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Volumn 289, Issue 21, 2014, Pages 14434-14447

New insights into the DT40 B cell receptor cluster using a proteomic proximity labeling assay

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84901421222     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.529578     Document Type: Article
Times cited : (103)

References (72)
  • 1
    • 84859354949 scopus 로고    scopus 로고
    • B-cell receptor: From resting state to activate
    • Treanor, B. (2012) B-cell receptor: from resting state to activate. Immunology 136, 21-27
    • (2012) Immunology , vol.136 , pp. 21-27
    • Treanor, B.1
  • 2
    • 0037329199 scopus 로고    scopus 로고
    • Visualizing lipid raft dynamics and early signaling events during antigen receptor-mediated B-lymphocyte activation
    • DOI 10.1091/mbc.02-05-0078
    • Gupta, N., and DeFranco, A. L. (2003) Visualizing lipid raft dynamics and early signaling events during antigen receptor-mediated B-lymphocyte activation. Mol. Biol. Cell 14, 432-444 (Pubitemid 36237007)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.2 , pp. 432-444
    • Gupta, N.1    DeFranco, A.L.2
  • 3
    • 18244406506 scopus 로고    scopus 로고
    • Plasticity of B cell receptor internalization upon conditional depletion of clathrin
    • DOI 10.1091/mbc.E05-01-0025
    • Stoddart, A., Jackson, A. P., and Brodsky, F. M. (2005) Plasticity of B cell receptor internalization upon conditional depletion of clathrin. Mol. Biol. Cell 16, 2339-2348 (Pubitemid 40632216)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.5 , pp. 2339-2348
    • Stoddart, A.1    Jackson, A.P.2    Brodsky, F.M.3
  • 4
    • 0030831199 scopus 로고    scopus 로고
    • The complexity of signaling pathways activated by the Bcr
    • DeFranco, A. L. (1997) The complexity of signaling pathways activated by the Bcr. Curr. Opin. Immunol. 9, 296-308
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 296-308
    • Defranco, A.L.1
  • 5
    • 60649093057 scopus 로고    scopus 로고
    • Biochemical and proteomic approaches for the study of membrane microdomains
    • Zheng, Y. Z., and Foster, L. J. (2009) Biochemical and proteomic approaches for the study of membrane microdomains. J. Proteomics 72, 12-22
    • (2009) J. Proteomics , vol.72 , pp. 12-22
    • Zheng, Y.Z.1    Foster, L.J.2
  • 6
    • 70350354671 scopus 로고    scopus 로고
    • The molecular assembly and organization of signaling active B-cell receptor oligomers
    • Tolar, P., Sohn, H. W., Liu, W., and Pierce, S. K. (2009) The molecular assembly and organization of signaling active B-cell receptor oligomers. Immunol. Rev. 232, 34-41
    • (2009) Immunol. Rev. , vol.232 , pp. 34-41
    • Tolar, P.1    Sohn, H.W.2    Liu, W.3    Pierce, S.K.4
  • 7
    • 40549140726 scopus 로고    scopus 로고
    • Proteomic approaches to the analysis of multiprotein signaling complexes
    • DOI 10.1002/pmic.200700650
    • Yang, W., Steen, H., and Freeman, M. R. (2008) Proteomic approaches to the analysis of multiprotein signaling complexes. Proteomics 8, 832-851 (Pubitemid 351362938)
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 832-851
    • Yang, W.1    Steen, H.2    Freeman, M.R.3
  • 8
    • 84855463114 scopus 로고    scopus 로고
    • A proteomics approach to the cell-surface interactome using the enzyme-mediated activation of radical sources reaction
    • Jiang, S., Kotani, N., Ohnishi, T., Miyagawa-Yamguchi, A., Tsuda, M., Yamashita, R., Ishiura, Y., and Honke, K. (2012) A proteomics approach to the cell-surface interactome using the enzyme-mediated activation of radical sources reaction. Proteomics 12, 54-62
