메뉴 건너뛰기




Volumn 75, Issue 15, 2012, Pages 4610-4619

On-bead tryptic proteolysis: An attractive procedure for LC-MS/MS analysis of the Drosophila caspase 8 protein complex during immune response against bacteria

Author keywords

Dredd; Imd pathway; On bead digestion; Protein complex; Technology

Indexed keywords

BG4 PROTEIN; BIOTIN; CASPASE 8; COMPLEMENTARY DNA; CP190 PROTEIN; DREDD PROTEIN; DROSOPHILA PROTEIN; HEAT SHOCK PROTEIN 7C; PLASMID DNA; Q9VP57 PROTEIN; Q9VXQ5 PROTEIN; Q9W1B9 PROTEIN; STREPTAVIDIN; TBB1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84864090317     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.03.003     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • Lemaitre B., Hoffmann J. The host defense of Drosophila melanogaster. Annu Rev Immunol 2007, 25:697-743.
    • (2007) Annu Rev Immunol , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 2
    • 43249114465 scopus 로고    scopus 로고
    • Positive and negative regulation of the Drosophila immune response
    • Aggarwal K., Silverman N. Positive and negative regulation of the Drosophila immune response. BMB Rep 2008, 41(4):267-277.
    • (2008) BMB Rep , vol.41 , Issue.4 , pp. 267-277
    • Aggarwal, K.1    Silverman, N.2
  • 3
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar M., Gobert V., Michel T., Belvin M., Duyk G., Hoffmann J., et al. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 2002, 416(6881):640-644.
    • (2002) Nature , vol.416 , Issue.6881 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffmann, J.6
  • 4
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: an evolutionary perspective
    • Hoffmann J., Reichhart J. Drosophila innate immunity: an evolutionary perspective. Nat Immunol 2002, 2:121-126.
    • (2002) Nat Immunol , vol.2 , pp. 121-126
    • Hoffmann, J.1    Reichhart, J.2
  • 5
    • 80052197892 scopus 로고    scopus 로고
    • The protein Dredd is an essential component of the c-Jun N-terminal kinase pathway in the Drosophila immune response
    • Guntermann S., Foley E. The protein Dredd is an essential component of the c-Jun N-terminal kinase pathway in the Drosophila immune response. J Biol Chem 2011, 286(35):30284-30294.
    • (2011) J Biol Chem , vol.286 , Issue.35 , pp. 30284-30294
    • Guntermann, S.1    Foley, E.2
  • 6
    • 74749093547 scopus 로고    scopus 로고
    • Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling
    • Paquette N., Broemer M., Aggarwal K., Chen L., Husson M., Ertürk-Hasdemir D., et al. Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling. Mol Cell 2010, 37(2):172-182.
    • (2010) Mol Cell , vol.37 , Issue.2 , pp. 172-182
    • Paquette, N.1    Broemer, M.2    Aggarwal, K.3    Chen, L.4    Husson, M.5    Ertürk-Hasdemir, D.6
  • 7
    • 55749099458 scopus 로고    scopus 로고
    • Biotinylation reagents for the study of cell surface proteins
    • Elia G. Biotinylation reagents for the study of cell surface proteins. Proteomics 2008, 8(19):4012-4024.
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 4012-4024
    • Elia, G.1
  • 9
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 1999, 17(10):994-999.
    • (1999) Nat Biotechnol , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 10
    • 3543072968 scopus 로고    scopus 로고
    • Purification of biotinylated proteins on streptavidin resin: a protocol for quantitative elution
    • Rybak J., Scheurer S.B., Neri D., Elia G. Purification of biotinylated proteins on streptavidin resin: a protocol for quantitative elution. Proteomics 2004, 4(8):2296-2299.
    • (2004) Proteomics , vol.4 , Issue.8 , pp. 2296-2299
    • Rybak, J.1    Scheurer, S.B.2    Neri, D.3    Elia, G.4
  • 11
    • 77950689437 scopus 로고    scopus 로고
    • Immunoprecipitation on magnetic beads and liquid chromatography-tandem mass spectrometry for carbonic anhydrase II quantification in human serum
    • Callipo L., Caruso G., Foglia P., Gubbiotti R., Samperi R., Laganà A. Immunoprecipitation on magnetic beads and liquid chromatography-tandem mass spectrometry for carbonic anhydrase II quantification in human serum. Anal Biochem 2010, 400(2):195-202.
    • (2010) Anal Biochem , vol.400 , Issue.2 , pp. 195-202
    • Callipo, L.1    Caruso, G.2    Foglia, P.3    Gubbiotti, R.4    Samperi, R.5    Laganà, A.6
  • 12
