메뉴 건너뛰기




Volumn 13, Issue 3, 2017, Pages

Proteomics and integrative omic approaches for understanding host–pathogen interactions and infectious diseases

Author keywords

networks; omics; organelle; systems biology; virus infection

Indexed keywords

PROTEOME;

EID: 85016256763     PISSN: None     EISSN: 17444292     Source Type: Journal    
DOI: 10.15252/msb.20167062     Document Type: Review
Times cited : (155)

References (145)
  • 4
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M (2003) Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426: 570–574
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 5
    • 84871865189 scopus 로고    scopus 로고
    • Popular computational methods to assess multiprotein complexes derived from label-free affinity purification and mass spectrometry (AP-MS) experiments
    • Armean IM, Lilley KS, Trotter MW (2013) Popular computational methods to assess multiprotein complexes derived from label-free affinity purification and mass spectrometry (AP-MS) experiments. Mol Cell Proteomics 12: 1–13
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1-13
    • Armean, I.M.1    Lilley, K.S.2    Trotter, M.W.3
  • 8
    • 84973452237 scopus 로고    scopus 로고
    • Global mapping of O-glycosylation of varicella zoster virus, human cytomegalovirus, and Epstein-barr virus
    • Bagdonaite I, Norden R, Joshi HJ, King SL, Vakhrushev SY, Olofsson S, Wandall HH (2016) Global mapping of O-glycosylation of varicella zoster virus, human cytomegalovirus, and Epstein-barr virus. J Biol Chem 291: 12014–12028
    • (2016) J Biol Chem , vol.291 , pp. 12014-12028
    • Bagdonaite, I.1    Norden, R.2    Joshi, H.J.3    King, S.L.4    Vakhrushev, S.Y.5    Olofsson, S.6    Wandall, H.H.7
  • 9
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
    • Bantscheff M, Lemeer S, Savitski MM, Kuster B (2012) Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal Bioanal Chem 404: 939–965
    • (2012) Anal Bioanal Chem , vol.404 , pp. 939-965
    • Bantscheff, M.1    Lemeer, S.2    Savitski, M.M.3    Kuster, B.4
  • 10
    • 84875938497 scopus 로고    scopus 로고
    • Proteomics analysis of herpes simplex virus type 1-infected cells reveals dynamic changes of viral protein expression, ubiquitylation, and phosphorylation
    • Bell C, Desjardins M, Thibault P, Radtke K (2013) Proteomics analysis of herpes simplex virus type 1-infected cells reveals dynamic changes of viral protein expression, ubiquitylation, and phosphorylation. J Proteome Res 12: 1820–1829
    • (2013) J Proteome Res , vol.12 , pp. 1820-1829
    • Bell, C.1    Desjardins, M.2    Thibault, P.3    Radtke, K.4
  • 11
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • Bensimon A, Heck AJ, Aebersold R (2012) Mass spectrometry-based proteomics and network biology. Annu Rev Biochem 81: 379–405
    • (2012) Annu Rev Biochem , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 12
    • 84929659133 scopus 로고    scopus 로고
    • Quantification of the host response proteome after herpes simplex virus type 1 infection
    • Berard AR, Coombs KM, Severini A (2015) Quantification of the host response proteome after herpes simplex virus type 1 infection. J Proteome Res 14: 2121–2142
    • (2015) J Proteome Res , vol.14 , pp. 2121-2142
    • Berard, A.R.1    Coombs, K.M.2    Severini, A.3
  • 13
    • 0032888951 scopus 로고    scopus 로고
    • Phosphorylation of the human T-cell leukemia virus type 1 transactivator tax on adjacent serine residues is critical for tax activation
    • Bex F, Murphy K, Wattiez R, Burny A, Gaynor RB (1999) Phosphorylation of the human T-cell leukemia virus type 1 transactivator tax on adjacent serine residues is critical for tax activation. J Virol 73: 738–745
    • (1999) J Virol , vol.73 , pp. 738-745
    • Bex, F.1    Murphy, K.2    Wattiez, R.3    Burny, A.4    Gaynor, R.B.5
  • 15
    • 77951275498 scopus 로고    scopus 로고
    • Performance of matrix-assisted laser desorption ionization-time of flight mass spectrometry for identification of bacterial strains routinely isolated in a clinical microbiology laboratory
    • Bizzini A, Durussel C, Bille J, Greub G, Prod'hom G (2010) Performance of matrix-assisted laser desorption ionization-time of flight mass spectrometry for identification of bacterial strains routinely isolated in a clinical microbiology laboratory. J Clin Microbiol 48: 1549–1554.