    • (2012) Proteomics , vol.12 , pp. 54-62
    • Jiang, S.1    Kotani, N.2    Ohnishi, T.3    Miyagawa-Yamguchi, A.4    Tsuda, M.5    Yamashita, R.6    Ishiura, Y.7    Honke, K.8
  • 9
    • 84874956967 scopus 로고    scopus 로고
    • Proteomic mapping of mitochondria in livingcells via spatially restricted enzymatic tagging
    • Rhee, H. W., Zou, P., Udeshi, N. D., Martell, J. D., Mootha, V. K., Carr, S. A., and Ting, A. Y. (2013) Proteomic mapping of mitochondria in livingcells via spatially restricted enzymatic tagging. Science 339, 1328-1331
    • (2013) Science , vol.339 , pp. 1328-1331
    • Rhee, H.W.1    Zou, P.2    Udeshi, N.D.3    Martell, J.D.4    Mootha, V.K.5    Carr, S.A.6    Ting, A.Y.7
  • 10
    • 0025936509 scopus 로고
    • Increased ratio of targeted to random integration after transfection of chicken B cell lines
    • Buerstedde, J. M., and Takeda, S. (1991) Increased ratio of targeted to random integration after transfection of chicken B cell lines. Cell 67, 179-188 (Pubitemid 121001434)
    • (1991) Cell , vol.67 , Issue.1 , pp. 179-188
    • Buerstedde, J.-M.1    Takeda, S.2
  • 11
    • 0028980409 scopus 로고
    • Requirement of phospholipase C- γ 2 activation in surface immunoglobulin M-induced B cell apoptosis
    • Takata, M., Homma, Y., and Kurosaki, T. (1995) Requirement of phospholipase C- γ 2 activation in surface immunoglobulin M-induced B cell apoptosis. J. Exp. Med. 182, 907-914
    • (1995) J. Exp. Med. , vol.182 , pp. 907-914
    • Takata, M.1    Homma, Y.2    Kurosaki, T.3
  • 12
    • 3242656574 scopus 로고    scopus 로고
    • Analysis of B-cell signaling using Dt40 B-cell line
    • Yasuda, T., and Yamamoto, T. (2004) Analysis of B-cell signaling using Dt40 B-cell line. Methods Mol. Biol. 271, 261-270
    • (2004) Methods Mol. Biol. , vol.271 , pp. 261-270
    • Yasuda, T.1    Yamamoto, T.2
  • 14
    • 0038275858 scopus 로고    scopus 로고
    • The B cell-specific major raft protein, Raftlin, is necessary for the integrity of lipid raft and BCR signal transduction
    • DOI 10.1093/emboj/cdg293
    • Saeki, K., Miura, Y., Aki, D., Kurosaki, T., and Yoshimura, A. (2003) The B cell-specific major raft protein, Raftlin, is necessary for the integrity of lipid raft and Bcr signal transduction. EMBO J. 22, 3015-3026 (Pubitemid 36758622)
    • (2003) EMBO Journal , vol.22 , Issue.12 , pp. 3015-3026
    • Saeki, K.1    Miura, Y.2    Aki, D.3    Kurosaki, T.4    Yoshimura, A.5
  • 16
    • 0029899771 scopus 로고    scopus 로고
    • Chicken B-cell marker chB6 (Bu-1) is a highly glycosylated protein of unique structure
    • DOI 10.1007/s002510050113
    • Tregaskes, C. A., Bumstead, N., Davison, T. F., and Young, J. R. (1996) Chicken B-cell marker Chb6 (Bu-1) is a highly glycosylated protein of unique structure. Immunogenetics 44, 212-217 (Pubitemid 26225914)
    • (1996) Immunogenetics , vol.44 , Issue.3 , pp. 212-217
    • Tregaskes, C.A.1    Bumstead, N.2    Davison, T.F.3    Young, J.R.4
  • 17
    • 10044276833 scopus 로고    scopus 로고
    • New water-soluble phosphines as reductants of peptide and protein disulfide bonds: Reactivity and membrane permeability
    • DOI 10.1021/bi048329a
    • Cline, D. J., Redding, S. E., Brohawn, S. G., Psathas, J. N., Schneider, J. P., and Thorpe, C. (2004) New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability. Biochemistry 43, 15195-15203 (Pubitemid 39602180)
    • (2004) Biochemistry , vol.43 , Issue.48 , pp. 15195-15203
