. J. Immunol. 191:1029-42
    • (2013) J. Immunol , vol.191 , pp. 1029-1042
    • Wang, H.1    Henry, O.2    Distefano, M.D.3    Wang, Y.C.4    Raikkonen, J.5
  • 88
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: A family of versatile cytolinker proteins
    • Leung CL, Green KJ, Liem RK. 2002. Plakins: a family of versatile cytolinker proteins. Trends Cell Biol. 12:37-45
    • (2002) Trends Cell Biol , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.3
  • 89
    • 3042822399 scopus 로고    scopus 로고
    • Plakins: Goliaths that link cell junctions and the cytoskeleton
    • Jefferson JJ, Leung CL, Liem RK. 2004. Plakins: Goliaths that link cell junctions and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 5:542-53
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 542-553
    • Jefferson, J.J.1    Leung, C.L.2    Liem, R.K.3
  • 90
    • 84897055612 scopus 로고    scopus 로고
    • Plakins, a versatile family of cytolinkers: Roles in skin integrity and in human diseases
    • Bouameur JE, Favre B, Borradori L. 2014. Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases. J. Investig. Dermatol. 134:885-94
    • (2014) J. Investig. Dermatol , vol.134 , pp. 885-894
    • Bouameur, J.E.1    Favre, B.2    Borradori, L.3
  • 91
    • 0037115692 scopus 로고    scopus 로고
    • Interaction of periplakin and envoplakin with intermediate filaments
    • Karashima T, Watt FM. 2002. Interaction of periplakin and envoplakin with intermediate filaments. J. Cell Sci. 115:5027-37
    • (2002) J. Cell Sci , vol.115 , pp. 5027-5037
    • Karashima, T.1    Watt, F.M.2
  • 92
    • 34548601698 scopus 로고    scopus 로고
    • Cytolinker cross-talk: Periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration
    • Boczonadi V, McInroy L, Maatta A. 2007. Cytolinker cross-talk: Periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration. Exp. Cell Res. 313:3579-91
    • (2007) Exp. Cell Res , vol.313 , pp. 3579-3591
    • Boczonadi, V.1    McInroy, L.2    Maatta, A.3
  • 93
    • 4444230618 scopus 로고    scopus 로고
    • Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane
    • Groot KR, Sevilla LM,Nishi K, DiColandrea T, Watt FM. 2004. Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane. J. Cell Biol. 166:653-59
    • (2004) J. Cell Biol , vol.166 , pp. 653-659
    • Groot, K.R.1    Sevilla, L.M.2    Nishi, K.3    DiColandrea, T.4    Watt, F.M.5
  • 94
    • 11944249598 scopus 로고    scopus 로고
    • Breaking the connection: Caspase 6 disconnects intermediate filament-binding domain of periplakin from its actin-binding N-terminal region
    • Kalinin AE, Aho M, Uitto J, Aho S. 2005. Breaking the connection: caspase 6 disconnects intermediate filament-binding domain of periplakin from its actin-binding N-terminal region. J. Investig. Dermatol. 124:46-55
    • (2005) J. Investig. Dermatol , vol.124 , pp. 46-55
    • Kalinin, A.E.1    Aho, M.2    Uitto, J.3    Aho, S.4
  • 95
    • 3142685132 scopus 로고    scopus 로고
    • Direct interaction between FcγRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity
    • Beekman JM, Bakema JE, van Winkel JG, Leusen JH. 2004. Direct interaction between FcγRI (CD64) and periplakin controls receptor endocytosis and ligand binding capacity. PNAS 101:10392-97
    • (2004) PNAS , vol.101 , pp. 10392-10397
    • Beekman, J.M.1    Bakema, J.E.2    Van Winkel, J.G.3    Leusen, J.H.4
  • 97
    • 0034735518 scopus 로고    scopus 로고