    • (2010) J Clin Microbiol , vol.48 , pp. 1549-1554
    • Bizzini, A.1    Durussel, C.2    Bille, J.3    Greub, G.4    Prod'hom, G.5
  • 17
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of I kappa B
    • Bour S, Perrin C, Akari H, Strebel K (2001) The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of I kappa B. J Biol Chem 276: 15920–15928
    • (2001) J Biol Chem , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 19
    • 84931005724 scopus 로고    scopus 로고
    • Proteomic identification of nuclear processes manipulated by cytomegalovirus early during infection
    • Carter DM, Westdorp K, Noon KR, Terhune SS (2015) Proteomic identification of nuclear processes manipulated by cytomegalovirus early during infection. Proteomics 15: 1995–2005
    • (2015) Proteomics , vol.15 , pp. 1995-2005
    • Carter, D.M.1    Westdorp, K.2    Noon, K.R.3    Terhune, S.S.4
  • 20
    • 84896999760 scopus 로고    scopus 로고
    • MRM for the verification of cancer biomarker proteins: recent applications to human plasma and serum
    • Chambers AG, Percy AJ, Simon R, Borchers CH (2014) MRM for the verification of cancer biomarker proteins: recent applications to human plasma and serum. Expert Rev Proteomics 11: 137–148
    • (2014) Expert Rev Proteomics , vol.11 , pp. 137-148
    • Chambers, A.G.1    Percy, A.J.2    Simon, R.3    Borchers, C.H.4
  • 21
    • 84884404368 scopus 로고    scopus 로고
    • Targeted identification of glycosylated proteins in the gastric pathogen Helicobacter pylori (Hp)
    • Champasa K, Longwell SA, Eldridge AM, Stemmler EA, Dube DH (2013) Targeted identification of glycosylated proteins in the gastric pathogen Helicobacter pylori (Hp). Mol Cell Proteomics 12: 2568–2586
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2568-2586
    • Champasa, K.1    Longwell, S.A.2    Eldridge, A.M.3    Stemmler, E.A.4    Dube, D.H.5
  • 22
    • 84860602175 scopus 로고    scopus 로고
    • Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions
    • Chavez JD, Cilia M, Weisbrod CR, Ju HJ, Eng JK, Gray SM, Bruce JE (2012) Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions. J Proteome Res 11: 2968–2981
    • (2012) J Proteome Res , vol.11 , pp. 2968-2981
    • Chavez, J.D.1    Cilia, M.2    Weisbrod, C.R.3    Ju, H.J.4    Eng, J.K.5    Gray, S.M.6    Bruce, J.E.7
  • 26
    • 84907033616 scopus 로고    scopus 로고
    • MSstats: an R package for statistical analysis of quantitative mass spectrometry-based proteomic experiments
    • Choi M, Chang CY, Clough T, Broudy D, Killeen T, MacLean B, Vitek O (2014) MSstats: an R package for statistical analysis of quantitative mass spectrometry-based proteomic experiments. Bioinformatics 30: 2524–2526
    • (2014) Bioinformatics , vol.30 , pp. 2524-2526
    • Choi, M.1    Chang, C.Y.2    Clough, T.3    Broudy, D.4    Killeen, T.5    MacLean, B.6    Vitek, O.7
  • 28
    • 80054775043 scopus 로고    scopus 로고
    • Protein turnover methods in single-celled organisms: dynamic SILAC
    • Claydon AJ, Beynon RJ (2011) Protein turnover methods in single-celled organisms: dynamic SILAC. Methods Mol Biol 759: 179–195
    • (2011) Methods Mol Biol , vol.759 , pp. 179-195
    • Claydon, A.J.1    Beynon, R.J.2
  • 30
    • 85056746600 scopus 로고    scopus 로고
    • The ubiquitination of NF-kappaB subunits in the control of transcription
    • Collins PE, Mitxitorena I, Carmody RJ (2016) The ubiquitination of NF-kappaB subunits in the control of transcription. Cells 5: 23
    • (2016) Cells , vol.5 , pp. 23
    • Collins, P.E.1    Mitxitorena, I.2    Carmody, R.J.3
  • 31
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox J, Hein MY, Luber CA, Paron I, Nagaraj N, Mann M (2014) Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol Cell Proteomics 13: 2513–2526
    • (2014) Mol Cell Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 33
    • 52649089194 scopus 로고    scopus 로고
    • Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts
    • Cuevas-Bennett C, Shenk T (2008) Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts. J Virol 82: 9525–9536
    • (2008) J Virol , vol.82 , pp. 9525-9536
    • Cuevas-Bennett, C.1    Shenk, T.2
  • 35
    • 79851514364 scopus 로고    scopus 로고
    • Early proteomic analysis may allow noninvasive identification of hepatitis C response to treatment with pegylated interferon alpha-2b and ribavirin
    • Devitt EJ, Power KA, Lawless MW, Browne JA, Gaora PO, Gallagher WM, Crowe J (2011) Early proteomic analysis may allow noninvasive identification of hepatitis C response to treatment with pegylated interferon alpha-2b and ribavirin. Eur J Gastroenterol Hepatol 23: 177–183