    • Cline, D.J.1    Redding, S.E.2    Brohawn, S.G.3    Psathas, J.N.4    Schneider, J.P.5    Thorpe, C.6
  • 18
    • 0033081775 scopus 로고    scopus 로고
    • Signal amplification in flow cytometry using biotin tyramine
    • DOI 10.1002/(SICI)1097-0320(19990201)35:2<176::AID-CYTO10>3.0.CO;2- S
    • Earnshaw, J. C., and Osbourn, J. K. (1999) Signal amplification in flow cytometry using biotin tyramine. Cytometry 35, 176-179 (Pubitemid 29053255)
    • (1999) Cytometry , vol.35 , Issue.2 , pp. 176-179
    • Earnshaw, J.C.1    Osbourn, J.K.2
  • 19
    • 79961189743 scopus 로고    scopus 로고
    • Method for suppressing non-specific protein interactions observed with affinity resins
    • Rees, J. S., and Lilley, K. S. (2011) Method for suppressing non-specific protein interactions observed with affinity resins. Methods 54, 407-412
    • (2011) Methods , vol.54 , pp. 407-412
    • Rees, J.S.1    Lilley, K.S.2
  • 21
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • DOI 10.1074/mcp.M500061-MCP200
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T., Nagasu, T., Rappsilber, J., and Mann, M. (2005) Exponentially modified protein abundance index (Empai) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 4, 1265-1272 (Pubitemid 41448714)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 22
    • 0023856621 scopus 로고
    • Monoclonal antibodies against chicken Bu-la and Bu-lb alloantigens
    • Veromaa, T., Vainio, O., Eerola, E., and Toivanen, P. (1988) Monoclonal antibodies against chicken Bu-1a and Bu-1b alloantigens. Hybridoma 7, 41-48 (Pubitemid 18077663)
    • (1988) Hybridoma , vol.7 , Issue.1 , pp. 41-48
    • Veromaa, T.1    Vainio, O.2    Eerola, E.3    Toivanen, P.4
  • 23
    • 1542313888 scopus 로고    scopus 로고
    • Requirement for TRAF3 in Signaling by LMP1 but Not CD40 in B Lymphocytes
    • DOI 10.1084/jem.20031255
    • Xie, P., Hostager, B. S., and Bishop, G. A. (2004) Requirement for Traf3 in signaling by Lmp1 but not Cd40 in B lymphocytes. J. Exp. Med. 199, 661-671 (Pubitemid 38316433)
    • (2004) Journal of Experimental Medicine , vol.199 , Issue.5 , pp. 661-671
    • Xie, P.1    Hostager, B.S.2    Bishop, G.A.3
  • 24
    • 38849202566 scopus 로고    scopus 로고
    • Identification of the avian B-cell-specific Bu-1 alloantigen by a novel monoclonal antibody
    • DOI 10.3382/ps.2007-00365
    • Igyártó, B. Z., Nagy, N., Magyar, A., and Oláh, I. (2008) Identification of the avian B-cell-specific Bu-1 alloantigen by a novel monoclonal antibody. Poult. Sci. 87, 351-355 (Pubitemid 351198502)
    • (2008) Poultry Science , vol.87 , Issue.2 , pp. 351-355
    • Igyarto, B.Z.1    Nagy, N.2    Magyar, A.3    Olah, I.4
  • 25
    • 60049093598 scopus 로고    scopus 로고
    • Blobfinder: A tool for fluorescence microscopy image cytometry
    • Allalou, A., and Wählby, C. (2009) Blobfinder: A tool for fluorescence microscopy image cytometry. Comput. Methods Programs Biomed. 94, 58-65
    • (2009) Comput. Methods Programs Biomed. , vol.94 , pp. 58-65
    • Allalou, A.1    Wählby, C.2
  • 26
    • 84864386788 scopus 로고    scopus 로고
    • Mapping of potent and specific binding motifs, Glogen and Gvogea, for integrinα1α1 using collagen toolkits Ii and Iii
    • Hamaia, S. W., Pugh, N., Raynal, N., Némoz, B., Stone, R., Gullberg, D., Bihan, D., and Farndale, R. W. (2012) Mapping of potent and specific binding motifs, Glogen and Gvogea, for integrinα1α1 using collagen toolkits Ii and Iii. J. Biol. Chem. 287, 26019-26028
    • (2012) J. Biol. Chem. , vol.287 , pp. 26019-26028
    • Hamaia, S.W.1    Pugh, N.2    Raynal, N.3    Némoz, B.4    Stone, R.5    Gullberg, D.6    Bihan, D.7    Farndale, R.W.8