    • Subcellular distribution of envoplakin and periplakin: Insights into their role as precursors of the epidermal cornified envelope
    • DiColandrea T, Karashima T, Maatta A, Watt FM. 2000. Subcellular distribution of envoplakin and periplakin: insights into their role as precursors of the epidermal cornified envelope. J. Cell Biol. 151:573-86
    • (2000) J. Cell Biol , vol.151 , pp. 573-586
    • DiColandrea, T.1    Karashima, T.2    Maatta, A.3    Watt, F.M.4
  • 98
    • 38049014451 scopus 로고    scopus 로고
    • Mice deficient in involucrin, envoplakin, and periplakin have a defective epidermal barrier
    • Sevilla LM, Nachat R, Groot KR, Klement JF, Uitto J, et al. 2007. Mice deficient in involucrin, envoplakin, and periplakin have a defective epidermal barrier. J. Cell Biol. 179:1599-612
    • (2007) J. Cell Biol , vol.179 , pp. 1599-1612
    • Sevilla, L.M.1    Nachat, R.2    Groot, K.R.3    Klement, J.F.4    Uitto, J.5
  • 99
    • 84899867231 scopus 로고    scopus 로고
    • Epidermal barrier defects link atopic dermatitis with altered skin cancer susceptibility
    • Cipolat S, HosteE,Natsuga K, Quist SR, WattFM.2014. Epidermal barrier defects link atopic dermatitis with altered skin cancer susceptibility. eLife 3:e01888
    • (2014) ELife , vol.3 , pp. e01888
    • Cipolat, S.1    Hoste, E.2    Natsuga, K.3    Quist, S.R.4    Watt, F.M.5
  • 100
    • 79953305850 scopus 로고    scopus 로고
    • The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat
    • Ortega E, Buey RM, Sonnenberg A, de Pereda JM. 2011. The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat. J. Biol. Chem. 286:12429-38
    • (2011) J. Biol. Chem , vol.286 , pp. 12429-12438
    • Ortega, E.1    Buey, R.M.2    Sonnenberg, A.3    De Pereda, J.M.4
  • 101
    • 34249663775 scopus 로고    scopus 로고
    • Increased internalization of p120-uncoupled E-cadherin and a requirement for a dileucine motif in the cytoplasmic domain for endocytosis of the protein
    • Miyashita Y,OzawaM. 2007. Increased internalization of p120-uncoupled E-cadherin and a requirement for a dileucine motif in the cytoplasmic domain for endocytosis of the protein. J. Biol. Chem. 282:11540-48
    • (2007) J. Biol. Chem , vol.282 , pp. 11540-11548
    • Miyashita, Y.1    Ozawa, M.2
  • 102
    • 77950932981 scopus 로고    scopus 로고
    • Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion
    • IshiyamaN, Lee SH, Liu S, Li GY, SmithMJ, et al. 2010. Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion. Cell 141:117-28
    • (2010) Cell , vol.141 , pp. 117-128
    • Ishiyama, N.1    Lee, S.H.2    Liu, S.3    Li, G.Y.4    Smith, M.J.5
  • 103
    • 84866525950 scopus 로고    scopus 로고
    • The molecular basis for modulation of humanVγ9Vδ2Tcell responses byCD277/butyrophilin-3 (BTN3A)-specific antibodies
    • Palakodeti A, Sandstrom A, Sundaresan L, Harly C, Nedellec S, et al. 2012. The molecular basis for modulation of humanVγ9Vδ2Tcell responses byCD277/butyrophilin-3 (BTN3A)-specific antibodies. J. Biol. Chem. 287:32780-90
    • (2012) J. Biol. Chem , vol.287 , pp. 32780-32790
    • Palakodeti, A.1    Sandstrom, A.2    Sundaresan, L.3    Harly, C.4    Nedellec, S.5
  • 104
    • 84892956643 scopus 로고    scopus 로고
    • A test of current models for the mechanism of milk-lipid droplet secretion
    • Jeong J, Lisinski I, Kadegowda AK, Shin H, Wooding FB, et al. 2013. A test of current models for the mechanism of milk-lipid droplet secretion. Traffic 14:974-86
    • (2013) Traffic , vol.14 , pp. 974-986