    • (2011) Eur J Gastroenterol Hepatol , vol.23 , pp. 177-183
    • Devitt, E.J.1    Power, K.A.2    Lawless, M.W.3    Browne, J.A.4    Gaora, P.O.5    Gallagher, W.M.6    Crowe, J.7
  • 37
    • 34347218266 scopus 로고    scopus 로고
    • Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging
    • Dieterich DC, Lee JJ, Link AJ, Graumann J, Tirrell DA, Schuman EM (2007) Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging. Nat Protoc 2: 532–540
    • (2007) Nat Protoc , vol.2 , pp. 532-540
    • Dieterich, D.C.1    Lee, J.J.2    Link, A.J.3    Graumann, J.4    Tirrell, D.A.5    Schuman, E.M.6
  • 38
    • 84940542596 scopus 로고    scopus 로고
    • Interactions of the antiviral factor interferon gamma-inducible protein 16 (IFI16) mediate immune signaling and herpes simplex virus-1 immunosuppression
    • Diner BA, Lum KK, Javitt A, Cristea IM (2015) Interactions of the antiviral factor interferon gamma-inducible protein 16 (IFI16) mediate immune signaling and herpes simplex virus-1 immunosuppression. Mol Cell Proteomics 14: 2341–2356
    • (2015) Mol Cell Proteomics , vol.14 , pp. 2341-2356
    • Diner, B.A.1    Lum, K.K.2    Javitt, A.3    Cristea, I.M.4
  • 39
    • 85007554197 scopus 로고    scopus 로고
    • Viral DNA sensors IFI16 and Cyclic GMP-AMP synthase possess distinct functions in regulating viral gene expression, immune defenses, and apoptotic responses during herpesvirus infection
    • Diner BA, Lum KK, Toettcher JE, Cristea IM (2016) Viral DNA sensors IFI16 and Cyclic GMP-AMP synthase possess distinct functions in regulating viral gene expression, immune defenses, and apoptotic responses during herpesvirus infection. MBio 7: e01553-16
    • (2016) MBio , vol.7
    • Diner, B.A.1    Lum, K.K.2    Toettcher, J.E.3    Cristea, I.M.4
  • 42
    • 84947997488 scopus 로고    scopus 로고
    • Improving the phosphoproteome coverage for limited sample amounts using TiO2-SIMAC-HILIC (TiSH) phosphopeptide enrichment and fractionation
    • Engholm-Keller K, Larsen MR (2016) Improving the phosphoproteome coverage for limited sample amounts using TiO2-SIMAC-HILIC (TiSH) phosphopeptide enrichment and fractionation. Methods Mol Biol 1355: 161–177
    • (2016) Methods Mol Biol , vol.1355 , pp. 161-177
    • Engholm-Keller, K.1    Larsen, M.R.2
  • 45
    • 75749101060 scopus 로고    scopus 로고
    • A recipe for proteomics diagnostic test development: the OVA1 test, from biomarker discovery to FDA clearance
    • Fung ET (2010) A recipe for proteomics diagnostic test development: the OVA1 test, from biomarker discovery to FDA clearance. Clin Chem 56: 327–329
    • (2010) Clin Chem , vol.56 , pp. 327-329
    • Fung, E.T.1
  • 50
    • 85017004540 scopus 로고    scopus 로고
    • The impact of mass spectrometry-based proteomics on fundamental discoveries in virology
    • Greco TM, Diner BA, Cristea IM (2014) The impact of mass spectrometry-based proteomics on fundamental discoveries in virology. Annu Rev Virol 1: 581–604
    • (2014) Annu Rev Virol , vol.1 , pp. 581-604
    • Greco, T.M.1    Diner, B.A.2    Cristea, I.M.3
  • 52
    • 84872048340 scopus 로고    scopus 로고
    • Increased expression of LDL receptor-related protein 1 during human cytomegalovirus infection reduces virion cholesterol and infectivity
    • Gudleski-O'Regan N, Greco TM, Cristea IM, Shenk T (2012) Increased expression of LDL receptor-related protein 1 during human cytomegalovirus infection reduces virion cholesterol and infectivity. Cell Host Microbe 12: 86–96
    • (2012) Cell Host Microbe , vol.12 , pp. 86-96
    • Gudleski-O'Regan, N.1    Greco, T.M.2    Cristea, I.M.3    Shenk, T.4
  • 54
    • 84903843093 scopus 로고    scopus 로고
    • Identification of the flagellin glycosylation system in Burkholderia cenocepacia and the contribution of glycosylated flagellin to evasion of human innate immune responses
    • Hanuszkiewicz A, Pittock P, Humphries F, Moll H, Rosales AR, Molinaro A, Moynagh PN, Lajoie GA, Valvano MA (2014) Identification of the flagellin glycosylation system in Burkholderia cenocepacia and the contribution of glycosylated flagellin to evasion of human innate immune responses. J Biol Chem 289: 19231–19244
    • (2014) J Biol Chem , vol.289 , pp. 19231-19244
    • Hanuszkiewicz, A.1    Pittock, P.2    Humphries, F.3    Moll, H.4    Rosales, A.R.5    Molinaro, A.6    Moynagh, P.N.7    Lajoie, G.A.8    Valvano, M.A.9
  • 57
    • 84924194443 scopus 로고    scopus 로고