  • 27
    • 0024852342 scopus 로고
    • Catalyzed reporter deposition, a novel method of signal amplification. Application to immunoassays
    • DOI 10.1016/0022-1759(89)90104-X
    • Bobrow, M. N., Harris, T. D., Shaughnessy, K. J., and Litt, G. J. (1989) Catalyzed reporter deposition: A novel method of signal amplification. Application to immunoassays. J. Immunol. Methods 125, 279-285 (Pubitemid 20018033)
    • (1989) Journal of Immunological Methods , vol.125 , Issue.1-2 , pp. 279-285
    • Bobrow, M.N.1    Harris, T.D.2    Shaughnessy, K.J.3    Litt, G.J.4
  • 28
    • 6344274704 scopus 로고    scopus 로고
    • The B lymphocyte adaptor molecule of 32 kilodaltons (Bam32) regulates B cell antigen receptor internalization
    • Niiro, H., Allam, A., Stoddart, A., Brodsky, F. M., Marshall, A. J., and Clark, E. A. (2004) The B lymphocyte adaptor molecule of 32 kilodaltons (Bam32) regulates B cell antigen receptor internalization. J. Immunol. 173, 5601-5609 (Pubitemid 39392147)
    • (2004) Journal of Immunology , vol.173 , Issue.9 , pp. 5601-5609
    • Niiro, H.1    Allam, A.2    Stoddart, A.3    Brodsky, F.M.4    Marshall, A.J.5    Clark, E.A.6
  • 29
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • DOI 10.1074/mcp.M500190-MCP200
    • Gruhler, A., Schulze, W. X., Matthiesen, R., Mann, M., and Jensen, O. N. (2005) Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. Mol. Cell. Proteomics 4, 1697-1709 (Pubitemid 41749263)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.11 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3    Mann, M.4    Jensen, O.N.5
  • 30
    • 70449462623 scopus 로고    scopus 로고
    • Rho Gtpase Cdc42 is essential for B-lymphocyte development and activation
    • Guo, F., Velu, C. S., Grimes, H. L., and Zheng, Y. (2009) Rho Gtpase Cdc42 is essential for B-lymphocyte development and activation. Blood 114, 2909-2916
    • (2009) Blood , vol.114 , pp. 2909-2916
    • Guo, F.1    Velu, C.S.2    Grimes, H.L.3    Zheng, Y.4
  • 31
    • 1242338896 scopus 로고    scopus 로고
    • The avian chB6 alloantigen induces apoptosis in DT40 B cells
    • DOI 10.1016/j.cellimm.2003.11.009
    • Funk, P. E., Pifer, J., Kharas, M., Crisafi, G., and Johnson, A. (2003) The avian Chb6 alloantigen induces apoptosis in Dt40 B cells. Cell. Immunol. 226, 95-104 (Pubitemid 38220836)
    • (2003) Cellular Immunology , vol.226 , Issue.2 , pp. 95-104
    • Funk, P.E.1    Pifer, J.2    Kharas, M.3    Crisafi, G.4    Johnson, A.5
  • 32
    • 0035028703 scopus 로고    scopus 로고
    • Floating the raft hypothesis: The roles of lipid rafts in B cell antigen receptor function
    • DOI 10.1006/smim.2000.0302
    • Cheng, P. C., Cherukuri, A., Dykstra, M., Malapati, S., Sproul, T., Chen, M. R., and Pierce, S. K. (2001) Floating the raft hypothesis: the roles of lipid rafts in B cell antigen receptor function. Semin. Immunol. 13, 107-114 (Pubitemid 32382332)
    • (2001) Seminars in Immunology , vol.13 , Issue.2 , pp. 107-114
    • Cheng, P.C.1    Cherukuri, A.2    Dykstra, M.3    Malapati, S.4    Sproul, T.5    Chen, M.R.6    Pierce, S.K.7
  • 33
    • 0036800489 scopus 로고    scopus 로고
    • Lipid rafts unite signaling cascades with clathrin to regulate BCR internalization
    • DOI 10.1016/S1074-7613(02)00416-8
    • Stoddart, A., Dykstra, M. L., Brown, B. K., Song, W., Pierce, S. K., and Brodsky, F. M. (2002) Lipid rafts unite signaling cascades with clathrin to regulate Bcr internalization. Immunity 17, 451-462 (Pubitemid 35223534)