    • Jeong, J.1    Lisinski, I.2    Kadegowda, A.K.3    Shin, H.4    Wooding, F.B.5
  • 105
    • 3042750635 scopus 로고    scopus 로고
    • Expression of butyrophilin (Btn1a1) in lactatingmammary gland is essential for the regulated secretion ofmilk-lipid droplets
    • Ogg SL, Weldon AK, Dobbie L, Smith AJ, Mather IH. 2004. Expression of butyrophilin (Btn1a1) in lactatingmammary gland is essential for the regulated secretion ofmilk-lipid droplets. PNAS 101:10084-89
    • (2004) PNAS , vol.101 , pp. 10084-10089
    • Ogg, S.L.1    Weldon, A.K.2    Dobbie, L.3    Smith, A.J.4    Mather, I.H.5
  • 106
    • 84902995875 scopus 로고    scopus 로고
    • Phosphoantigens and butyrophilin 3A1 induce similar intracellular activation signaling in human TCRVγ9+ γδT lymphocytes
    • Decaup E, Duault C, Bezombes C, Poupot M, Savina A, et al. 2014. Phosphoantigens and butyrophilin 3A1 induce similar intracellular activation signaling in human TCRVγ9+ γδT lymphocytes. Immunol. Lett. 161:133-37
    • (2014) Immunol. Lett , vol.161 , pp. 133-137
    • Decaup, E.1    Duault, C.2    Bezombes, C.3    Poupot, M.4    Savina, A.5
  • 107
    • 77957865633 scopus 로고    scopus 로고
    • Stimulation of human butyrophilin 3 molecules results in negative regulation of cellular immunity
    • Yamashiro H, Yoshizaki S, Tadaki T, Egawa K, Seo N. 2010. Stimulation of human butyrophilin 3 molecules results in negative regulation of cellular immunity. J. Leukoc. Biol. 88:757-67
    • (2010) J. Leukoc. Biol , vol.88 , pp. 757-767
    • Yamashiro, H.1    Yoshizaki, S.2    Tadaki, T.3    Egawa, K.4    Seo, N.5
  • 108
    • 78649514107 scopus 로고    scopus 로고
    • Ligation of the BT3 molecules, members of the B7 family, enhance the proinflammatory responses of human monocytes and monocytederived dendritic cells
    • Simone R, Barbarat B, Rabellino A, Icardi G, Bagnasco M, et al. 2010. Ligation of the BT3 molecules, members of the B7 family, enhance the proinflammatory responses of human monocytes and monocytederived dendritic cells. Mol. Immunol. 48:109-18
    • (2010) Mol. Immunol , vol.48 , pp. 109-118
    • Simone, R.1    Barbarat, B.2    Rabellino, A.3    Icardi, G.4    Bagnasco, M.5
  • 109
  • 110
    • 0025102648 scopus 로고
    • Cloning and analysis of cDNA encoding bovine butyrophilin, an apical glycoprotein expressed in mammary tissue and secreted in association with the milk-fat globule membrane during lactation
    • Jack LJ, Mather IH. 1990. Cloning and analysis of cDNA encoding bovine butyrophilin, an apical glycoprotein expressed in mammary tissue and secreted in association with the milk-fat globule membrane during lactation. J. Biol. Chem. 265:14481-86
    • (1990) J. Biol. Chem , vol.265 , pp. 14481-14486
    • Jack, L.J.1    Mather, I.H.2
  • 111
    • 0041378062 scopus 로고    scopus 로고
    • Xanthine oxidoreductase is central to the evolution and function of the innate immune system
    • Vorbach C, Harrison R, Capecchi MR. 2003. Xanthine oxidoreductase is central to the evolution and function of the innate immune system. Trends Immunol. 24:512-17
    • (2003) Trends Immunol , vol.24 , pp. 512-517
    • Vorbach, C.1    Harrison, R.2    Capecchi, M.R.3
  • 112
    • 69249126167 scopus 로고    scopus 로고
    • The PRY/SPRY/B30.2 domain of butyrophilin 1A1 (BTN1A1) binds to xanthine oxidoreductase: Implications for the function of BTN1A1 in the mammary gland and other tissues