    • Proteomic analysis of mitochondrial-associated ER membranes (MAM) during RNA virus infection reveals dynamic changes in protein and organelle trafficking
    • Horner SM, Wilkins C, Badil S, Iskarpatyoti J, Gale M Jr (2015) Proteomic analysis of mitochondrial-associated ER membranes (MAM) during RNA virus infection reveals dynamic changes in protein and organelle trafficking. PLoS One 10: e0117963
    • (2015) PLoS One , vol.10
    • Horner, S.M.1    Wilkins, C.2    Badil, S.3    Iskarpatyoti, J.4    Gale, M.5
  • 59
    • 84990890050 scopus 로고    scopus 로고
    • Sumoylation promotes the stability of the DNA sensor cGAS and the adaptor STING to regulate the kinetics of response to DNA virus
    • Hu MM, Yang Q, Xie XQ, Liao CY, Lin H, Liu TT, Yin L, Shu HB (2016) Sumoylation promotes the stability of the DNA sensor cGAS and the adaptor STING to regulate the kinetics of response to DNA virus. Immunity 45: 555–569
    • (2016) Immunity , vol.45 , pp. 555-569
    • Hu, M.M.1    Yang, Q.2    Xie, X.Q.3    Liao, C.Y.4    Lin, H.5    Liu, T.T.6    Yin, L.7    Shu, H.B.8
  • 60
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • da Huang W, Sherman BT, Lempicki RA (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4: 44–57
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 61
    • 84962564916 scopus 로고    scopus 로고
    • Direct identification of urinary tract pathogens from urine samples, combining urine screening methods and matrix-assisted laser desorption ionization-time of flight mass spectrometry
    • Inigo M, Coello A, Fernandez-Rivas G, Rivaya B, Hidalgo J, Quesada MD, Ausina V (2016) Direct identification of urinary tract pathogens from urine samples, combining urine screening methods and matrix-assisted laser desorption ionization-time of flight mass spectrometry. J Clin Microbiol 54: 988–993
    • (2016) J Clin Microbiol , vol.54 , pp. 988-993
    • Inigo, M.1    Coello, A.2    Fernandez-Rivas, G.3    Rivaya, B.4    Hidalgo, J.5    Quesada, M.D.6    Ausina, V.7
  • 62
    • 84979673478 scopus 로고    scopus 로고
    • Global, quantitative and dynamic mapping of protein subcellular localization
    • Itzhak DN, Tyanova S, Cox J, Borner GH (2016) Global, quantitative and dynamic mapping of protein subcellular localization. eLife 5: e16950
    • (2016) eLife , vol.5
    • Itzhak, D.N.1    Tyanova, S.2    Cox, J.3    Borner, G.H.4
  • 63
  • 66
    • 84922069715 scopus 로고    scopus 로고
    • Emerging functions of the unfolded protein response in immunity
    • Janssens S, Pulendran B, Lambrecht BN (2014) Emerging functions of the unfolded protein response in immunity. Nat Immunol 15: 910–919
    • (2014) Nat Immunol , vol.15 , pp. 910-919
    • Janssens, S.1    Pulendran, B.2    Lambrecht, B.N.3
  • 67
    • 84994577484 scopus 로고    scopus 로고
    • A portrait of the human organelle proteome in space and time during cytomegalovirus infection
    • e6
    • Jean Beltran PM, Mathias RA, Cristea IM (2016) A portrait of the human organelle proteome in space and time during cytomegalovirus infection. Cell Syst 3:361–373.e6
    • (2016) Cell Syst , vol.3 , pp. 361-373
    • Jean Beltran, P.M.1    Mathias, R.A.2    Cristea, I.M.3
  • 69
    • 84921712005 scopus 로고    scopus 로고
    • Quantitative proteomic identification of host factors involved in the Salmonella typhimurium infection cycle
    • Kaloyanova D, Vogels M, van Balkom BW, Helms JB (2015) Quantitative proteomic identification of host factors involved in the Salmonella typhimurium infection cycle. Methods Mol Biol 1225: 29–45
    • (2015) Methods Mol Biol , vol.1225 , pp. 29-45
    • Kaloyanova, D.1    Vogels, M.2    van Balkom, B.W.3    Helms, J.B.4
  • 72
    • 84943742970 scopus 로고    scopus 로고
    • A novel combined RNA-protein interaction analysis distinguishes HIV-1 Gag protein binding sites from structural change in the viral RNA leader
    • Kenyon JC, Prestwood LJ, Lever AM (2015) A novel combined RNA-protein interaction analysis distinguishes HIV-1 Gag protein binding sites from structural change in the viral RNA leader. Sci Rep 5: 14369
    • (2015) Sci Rep , vol.5 , pp. 14369
    • Kenyon, J.C.1    Prestwood, L.J.2    Lever, A.M.3
  • 73
    • 84973369409 scopus 로고    scopus 로고
    • Integrated omics and computational glycobiology reveal structural basis for influenza a virus glycan microheterogeneity and host interactions
    • Khatri K, Klein JA, White MR, Grant OC, Leymarie N, Woods RJ, Hartshorn KL, Zaia J (2016) Integrated omics and computational glycobiology reveal structural basis for influenza a virus glycan microheterogeneity and host interactions. Mol Cell Proteomics 15: 1895–1912