    • (2002) Immunity , vol.17 , Issue.4 , pp. 451-462
    • Stoddart, A.1    Dykstra, M.L.2    Brown, B.K.3    Song, W.4    Pierce, S.K.5    Brodsky, F.M.6
  • 35
    • 0347990658 scopus 로고    scopus 로고
    • Dynamic control of b lymphocyte development in the bursa of fabricius
    • Funk, P. E., and Palmer, J. L. (2003) Dynamic control of B lymphocyte development in the bursa of fabricius. Arch. Immunol. Ther. Exp. 51, 389-398 (Pubitemid 38044449)
    • (2003) Archivum Immunologiae et Therapiae Experimentalis , vol.51 , Issue.6 , pp. 389-398
    • Funk, P.E.1    Palmer, J.L.2
  • 37
    • 84862221167 scopus 로고    scopus 로고
    • Smart 7: Recent updates to the protein domain annotation resource
    • Letunic, I., Doerks, T., and Bork, P. (2012) Smart 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40, D302-D305
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 38
    • 0037438349 scopus 로고    scopus 로고
    • Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling
    • Fragoso, R., Ren, D., Zhang, X., Su, M. W., Burakoff, S. J., and Jin, Y. J. (2003) Lipid raft distribution of Cd4 depends on its palmitoylation and association with Lck, and evidence for Cd4-induced lipid raft aggregation as an additional mechanism to enhance Cd3 signaling. J. Immunol. 170, 913-921 (Pubitemid 36070545)
    • (2003) Journal of Immunology , vol.170 , Issue.2 , pp. 913-921
    • Fragoso, R.1    Ren, D.2    Zhang, X.3    Wei-Chih Su, M.4    Burakoff, S.J.5    Jin, Y.-J.6
  • 39
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
    • DOI 10.1016/0968-0004(94)90129-5
    • Feller, S. M., Ren, R., Hanafusa, H., and Baltimore, D. (1994) Sh2 and Sh3 domains as molecular adhesives: the interactions of Crk and Abl. Trends Biochem. Sci. 19, 453-458 (Pubitemid 24342756)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.11 , pp. 453-458
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 40
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • DOI 10.1016/S0968-0004(98)01298-5, PII S0968000498012985
    • Altschul, S. F., and Koonin, E. V. (1998) Iterated profile searches with Psi-Blast: A tool for discovery in protein databases. Trends Biochem. Sci. 23, 444-447 (Pubitemid 28540746)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.11 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 41
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • DOI 10.1006/jmbi.2001.4762
    • Shi, J., Blundell, T. L., and Mizuguchi, K. (2001) Fugue: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310, 243-257 (Pubitemid 32619966)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.1 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 43
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 44
    • 49649087786 scopus 로고    scopus 로고
    • Regulation of integrin activation through the B-cell receptor
    • Arana, E., Harwood, N. E., and Batista, F. D. (2008) Regulation of integrin activation through the B-cell receptor. J. Cell Sci. 121, 2279-2286
    • (2008) J. Cell Sci. , vol.121 , pp. 2279-2286
    • Arana, E.1    Harwood, N.E.2    Batista, F.D.3
  • 45
    • 0031841822 scopus 로고    scopus 로고
    • Identification of a proline-rich sequence in the CD2 cytoplasmic domain critical for regulation of integrin-mediated adhesion and activation of phosphoinositide 3-kinase
    • Kivens, W. J., Hunt, S. W., 3rd, Mobley, J. L., Zell, T., Dell, C. L., Bierer, B. E., and Shimizu, Y. (1998) Identification of a proline-rich sequence in the Cd2 cytoplasmic domain critical for regulation of integrin-mediated adhesion and activation of phosphoinositide 3-kinase. Mol. Cell. Biol. 18, 5291-5307 (Pubitemid 28388113)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 5291-5307