    • Jeong J, Rao AU, Xu J, Ogg SL, Hathout Y, et al. 2009. The PRY/SPRY/B30.2 domain of butyrophilin 1A1 (BTN1A1) binds to xanthine oxidoreductase: implications for the function of BTN1A1 in the mammary gland and other tissues. J. Biol. Chem. 284:22444-56
    • (2009) J. Biol. Chem , vol.284 , pp. 22444-22456
    • Jeong, J.1    Rao, A.U.2    Xu, J.3    Ogg, S.L.4    Hathout, Y.5
  • 113
    • 84908489221 scopus 로고    scopus 로고
    • Stat3 controls cell death during mammary gland involution by regulating uptake of milk fat globules and lysosomal membrane permeabilization
    • Sargeant TJ, Lloyd-Lewis B, Resemann HK, Ramos-Montoya A, Skepper J, Watson CJ. 2014. Stat3 controls cell death during mammary gland involution by regulating uptake of milk fat globules and lysosomal membrane permeabilization. Nat. Cell Biol. 16:1057-68
    • (2014) Nat. Cell Biol , vol.16 , pp. 1057-1068
    • Sargeant, T.J.1    Lloyd-Lewis, B.2    Resemann, H.K.3    Ramos-Montoya, A.4    Skepper, J.5    Watson, C.J.6
  • 114
    • 0026758255 scopus 로고
    • Myelin/oligodendrocyte glycoprotein is a unique member of the immunoglobulin superfamily
    • Gardinier MV, Amiguet P, Linington C, Matthieu JM. 1992. Myelin/oligodendrocyte glycoprotein is a unique member of the immunoglobulin superfamily. J. Neurosci. Res. 33:177-87
    • (1992) J. Neurosci. Res , vol.33 , pp. 177-187
    • Gardinier, M.V.1    Amiguet, P.2    Linington, C.3    Matthieu, J.M.4
  • 115
    • 0038797820 scopus 로고    scopus 로고
    • Genetic variation in myelin oligodendrocyte glycoprotein expression and susceptibility to experimental autoimmune encephalomyelitis
    • Pagany M, Jagodic M, Bourquin C, Olsson T, Linington C. 2003. Genetic variation in myelin oligodendrocyte glycoprotein expression and susceptibility to experimental autoimmune encephalomyelitis. J. Neuroimmunol. 139:1-8
    • (2003) J. Neuroimmunol , vol.139 , pp. 1-8
    • Pagany, M.1    Jagodic, M.2    Bourquin, C.3    Olsson, T.4    Linington, C.5
  • 116
    • 84881368722 scopus 로고    scopus 로고
    • The spectrum of MOG autoantibody-associated demyelinating diseases
    • Reindl M, Di Pauli F, Rostasy K, Berger T. 2013. The spectrum of MOG autoantibody-associated demyelinating diseases. Nat. Rev. Neurol. 9:455-61
    • (2013) Nat. Rev. Neurol , vol.9 , pp. 455-461
    • Reindl, M.1    Di Pauli, F.2    Rostasy, K.3    Berger, T.4
  • 117
    • 0347364679 scopus 로고    scopus 로고
    • Antibody cross-reactivity between myelin oligodendrocyte glycoprotein and the milk protein butyrophilin in multiple sclerosis
    • Guggenmos J, Schubart AS, Ogg S, Andersson M, Olsson T, et al. 2004. Antibody cross-reactivity between myelin oligodendrocyte glycoprotein and the milk protein butyrophilin in multiple sclerosis. J. Immunol. 172:661-68
    • (2004) J. Immunol , vol.172 , pp. 661-668
    • Guggenmos, J.1    Schubart, A.S.2    Ogg, S.3    Andersson, M.4    Olsson, T.5
  • 118
    • 0027193351 scopus 로고
    • T cells specific for the myelin oligodendrocyte glycoprotein mediate an unusual autoimmune inflammatory response in the central nervous system
    • Linington C, Berger T, Perry L, Weerth S, Hinze-Selch D, et al. 1993. T cells specific for the myelin oligodendrocyte glycoprotein mediate an unusual autoimmune inflammatory response in the central nervous system. Eur. J. Immunol. 23:1364-72
    • (1993) Eur. J. Immunol , vol.23 , pp. 1364-1372
    • Linington, C.1    Berger, T.2    Perry, L.3    Weerth, S.4    Hinze-Selch, D.5