    • (2016) Mol Cell Proteomics , vol.15 , pp. 1895-1912
    • Khatri, K.1    Klein, J.A.2    White, M.R.3    Grant, O.C.4    Leymarie, N.5    Woods, R.J.6    Hartshorn, K.L.7    Zaia, J.8
  • 74
    • 80053404377 scopus 로고    scopus 로고
    • Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates
    • Kleifeld O, Doucet A, Prudova A, auf dem Keller U, Gioia M, Kizhakkedathu JN, Overall CM (2011) Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates. Nat Protoc 6: 1578–1611
    • (2011) Nat Protoc , vol.6 , pp. 1578-1611
    • Kleifeld, O.1    Doucet, A.2    Prudova, A.3    auf dem Keller, U.4    Gioia, M.5    Kizhakkedathu, J.N.6    Overall, C.M.7
  • 75
    • 84938910338 scopus 로고    scopus 로고
    • Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment
    • Konijnenberg A, Bannwarth L, Yilmaz D, Kocer A, Venien-Bryan C, Sobott F (2015) Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment. Protein Sci 24: 1292–1300
    • (2015) Protein Sci , vol.24 , pp. 1292-1300
    • Konijnenberg, A.1    Bannwarth, L.2    Yilmaz, D.3    Kocer, A.4    Venien-Bryan, C.5    Sobott, F.6
  • 76
    • 84872576880 scopus 로고    scopus 로고
    • Efficient retrograde transport of pseudorabies virus within neurons requires local protein synthesis in axons
    • Koyuncu OO, Perlman DH, Enquist LW (2013) Efficient retrograde transport of pseudorabies virus within neurons requires local protein synthesis in axons. Cell Host Microbe 13: 54–66
    • (2013) Cell Host Microbe , vol.13 , pp. 54-66
    • Koyuncu, O.O.1    Perlman, D.H.2    Enquist, L.W.3
  • 78
    • 84947493332 scopus 로고    scopus 로고
    • Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics
    • Kulej K, Avgousti DC, Weitzman MD, Garcia BA (2015) Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics. Methods 90: 8–20
    • (2015) Methods , vol.90 , pp. 8-20
    • Kulej, K.1    Avgousti, D.C.2    Weitzman, M.D.3    Garcia, B.A.4
  • 80
    • 71049140093 scopus 로고    scopus 로고
    • Direct identification of bacteria in positive blood culture bottles by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry
    • La Scola B, Raoult D (2009) Direct identification of bacteria in positive blood culture bottles by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry. PLoS One 4: e8041
    • (2009) PLoS One , vol.4
    • La Scola, B.1    Raoult, D.2
  • 81
    • 84856628618 scopus 로고    scopus 로고
    • Posttranslational modifications of proteins in the pathobiology of medically relevant fungi
    • Leach MD, Brown AJ (2012) Posttranslational modifications of proteins in the pathobiology of medically relevant fungi. Eukaryot Cell 11: 98–108
    • (2012) Eukaryot Cell , vol.11 , pp. 98-108
    • Leach, M.D.1    Brown, A.J.2
  • 82
    • 84952639674 scopus 로고    scopus 로고
    • Crosslinking and mass spectrometry: an integrated technology to understand the structure and function of molecular machines
    • Leitner A, Faini M, Stengel F, Aebersold R (2016) Crosslinking and mass spectrometry: an integrated technology to understand the structure and function of molecular machines. Trends Biochem Sci 41: 20–32
    • (2016) Trends Biochem Sci , vol.41 , pp. 20-32
    • Leitner, A.1    Faini, M.2    Stengel, F.3    Aebersold, R.4
  • 83
    • 84880636166 scopus 로고    scopus 로고
    • Thiouracil cross-linking mass spectrometry: a cell-based method to identify host factors involved in viral amplification
    • Lenarcic EM, Landry DM, Greco TM, Cristea IM, Thompson SR (2013) Thiouracil cross-linking mass spectrometry: a cell-based method to identify host factors involved in viral amplification. J Virol 87: 8697–8712
    • (2013) J Virol , vol.87 , pp. 8697-8712
    • Lenarcic, E.M.1    Landry, D.M.2    Greco, T.M.3    Cristea, I.M.4    Thompson, S.R.5
  • 85
    • 84862976171 scopus 로고    scopus 로고
    • Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16
    • Li T, Diner BA, Chen J, Cristea IM (2012b) Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16. Proc Natl Acad Sci USA 109: 10558–10563
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 10558-10563
    • Li, T.1    Diner, B.A.2    Chen, J.3    Cristea, I.M.4
  • 86
    • 84887929864 scopus 로고    scopus 로고
    • Human cytomegalovirus tegument protein pUL83 inhibits IFI16-mediated DNA sensing for immune evasion
    • Li T, Chen J, Cristea IM (2013) Human cytomegalovirus tegument protein pUL83 inhibits IFI16-mediated DNA sensing for immune evasion. Cell Host Microbe 14: 591–599
    • (2013) Cell Host Microbe , vol.14 , pp. 591-599