    • Kivens, W.J.1    Hunt III, S.W.2    Mobley, J.L.3    Zell, T.4    Dell, C.L.5    Bierer, B.E.6    Shimizu, Y.7
  • 46
    • 0024828456 scopus 로고
    • Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes
    • DOI 10.1038/342811a0
    • van Kooyk, Y., van de Wiel-van Kemenade, P., Weder, P., Kuijpers, T. W., and Figdor, C. G. (1989) Enhancement of Lfa-1-mediated cell adhesion by triggering through Cd2 or Cd3 on T Lymphocytes. Nature 342, 811-813 (Pubitemid 20023816)
    • (1989) Nature , vol.342 , Issue.6251 , pp. 811-813
    • Van Kooyk, Y.1    Van De Wiel-Van Kemenade, P.2    Weder, P.3    Kuijpers, T.W.4    Figdor, C.G.5
  • 47
    • 7044224479 scopus 로고    scopus 로고
    • Physiological and pathological roles of α3 β 1 integrin
    • Tsuji, T. (2004) Physiological and pathological roles of α3 β 1 integrin. J. Membr. Biol. 200, 115-132
    • (2004) J. Membr. Biol. , vol.200 , pp. 115-132
    • Tsuji, T.1
  • 48
    • 0033040483 scopus 로고    scopus 로고
    • Amplification methods to increase the sensitivity of in situ hybridization: Play CARD(s)
    • Speel, E. J., Hopman, A. H., and Komminoth, P. (1999) Amplification methods to increase the sensitivity of in situ hybridization: play card(S). J. Histochem. Cytochem. 47, 281-288 (Pubitemid 29102659)
    • (1999) Journal of Histochemistry and Cytochemistry , vol.47 , Issue.3 , pp. 281-288
    • Speel, E.J.M.1    Hopman, A.H.N.2    Komminoth, P.3
  • 49
    • 3543115049 scopus 로고    scopus 로고
    • Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attack. A proteomic study using a tyrosylating fluorophore
    • DOI 10.1002/pmic.200300755
    • Avram, D., Romijn, E. P., Pap, E. H., Heck, A. J., and Wirtz, K. W. (2004) Identification of proteins in activated human neutrophils susceptible to tyrosyl radical attack: A proteomic study using a tyrosylating fluorophore. Proteomics 4, 2397-2407 (Pubitemid 39025341)
    • (2004) Proteomics , vol.4 , Issue.8 , pp. 2397-2407
    • Avram, D.1    Romijn, E.P.2    Pap, E.H.W.3    Heck, A.J.R.4    Wirtz, K.W.A.5
  • 50
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
    • Roux, K. J., Kim, D. I., Raida, M., and Burke, B. (2012) A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J. Cell Biol. 196, 801-810
    • (2012) J. Cell Biol. , vol.196 , pp. 801-810
    • Roux, K.J.1    Kim, D.I.2    Raida, M.3    Burke, B.4
  • 51
    • 0030808731 scopus 로고    scopus 로고
    • Signal amplification at the ultrastructural level using biotinylated tyramides and immunogold detection
    • DOI 10.1007/s004180050171
    • Schöfer, C., Weipoltshammer, K., Almeder, M., and Wachtler, F. (1997) Signal amplification at the ultrastructural level using biotinylated tyramides and immunogold detection. Histochem. Cell Biol. 108, 313-319 (Pubitemid 27468132)
    • (1997) Histochemistry and Cell Biology , vol.108 , Issue.4-5 , pp. 313-319
    • Schofer, C.1    Weipoltshammer, K.2    Almeder, M.3    Wachtler, F.4
  • 52
    • 79956307046 scopus 로고    scopus 로고
    • Regulation of Bcr signaling
    • Kurosaki, T. (2011) Regulation of Bcr signaling. Mol. Immunol. 48, 1287-1291
    • (2011) Mol. Immunol. , vol.48 , pp. 1287-1291
    • Kurosaki, T.1
  • 53
    • 79953010049 scopus 로고    scopus 로고
    • Proteomic characterization of plasma membrane-proximal T cell activation responses
    • de Wet, B., Zech, T., Salek, M., Acuto, O., and Harder, T. (2011) Proteomic characterization of plasma membrane-proximal T cell activation responses. J. Biol. Chem. 286, 4072-4080