    • 77955608229 scopus 로고    scopus 로고
    • Immunoaffinity purification using anti-PEG antibody followed by two-dimensional liquid chromatography/tandem mass spectrometry for the quantification of a PEGylated therapeutic peptide in human plasma
    • Xu Y., Mehl J.T., Bakhtiar R., Woolf E.J. Immunoaffinity purification using anti-PEG antibody followed by two-dimensional liquid chromatography/tandem mass spectrometry for the quantification of a PEGylated therapeutic peptide in human plasma. Anal Chem 2010, 82(16):6877-6886.
    • (2010) Anal Chem , vol.82 , Issue.16 , pp. 6877-6886
    • Xu, Y.1    Mehl, J.T.2    Bakhtiar, R.3    Woolf, E.J.4
  • 13
    • 0038359388 scopus 로고    scopus 로고
    • Strategy for analysis of cardiac troponins in biological samples with a combination of affinity chromatography and mass spectrometry
    • Labugger R., Simpson J.A., Quick M., Brown H.A., Collier C.E., Neverova I., et al. Strategy for analysis of cardiac troponins in biological samples with a combination of affinity chromatography and mass spectrometry. Clin Chem 2003, 49(6 Pt 1):873-879.
    • (2003) Clin Chem , vol.49 , Issue.6 PART 1 , pp. 873-879
    • Labugger, R.1    Simpson, J.A.2    Quick, M.3    Brown, H.A.4    Collier, C.E.5    Neverova, I.6
  • 14
    • 77954716955 scopus 로고    scopus 로고
    • Proteome analysis of the surface of Trichomonas vaginalis reveals novel proteins and strain-dependent differential expression
    • de Miguel N., Lustig G., Twu O., Chattopadhyay A., Wohlschlegel J.A., Johnson P.J. Proteome analysis of the surface of Trichomonas vaginalis reveals novel proteins and strain-dependent differential expression. Mol Cell Proteomics 2010, 9(7):1554-1566.
    • (2010) Mol Cell Proteomics , vol.9 , Issue.7 , pp. 1554-1566
    • de Miguel, N.1    Lustig, G.2    Twu, O.3    Chattopadhyay, A.4    Wohlschlegel, J.A.5    Johnson, P.J.6
  • 15
    • 1642332899 scopus 로고    scopus 로고
    • MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding
    • Chrestensen C.A., Schroeder M.J., Shabanowitz J., Hunt D.F., Pelo J.W., Worthington M.T., et al. MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding. J Biol Chem 2004, 279(11):10176-10184.
    • (2004) J Biol Chem , vol.279 , Issue.11 , pp. 10176-10184
    • Chrestensen, C.A.1    Schroeder, M.J.2    Shabanowitz, J.3    Hunt, D.F.4    Pelo, J.W.5    Worthington, M.T.6
  • 16
    • 35648998466 scopus 로고    scopus 로고
    • Proteomics evaluation of chemically cleavable activity-based probes
    • Fonović M., Verhelst S.H., Sorum M.T., Bogyo M. Proteomics evaluation of chemically cleavable activity-based probes. Mol Cell Proteomics 2007, 6(10):1761-1770.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.10 , pp. 1761-1770
    • Fonović, M.1    Verhelst, S.H.2    Sorum, M.T.3    Bogyo, M.4
  • 17
    • 18044400563 scopus 로고    scopus 로고
    • Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis
    • Georgel P., Naitza S., Kappler C., Ferrandon D., Zachary D., Swimmer C., et al. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Dev Cell 2001, 1(4):503-514.
    • (2001) Dev Cell , vol.1 , Issue.4 , pp. 503-514
    • Georgel, P.1    Naitza, S.2    Kappler, C.3    Ferrandon, D.4    Zachary, D.5    Swimmer, C.6
  • 18
    • 84872210040 scopus 로고    scopus 로고
    • Alternative elution conditions for the mass spectrometry analysis of polyhistidine-tagged proteins
    • Engel L., Becky Godat B., Rod Flemming M., Johnson T. Alternative elution conditions for the mass spectrometry analysis of polyhistidine-tagged proteins. Promega eNotes 2006, http://www.promega.com/enotes/applications/ap0070.html.
    • (2006) Promega eNotes
    • Engel, L.1    Becky Godat, B.2    Rod Flemming, M.3    Johnson, T.4
  • 19
    • 23844483215 scopus 로고    scopus 로고
    • Identification of JAK/STAT signalling components by genome-wide RNA interference
    • Müller P., Kuttenkeuler D., Gesellchen V., Zeidler M.P., Boutros M. Identification of JAK/STAT signalling components by genome-wide RNA interference. Nature 2005, 436(7052):871-875.
    • (2005) Nature , vol.436 , Issue.7052 , pp. 871-875
    • Müller, P.1    Kuttenkeuler, D.2    Gesellchen, V.3    Zeidler, M.P.4    Boutros, M.5
  • 20
    • 79953289737 scopus 로고    scopus 로고