    • Li, T.1    Chen, J.2    Cristea, I.M.3
  • 87
    • 84922597438 scopus 로고    scopus 로고
    • Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis
    • Liu F, Yang M, Wang X, Yang S, Gu J, Zhou J, Zhang XE, Deng J, Ge F (2014) Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis. Mol Cell Proteomics 13: 3352–3366
    • (2014) Mol Cell Proteomics , vol.13 , pp. 3352-3366
    • Liu, F.1    Yang, M.2    Wang, X.3    Yang, S.4    Gu, J.5    Zhou, J.6    Zhang, X.E.7    Deng, J.8    Ge, F.9
  • 91
    • 84960415855 scopus 로고    scopus 로고
    • Proteomic approaches to uncovering virus-host protein interactions during the progression of viral infection
    • Lum KK, Cristea IM (2016) Proteomic approaches to uncovering virus-host protein interactions during the progression of viral infection. Expert Rev Proteomics 13: 325–340
    • (2016) Expert Rev Proteomics , vol.13 , pp. 325-340
    • Lum, K.K.1    Cristea, I.M.2
  • 98
    • 84892511644 scopus 로고    scopus 로고
    • Large-scale gene function analysis with the PANTHER classification system
    • Mi H, Muruganujan A, Casagrande JT, Thomas PD (2013) Large-scale gene function analysis with the PANTHER classification system. Nat Protoc 8: 1551–1566
    • (2013) Nat Protoc , vol.8 , pp. 1551-1566
    • Mi, H.1    Muruganujan, A.2    Casagrande, J.T.3    Thomas, P.D.4
  • 99
    • 84982868458 scopus 로고    scopus 로고
    • Functional characterization of the Mycobacterium abscessus genome coupled with condition specific transcriptomics reveals conserved molecular strategies for host adaptation and persistence
    • Miranda-CasoLuengo AA, Staunton PM, Dinan AM, Lohan AJ, Loftus BJ (2016) Functional characterization of the Mycobacterium abscessus genome coupled with condition specific transcriptomics reveals conserved molecular strategies for host adaptation and persistence. BMC Genom 17: 553
    • (2016) BMC Genom , vol.17 , pp. 553
    • Miranda-CasoLuengo, A.A.1    Staunton, P.M.2    Dinan, A.M.3    Lohan, A.J.4    Loftus, B.J.5
  • 100
    • 33845480946 scopus 로고    scopus 로고
    • Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling
    • Mittal R, Peak-Chew SY, McMahon HT (2006) Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling. Proc Natl Acad Sci USA 103: 18574–18579
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18574-18579
    • Mittal, R.1    Peak-Chew, S.Y.2    McMahon, H.T.3
  • 101
    • 78149417909 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation
    • Monroe EB, Kang S, Kyere SK, Li R, Prevelige PE Jr (2010) Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation. Structure 18: 1483–1491
    • (2010) Structure , vol.18 , pp. 1483-1491
    • Monroe, E.B.1    Kang, S.2    Kyere, S.K.3    Li, R.4    Prevelige, P.E.5
  • 102
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman NJ, Cristea IM, Terhune SS, Rout MP, Chait BT, Shenk T (2008) Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 3: 253–262
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.S.3    Rout, M.P.4    Chait, B.T.5    Shenk, T.6
  • 103
    • 77951790602 scopus 로고    scopus 로고
    • A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation
    • Moorman NJ, Sharon-Friling R, Shenk T, Cristea IM (2010) A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation. Mol Cell Proteomics 9: 851–860
    • (2010) Mol Cell Proteomics , vol.9 , pp. 851-860
    • Moorman, N.J.1    Sharon-Friling, R.2    Shenk, T.3    Cristea, I.M.4
  • 104
    • 84872149525 scopus 로고    scopus 로고
    • Emerging infectious diseases in 2012: 20 years after the institute of medicine report
    • Morens DM, Fauci AS (2012) Emerging infectious diseases in 2012: 20 years after the institute of medicine report. MBio 3: e00494-12
    • (2012) MBio , vol.3
    • Morens, D.M.1    Fauci, A.S.2
  • 109
    • 84908540871 scopus 로고    scopus 로고
    • Proteogenomics: concepts, applications and computational strategies
    • Nesvizhskii AI (2014) Proteogenomics: concepts, applications and computational strategies. Nat Methods 11: 1114–1125
    • (2014) Nat Methods , vol.11 , pp. 1114-1125
    • Nesvizhskii, A.I.1
  • 110
    • 77956992830 scopus 로고    scopus 로고
    • Epigenetic reprogramming of host genes in viral and microbial pathogenesis
    • Paschos K, Allday MJ (2010) Epigenetic reprogramming of host genes in viral and microbial pathogenesis. Trends Microbiol 18: 439–447
    • (2010) Trends Microbiol , vol.18 , pp. 439-447
    • Paschos, K.1    Allday, M.J.2
  • 112
    • 65449183853 scopus 로고    scopus 로고
    • Viral avoidance and exploitation of the ubiquitin system