    • (2011) J. Biol. Chem. , vol.286 , pp. 4072-4080
    • De Wet, B.1    Zech, T.2    Salek, M.3    Acuto, O.4    Harder, T.5
  • 54
    • 33744494534 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics
    • DOI 10.1038/ni1337, PII N1337
    • Gupta, N., Wollscheid, B., Watts, J. D., Scheer, B., Aebersold, R., and De Franco, A. L. (2006) Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics. Nat. Immunol. 7, 625-633 (Pubitemid 43797344)
    • (2006) Nature Immunology , vol.7 , Issue.6 , pp. 625-633
    • Gupta, N.1    Wollscheid, B.2    Watts, J.D.3    Scheer, B.4    Aebersold, R.5    DeFranco, A.L.6
  • 55
    • 12344318370 scopus 로고    scopus 로고
    • RhoA GTPase regulates B cell receptor signaling
    • DOI 10.1016/j.molcel.2004.12.012, PII S1097276504007683
    • Saci, A., and Carpenter, C. L. (2005) RhoA GTPase regulates B cell receptor signaling. Mol. Cell 17, 205-214 (Pubitemid 40138616)
    • (2005) Molecular Cell , vol.17 , Issue.2 , pp. 205-214
    • Saci, A.1    Carpenter, C.L.2
  • 56
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • DOI 10.1083/jcb.131.6.1857
    • Hotchin, N. A., and Hall, A. (1995) The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho/Rac GTPases. J. Cell Biol. 131, 1857-1865 (Pubitemid 26007981)
    • (1995) Journal of Cell Biology , vol.131 , Issue.6 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 57
    • 61349202884 scopus 로고    scopus 로고
    • Mechanistic analysis of the amplification and diversification events induced by Vav proteins in B-lymphocytes
    • Caloca, M. J., Zugaza, J. L., and Bustelo, X. R. (2008) Mechanistic analysis of the amplification and diversification events induced by Vav proteins in B-lymphocytes. J. Biol. Chem. 283, 36454-36464
    • (2008) J. Biol. Chem. , vol.283 , pp. 36454-36464
    • Caloca, M.J.1    Zugaza, J.L.2    Bustelo, X.R.3
  • 58
    • 84863860582 scopus 로고    scopus 로고
    • The cytoskeleton coordinates the early events of B-cell activation
    • Harwood, N. E., and Batista, F. D. (2011) The cytoskeleton coordinates the early events of B-cell activation. Cold Spring Harbor Perspect. Biol. 3, a002360
    • (2011) Cold Spring Harbor Perspect. Biol. , vol.3
    • Harwood, N.E.1    Batista, F.D.2
  • 59
    • 0033082977 scopus 로고    scopus 로고
    • Antigen-stimulated dissociation of BCR mlg from Ig-α/Ig-β: Implications for receptor desensitization
    • Vilen, B. J., Nakamura, T., and Cambier, J. C. (1999) Antigen-stimulated dissociation of Bcr Mig from Ig- α/Ig- β: implications for receptor desensitization. Immunity 10, 239-248 (Pubitemid 29115629)
    • (1999) Immunity , vol.10 , Issue.2 , pp. 239-248
    • Vilen, B.J.1    Nakamura, T.2    Cambier, J.C.3
  • 60
    • 0033697266 scopus 로고    scopus 로고
    • Monomeric and oligomeric complexes of the B cell antigen receptor
    • Schamel, W. W., and Reth, M. (2000) Monomeric and oligomeric complexes of the B cell antigen receptor. Immunity 13, 5-14
    • (2000) Immunity , vol.13 , pp. 5-14
    • Schamel, W.W.1    Reth, M.2
  • 61
    • 39049117451 scopus 로고    scopus 로고
    • Identifying dynamic interactors of protein complexes by quantitative mass spectrometry
    • DOI 10.1074/mcp.M700261-MCP200
    • Wang, X., and Huang, L. (2008) Identifying dynamic interactors of protein complexes by quantitative mass spectrometry. Mol. Cell. Proteomics 7, 46-57 (Pubitemid 351248233)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.1 , pp. 46-57
    • Wang, X.1    Huang, L.2
  • 63
    • 0025117925 scopus 로고