  • 119
    • 85047692323 scopus 로고    scopus 로고
    • Myelin/oligodendrocyte glycoprotein-deficient (MOG-deficient) mice reveal lack of immune tolerance to MOG in wild-type mice
    • Delarasse C, Daubas P, Mars LT, Vizler C, Litzenburger T, et al. 2003. Myelin/oligodendrocyte glycoprotein-deficient (MOG-deficient) mice reveal lack of immune tolerance to MOG in wild-type mice. J. Clin. Investig. 112:544-53
    • (2003) J. Clin. Investig , vol.112 , pp. 544-553
    • Delarasse, C.1    Daubas, P.2    Mars, L.T.3    Vizler, C.4    Litzenburger, T.5
  • 120
    • 0034283668 scopus 로고    scopus 로고
    • Butyrophilin, a milk protein, modulates the encephalitogenic T cell response to myelin oligodendrocyte glycoprotein in experimental autoimmune encephalomyelitis
    • Stefferl A, Schubart A, Storch M, Amini A, Mather I, et al. 2000. Butyrophilin, a milk protein, modulates the encephalitogenic T cell response to myelin oligodendrocyte glycoprotein in experimental autoimmune encephalomyelitis. J. Immunol. 165:2859-65
    • (2000) J. Immunol , vol.165 , pp. 2859-2865
    • Stefferl, A.1    Schubart, A.2    Storch, M.3    Amini, A.4    Mather, I.5
  • 121
    • 0036773624 scopus 로고    scopus 로고
    • Multiple sclerosis candidate autoantigens except myelin oligodendrocyte glycoprotein are transcribed in human thymus
    • Bruno R, Sabater L, Sospedra M, Ferrer-Francesch X, Escudero D, et al. 2002. Multiple sclerosis candidate autoantigens except myelin oligodendrocyte glycoprotein are transcribed in human thymus. Eur. J. Immunol. 32:2737-47
    • (2002) Eur. J. Immunol , vol.32 , pp. 2737-2747
    • Bruno, R.1    Sabater, L.2    Sospedra, M.3    Ferrer-Francesch, X.4    Escudero, D.5
  • 122
    • 84903777311 scopus 로고    scopus 로고
    • CNS myelin induces regulatory functions of DC-SIGN-expressing, antigen-presenting cells via cognate interaction withMOG
    • Garcia-Vallejo JJ, Ilarregui JM, Kalay H, Chamorro S, Koning N, et al. 2014. CNS myelin induces regulatory functions of DC-SIGN-expressing, antigen-presenting cells via cognate interaction withMOG. J. Exp. Med. 211:1465-83
    • (2014) J. Exp. Med , vol.211 , pp. 1465-1483
    • Garcia-Vallejo, J.J.1    Ilarregui, J.M.2    Kalay, H.3    Chamorro, S.4    Koning, N.5
  • 123
    • 0033959287 scopus 로고    scopus 로고
    • Ermap, a gene coding for a novel erythroid specific adhesion/receptor membrane protein
    • Ye TZ, Gordon CT, Lai YH, Fujiwara Y, Peters LL, et al. 2000. Ermap, a gene coding for a novel erythroid specific adhesion/receptor membrane protein. Gene 242:337-45
    • (2000) Gene , vol.242 , pp. 337-345
    • Ye, T.Z.1    Gordon, C.T.2    Lai, Y.H.3    Fujiwara, Y.4    Peters, L.L.5
  • 125
    • 0037438591 scopus 로고    scopus 로고
    • Scianna antigens including Rd are expressed by ERMAP
    • Wagner FF, Poole J, FlegelWA. 2003. Scianna antigens including Rd are expressed by ERMAP. Blood 101:752-7
    • (2003) Blood , vol.101 , pp. 752-757
    • Wagner, F.F.1    Poole, J.2    Flegel, W.A.3
  • 126
    • 0026012596 scopus 로고
    • The B-G multigene family of the chicken major histocompatibility complex
    • Kaufman J, Skjodt K, Salomonsen J. 1991. The B-G multigene family of the chicken major histocompatibility complex. Crit. Rev. Immunol. 11:113-43
    • (1991) Crit. Rev. Immunol , vol.11 , pp. 113-143
    • Kaufman, J.1    Skjodt, K.2    Salomonsen, J.3
  • 127
    • 0026804865 scopus 로고
    • B-G: We know what it is, but what does it do?