    • Randow F, Lehner PJ (2009) Viral avoidance and exploitation of the ubiquitin system. Nat Cell Biol 11: 527–534
    • (2009) Nat Cell Biol , vol.11 , pp. 527-534
    • Randow, F.1    Lehner, P.J.2
  • 113
    • 69449090610 scopus 로고    scopus 로고
    • Ebolavirus glycoprotein GP masks both its own epitopes and the presence of cellular surface proteins
    • Reynard O, Borowiak M, Volchkova VA, Delpeut S, Mateo M, Volchkov VE (2009) Ebolavirus glycoprotein GP masks both its own epitopes and the presence of cellular surface proteins. J Virol 83: 9596–9601
    • (2009) J Virol , vol.83 , pp. 9596-9601
    • Reynard, O.1    Borowiak, M.2    Volchkova, V.A.3    Delpeut, S.4    Mateo, M.5    Volchkov, V.E.6
  • 114
    • 78650153662 scopus 로고    scopus 로고
    • Pathogen-mediated posttranslational modifications: a re-emerging field
    • Ribet D, Cossart P (2010) Pathogen-mediated posttranslational modifications: a re-emerging field. Cell 143: 694–702
    • (2010) Cell , vol.143 , pp. 694-702
    • Ribet, D.1    Cossart, P.2
  • 115
    • 84897480893 scopus 로고    scopus 로고
    • Cytomegalovirus vaccine: phase II clinical trial results
    • Rieder F, Steininger C (2014) Cytomegalovirus vaccine: phase II clinical trial results. Clin Microbiol Infect 20(Suppl. 5): 95–102
    • (2014) Clin Microbiol Infect , vol.20 , pp. 95-102
    • Rieder, F.1    Steininger, C.2
  • 120
    • 84957628834 scopus 로고    scopus 로고
    • Ion-current-based temporal proteomic profiling of influenza-a-virus-infected mouse lungs revealed underlying mechanisms of altered integrity of the lung microvascular barrier
    • Shen S, Li J, Hilchey S, Shen X, Tu C, Qiu X, Ng A, Ghaemmaghami S, Wu H, Zand MS, Qu J (2016) Ion-current-based temporal proteomic profiling of influenza-a-virus-infected mouse lungs revealed underlying mechanisms of altered integrity of the lung microvascular barrier. J Proteome Res 15: 540–553
    • (2016) J Proteome Res , vol.15 , pp. 540-553
    • Shen, S.1    Li, J.2    Hilchey, S.3    Shen, X.4    Tu, C.5    Qiu, X.6    Ng, A.7    Ghaemmaghami, S.8    Wu, H.9    Zand, M.S.10    Qu, J.11
  • 122
    • 84946865956 scopus 로고    scopus 로고
    • Highly pathogenic H5N1 and novel H7N9 influenza a viruses induce more profound proteomic host responses than seasonal and pandemic H1N1 strains
    • Simon PF, McCorrister S, Hu P, Chong P, Silaghi A, Westmacott G, Coombs KM, Kobasa D (2015) Highly pathogenic H5N1 and novel H7N9 influenza a viruses induce more profound proteomic host responses than seasonal and pandemic H1N1 strains. J Proteome Res 14: 4511–4523
    • (2015) J Proteome Res , vol.14 , pp. 4511-4523
    • Simon, P.F.1    McCorrister, S.2    Hu, P.3    Chong, P.4    Silaghi, A.5    Westmacott, G.6    Coombs, K.M.7    Kobasa, D.8
  • 124
    • 84874849330 scopus 로고    scopus 로고
    • Urinary proteomics analysis for sepsis biomarkers with iTRAQ labeling and two-dimensional liquid chromatography-tandem mass spectrometry
    • Su L, Zhou R, Liu C, Wen B, Xiao K, Kong W, Tan F, Huang Y, Cao L, Xie L (2013) Urinary proteomics analysis for sepsis biomarkers with iTRAQ labeling and two-dimensional liquid chromatography-tandem mass spectrometry. J Trauma Acute Care Surg 74: 940–945
    • (2013) J Trauma Acute Care Surg , vol.74 , pp. 940-945
    • Su, L.1    Zhou, R.2    Liu, C.3    Wen, B.4    Xiao, K.5    Kong, W.6    Tan, F.7    Huang, Y.8    Cao, L.9    Xie, L.10
  • 127
    • 84864293794 scopus 로고    scopus 로고
    • Viral and host control of cytomegalovirus maturation
    • Tandon R, Mocarski ES (2012) Viral and host control of cytomegalovirus maturation. Trends Microbiol 20: 392–401
    • (2012) Trends Microbiol , vol.20 , pp. 392-401
    • Tandon, R.1    Mocarski, E.S.2
  • 130
    • 84874619400 scopus 로고    scopus 로고
    • Refined preparation and use of anti-diglycine remnant (K-epsilon-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments
    • Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA (2013) Refined preparation and use of anti-diglycine remnant (K-epsilon-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Mol Cell Proteomics 12: 825–831
    • (2013) Mol Cell Proteomics , vol.12 , pp. 825-831
    • Udeshi, N.D.1    Svinkina, T.2    Mertins, P.3    Kuhn, E.4    Mani, D.R.5    Qiao, J.W.6    Carr, S.A.7
  • 131
  • 132
    • 11844269840 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappaB and IkappaB proteins: implications in cancer and inflammation
    • Viatour P, Merville MP, Bours V, Chariot A (2005) Phosphorylation of NF-kappaB and IkappaB proteins: implications in cancer and inflammation. Trends Biochem Sci 30: 43–52