    • Evi-2: A common integration site involved in murine myeloid leukemogenesis
    • Buchberg, A. M., Bedigian, H. G., Jenkins, N. A., and Copeland, N. G. (1990) Evi-2: A common integration site involved in murine myeloid leukemogenesis. Mol. Cell. Biol. 10, 4658-4666
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4658-4666
    • Buchberg, A.M.1    Bedigian, H.G.2    Jenkins, N.A.3    Copeland, N.G.4
  • 66
    • 0038392948 scopus 로고    scopus 로고
    • The SLAM family of immune-cell receptors
    • DOI 10.1016/S0952-7915(03)00041-4
    • Veillette, A., and Latour, S. (2003) The Slam family of immune-cell receptors. Curr. Opin. Immunol. 15, 277-285 (Pubitemid 36645103)
    • (2003) Current Opinion in Immunology , vol.15 , Issue.3 , pp. 277-285
    • Veillette, A.1    Latour, S.2
  • 67
    • 0028172534 scopus 로고
    • The immunoglobulin fold: Structural classification, sequence patterns and common core
    • Bork, P., Holm, L., and Sander, C. (1994) The immunoglobulin fold: structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 68
    • 0035138088 scopus 로고    scopus 로고
    • Laminin isoforms 8 and 10 are primary components of the subendothelial basement membrane promoting interaction with neoplastic lymphocytes
    • Spessotto, P., Yin, Z., Magro, G., Deutzmann, R., Chiu, A., Colombatti, A., and Perris, R. (2001) Laminin isoforms 8 and 10 are primary components of the subendothelial basement membrane promoting interaction with neoplastic lymphocytes. Cancer Res. 61, 339-347 (Pubitemid 32095736)
    • (2001) Cancer Research , vol.61 , Issue.1 , pp. 339-347
    • Spessotto, P.1    Yin, Z.2    Magro, G.3    Deutzmann, R.4    Chiu, A.5    Colombatti, A.6    Perris, R.7
  • 69
    • 3042777493 scopus 로고    scopus 로고
    • β1 Integrins show specific association with Cd98 protein in low density membranes
    • Kolesnikova, T. V., Mannion, B. A., Berditchevski, F., and Hemler, M. E. (2001)β1 Integrins show specific association with Cd98 protein in low density membranes. BMC Biochem. 2, 10
    • (2001) BMC Biochem. , vol.2 , pp. 10
    • Kolesnikova, T.V.1    Mannion, B.A.2    Berditchevski, F.3    Hemler, M.E.4
  • 70
    • 0033564326 scopus 로고    scopus 로고
    • Regulation of integrin-mediated T cell adhesion by the transmembrane protein tyrosine phosphatase CD45
    • Shenoi, H., Seavitt, J., Zheleznyak, A., Thomas, M. L., and Brown, E. J. (1999) Regulation of integrin-mediated T cell adhesion by the transmembrane protein tyrosine phosphatase Cd45. J. Immunol. 162, 7120-7127 (Pubitemid 29277681)
    • (1999) Journal of Immunology , vol.162 , Issue.12 , pp. 7120-7127
    • Shenoi, H.1    Seavitt, J.2    Zheleznyak, A.3    Thomas, M.L.4    Brown, E.J.5
  • 71
    • 0029846429 scopus 로고    scopus 로고
    • CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells
    • DOI 10.1074/jbc.271.48.30487
    • Yanagi, S., Sugawara, H., Kurosaki, M., Sabe, H., Yamamura, H., and Kurosaki, T. (1996) Cd45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells. J. Biol. Chem. 271, 30487-30492 (Pubitemid 26404055)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30487-30492
    • Yanagi, S.1    Sugawara, H.2    Kurosaki, M.3    Sabe, H.4    Yamamura, H.5    Kurosaki, T.6
  • 72
    • 0036481264 scopus 로고    scopus 로고
    • Lipid rafts and B-cell activation
    • Pierce, S. K. (2002) Lipid rafts and B-cell activation. Nat. Rev. Immunol. 2, 96-105 (Pubitemid 37323233)
    • (2002) Nature Reviews Immunology , vol.2 , Issue.2 , pp. 96-105
    • Pierce, S.K.1


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