    • Mapping of signaling networks through synthetic genetic interaction analysis by RNAi
    • Horn T., Sandmann T., Fischer B., Axelsson E., Huber W., Boutros M. Mapping of signaling networks through synthetic genetic interaction analysis by RNAi. Nat Methods 2011, 8:341-346.
    • (2011) Nat Methods , vol.8 , pp. 341-346
    • Horn, T.1    Sandmann, T.2    Fischer, B.3    Axelsson, E.4    Huber, W.5    Boutros, M.6
  • 21
    • 0036850985 scopus 로고    scopus 로고
    • The Drosophila immune defense against gram-negative infection requires the death protein dFADD
    • Naitza S., Rossé C., Kappler C., Georgel P., Belvin M., Gubb D., et al. The Drosophila immune defense against gram-negative infection requires the death protein dFADD. Immunity 2002, 17(5):575-581.
    • (2002) Immunity , vol.17 , Issue.5 , pp. 575-581
    • Naitza, S.1    Rossé, C.2    Kappler, C.3    Georgel, P.4    Belvin, M.5    Gubb, D.6
  • 22
    • 79955007479 scopus 로고    scopus 로고
    • Isolation and characterization of plant protein complexes by mass spectrometry
    • Pflieger D., Bigeard J., Hirt H. Isolation and characterization of plant protein complexes by mass spectrometry. Proteomics 2011, 11(9):1824-1833.
    • (2011) Proteomics , vol.11 , Issue.9 , pp. 1824-1833
    • Pflieger, D.1    Bigeard, J.2    Hirt, H.3
  • 23
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 2003, 60:523-533.
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 24
    • 59149096171 scopus 로고    scopus 로고
    • A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein
    • Goudreault M., D' Ambrosio L.M., Kean M.J., Mullin M.J., et al. A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. Mol Cell Proteomics 2009, 8:157-171.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 157-171
    • Goudreault, M.1    D' Ambrosio, L.M.2    Kean, M.J.3    Mullin, M.J.4
  • 25
    • 55949116385 scopus 로고    scopus 로고
    • Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes
    • Trinkle-Mulcahy L., Boulon S., Lam Y.W., Urcia R., Boisvert F.M., Vandermoere F., et al. Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes. J Cell Biol 2008, 183(2):223-239.
    • (2008) J Cell Biol , vol.183 , Issue.2 , pp. 223-239
    • Trinkle-Mulcahy, L.1    Boulon, S.2    Lam, Y.W.3    Urcia, R.4    Boisvert, F.M.5    Vandermoere, F.6
  • 26
    • 77951844076 scopus 로고    scopus 로고
    • Establishment of a protein frequency library and its application in the reliable identification of specific protein interaction partners
    • Boulon S., Ahmad Y., Trinkle-Mulcahy L., Verheggen C., Cobley A., Gregor P., et al. Establishment of a protein frequency library and its application in the reliable identification of specific protein interaction partners. Mol Cell Proteomics 2010, 9(5):861-879.
    • (2010) Mol Cell Proteomics , vol.9 , Issue.5 , pp. 861-879
    • Boulon, S.1    Ahmad, Y.2    Trinkle-Mulcahy, L.3    Verheggen, C.4    Cobley, A.5    Gregor, P.6
  • 27
    • 30544439962 scopus 로고    scopus 로고
    • In-solution digestion of proteins for mass spectrometry
    • Medziradszky K. In-solution digestion of proteins for mass spectrometry. Methods Enzymol 2005, 405:50-65.
    • (2005) Methods Enzymol , vol.405 , pp. 50-65
    • Medziradszky, K.1
  • 29
    • 79955933202 scopus 로고    scopus 로고
    • The Putzig-NURF nucleosome remodeling complex is required for ecdysone receptor signaling and innate immunity in Drosophila melanogaster
    • Kugler S., Gehring E., Wallkamm V., Krüger V., Nagel A. The Putzig-NURF nucleosome remodeling complex is required for ecdysone receptor signaling and innate immunity in Drosophila melanogaster. Genetics 2011, 188(1):127-139.
    • (2011) Genetics , vol.188 , Issue.1 , pp. 127-139
    • Kugler, S.1    Gehring, E.2    Wallkamm, V.3    Krüger, V.4    Nagel, A.5
  • 30
    • 84860388943 scopus 로고    scopus 로고
    • RNAi-independent role for Argonaute2 in CTCF/CP190 chromatin insulator function
    • Moshkovich N., Nisha P., Boyle P., Thompson B., Dale R., Lei E. RNAi-independent role for Argonaute2 in CTCF/CP190 chromatin insulator function. Genes Dev 2011, 25(16):1686-1701.
    • (2011) Genes Dev , vol.25 , Issue.16 , pp. 1686-1701
    • Moshkovich, N.1    Nisha, P.2    Boyle, P.3    Thompson, B.4    Dale, R.5    Lei, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.