    • (2005) Trends Biochem Sci , vol.30 , pp. 43-52
    • Viatour, P.1    Merville, M.P.2    Bours, V.3    Chariot, A.4
  • 133
    • 84988697134 scopus 로고    scopus 로고
    • Identification of RNA binding proteins associated with dengue virus RNA in infected cells reveals temporally distinct host factor requirements
    • Viktorovskaya OV, Greco TM, Cristea IM, Thompson SR (2016) Identification of RNA binding proteins associated with dengue virus RNA in infected cells reveals temporally distinct host factor requirements. PLoS Negl Trop Dis 10: e0004921
    • (2016) PLoS Negl Trop Dis , vol.10
    • Viktorovskaya, O.V.1    Greco, T.M.2    Cristea, I.M.3    Thompson, S.R.4
  • 135
    • 84957542019 scopus 로고    scopus 로고
    • HIV-1 transgenic rats display mitochondrial abnormalities consistent with abnormal energy generation and distribution
    • Villeneuve LM, Purnell PR, Stauch KL, Callen SE, Buch SJ, Fox HS (2016) HIV-1 transgenic rats display mitochondrial abnormalities consistent with abnormal energy generation and distribution. J Neurovirol 22: 564–574
    • (2016) J Neurovirol , vol.22 , pp. 564-574
    • Villeneuve, L.M.1    Purnell, P.R.2    Stauch, K.L.3    Callen, S.E.4    Buch, S.J.5    Fox, H.S.6
  • 136
    • 85027923406 scopus 로고    scopus 로고
    • Protein turnover analysis in Salmonella Typhimurium during infection by dynamic SILAC, Topograph, and quantitative proteomics
    • Wang Z, Han QQ, Zhou MT, Chen X, Guo L (2016) Protein turnover analysis in Salmonella Typhimurium during infection by dynamic SILAC, Topograph, and quantitative proteomics. J Basic Microbiol 56: 801–811
    • (2016) J Basic Microbiol , vol.56 , pp. 801-811
    • Wang, Z.1    Han, Q.Q.2    Zhou, M.T.3    Chen, X.4    Guo, L.5
  • 138
    • 84879589505 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) glycoprotein gB promotes virus entry in trans acting as the viral fusion protein rather than as a receptor-binding protein
    • Wille PT, Wisner TW, Ryckman B, Johnson DC (2013) Human cytomegalovirus (HCMV) glycoprotein gB promotes virus entry in trans acting as the viral fusion protein rather than as a receptor-binding protein. MBio 4: e00332-13
    • (2013) MBio , vol.4
    • Wille, P.T.1    Wisner, T.W.2    Ryckman, B.3    Johnson, D.C.4
  • 139
    • 30444431914 scopus 로고    scopus 로고
    • NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation
    • Williams SA, Chen LF, Kwon H, Ruiz-Jarabo CM, Verdin E, Greene WC (2006) NF-kappaB p50 promotes HIV latency through HDAC recruitment and repression of transcriptional initiation. EMBO J 25: 139–149
    • (2006) EMBO J , vol.25 , pp. 139-149
    • Williams, S.A.1    Chen, L.F.2    Kwon, H.3    Ruiz-Jarabo, C.M.4    Verdin, E.5    Greene, W.C.6
  • 141
    • 84864390283 scopus 로고    scopus 로고
    • The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology
    • Wu W, Tran KC, Teng MN, Heesom KJ, Matthews DA, Barr JN, Hiscox JA (2012) The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology. J Virol 86: 7777–7789
    • (2012) J Virol , vol.86 , pp. 7777-7789
    • Wu, W.1    Tran, K.C.2    Teng, M.N.3    Heesom, K.J.4    Matthews, D.A.5    Barr, J.N.6    Hiscox, J.A.7
  • 142
    • 84881492654 scopus 로고    scopus 로고
    • Mitochondrial proteomic analysis of human host cells infected with H3N2 swine influenza virus
    • Wu X, Wang H, Bai L, Yu Y, Sun Z, Yan Y, Zhou J (2013) Mitochondrial proteomic analysis of human host cells infected with H3N2 swine influenza virus. J Proteomics 91: 136–150
    • (2013) J Proteomics , vol.91 , pp. 136-150
    • Wu, X.1    Wang, H.2    Bai, L.3    Yu, Y.4    Sun, Z.5    Yan, Y.6    Zhou, J.7
  • 144
    • 84886625085 scopus 로고    scopus 로고
    • Autoantibody recognition of an N-terminal epitope of hnRNP L marks the risk for developing HBV-related hepatocellular carcinoma
    • Yau WY, Shih HC, Tsai MH, Sheu JC, Chen CH, Chow LP (2013) Autoantibody recognition of an N-terminal epitope of hnRNP L marks the risk for developing HBV-related hepatocellular carcinoma. J Proteomics 94: 346–358
    • (2013) J Proteomics , vol.94 , pp. 346-358
    • Yau, W.Y.1    Shih, H.C.2    Tsai, M.H.3    Sheu, J.C.4    Chen, C.H.5    Chow, L.P.6
  • 145
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska DF, Gnad F, Schropp K, Wisniewski JR, Mann M (2012) Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542–548
    • (2012) Mol Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wisniewski, J.R.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.