    • Kaufman J, Salomonsen J. 1992. B-G: we know what it is, but what does it do? Immunol. Today 13:1-3
    • (1992) Immunol. Today , vol.13 , pp. 1-3
    • Kaufman, J.1    Salomonsen, J.2
  • 128
    • 84903489675 scopus 로고    scopus 로고
    • Sequence of a complete chicken BG haplotype shows dynamic expansion and contraction of two gene lineages with particular expression patterns
    • Salomonsen J, Chattaway JA, Chan AC, Parker A,Huguet S, et al. 2014. Sequence of a complete chicken BG haplotype shows dynamic expansion and contraction of two gene lineages with particular expression patterns. PLOS Genet. 10:e1004417
    • (2014) PLOS Genet , vol.10 , pp. e1004417
    • Salomonsen, J.1    Chattaway, J.A.2    Chan, A.C.3    Parker, A.4    Huguet, S.5
  • 129
    • 0026100431 scopus 로고
    • Chicken major histocompatibility complex-encoded B-G antigens are found on many cell types that are important for the immune system
    • Salomonsen J, DunonD, Skjodt K, Thorpe D, Vainio O, Kaufman J. 1991. Chicken major histocompatibility complex-encoded B-G antigens are found on many cell types that are important for the immune system. PNAS 88:1359-63
    • (1991) PNAS , vol.88 , pp. 1359-1363
    • Salomonsen, J.1    Dunon, D.2    Skjodt, K.3    Thorpe, D.4    Vainio, O.5    Kaufman, J.6
  • 130
    • 0026029176 scopus 로고
    • The "adjuvant effect" of the polymorphic B-G antigens of the chicken major histocompatibility complex analyzed using purified molecules incorporated in liposomes
    • Salomonsen J, Eriksson H, Skjodt K, Lundgreen T, Simonsen M, Kaufman J. 1991. The "adjuvant effect" of the polymorphic B-G antigens of the chicken major histocompatibility complex analyzed using purified molecules incorporated in liposomes. Eur. J. Immunol. 21:649-58
    • (1991) Eur. J. Immunol , vol.21 , pp. 649-658
    • Salomonsen, J.1    Eriksson, H.2    Skjodt, K.3    Lundgreen, T.4    Simonsen, M.5    Kaufman, J.6
  • 131
    • 70349745517 scopus 로고    scopus 로고
    • BG1 has a major role in MHC-linked resistance to malignant lymphoma in the chicken
    • Goto RM, Wang Y, Taylor RL Jr, Wakenell PS, Hosomichi K, et al. 2009. BG1 has a major role in MHC-linked resistance to malignant lymphoma in the chicken. PNAS 106:16740-45
    • (2009) PNAS , vol.106 , pp. 16740-16745
    • Goto, R.M.1    Wang, Y.2    Taylor, R.L.3    Wakenell, P.S.4    Hosomichi, K.5
  • 132
    • 23244435781 scopus 로고    scopus 로고
    • The receptor for the subgroup C avian sarcoma and leukosis viruses, Tvc, is related to mammalian butyrophilins, members of the immunoglobulin superfamily
    • Elleder D, Stepanets V, Melder DC, Senigl F, Geryk J, et al. 2005. The receptor for the subgroup C avian sarcoma and leukosis viruses, Tvc, is related to mammalian butyrophilins, members of the immunoglobulin superfamily. J. Virol. 79:10408-19
    • (2005) J. Virol , vol.79 , pp. 10408-10419
    • Elleder, D.1    Stepanets, V.2    Melder, D.C.3    Senigl, F.4    Geryk, J.5
  • 135
    • 0032736029 scopus 로고    scopus 로고
    • B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation and interleukin-10 secretion
    • Dong H, Zhu G, Tamada K, Chen L. 1999. B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation and interleukin-10 secretion. Nat. Med. 5:1365-69
    • (1999) Nat. Med , vol.5 , pp. 1365-1369
    • Dong, H.1    Zhu, G.2    Tamada, K.3    Chen, L.4


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