메뉴 건너뛰기




Volumn 15, Issue 2, 2016, Pages 540-553

Ion-Current-Based Temporal Proteomic Profiling of Influenza-A-Virus-Infected Mouse Lungs Revealed Underlying Mechanisms of Altered Integrity of the Lung Microvascular Barrier

Author keywords

bottom up proteomics; host factors; influenza; ion current based quantification; microvascular barrier

Indexed keywords

CADHERIN; CATENIN; CLAUDIN; GELATINASE A; GELATINASE B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN ZO1; PROTEOME; STRESS ACTIVATED PROTEIN KINASE; SUPEROXIDE DISMUTASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TUMOR NECROSIS FACTOR ALPHA;

EID: 84957628834     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00927     Document Type: Article
Times cited : (12)

References (101)
  • 1
    • 79551553098 scopus 로고    scopus 로고
    • Pathogenesis of the 1918 Pandemic Influenza Virus
    • Watanabe, T.; Kawaoka, Y. Pathogenesis of the 1918 Pandemic Influenza Virus PLoS Pathog. 2011, 7, e1001218 10.1371/journal.ppat.1001218
    • (2011) PLoS Pathog. , vol.7 , pp. e1001218
    • Watanabe, T.1    Kawaoka, Y.2
  • 2
    • 79851496686 scopus 로고    scopus 로고
    • Emerging influenza antiviral resistance threats
    • Hayden, F. G.; de Jong, M. D. Emerging influenza antiviral resistance threats J. Infect. Dis. 2011, 203, 6-10 10.1093/infdis/jiq012
    • (2011) J. Infect. Dis. , vol.203 , pp. 6-10
    • Hayden, F.G.1    De Jong, M.D.2
  • 7
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P.; Rochon, Y.; Franza, B. R.; Aebersold, R. Correlation between protein and mRNA abundance in yeast Mol. Cell. Biol. 1999, 19, 1720-30 10.1128/MCB.19.3.1720
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 9
    • 0036468595 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis: Recent advances in sample preparation, detection and quantitation
    • Lilley, K. S.; Razzaq, A.; Dupree, P. Two-dimensional gel electrophoresis: recent advances in sample preparation, detection and quantitation Curr. Opin. Chem. Biol. 2002, 6, 46-50 10.1016/S1367-5931(01)00275-7
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 46-50
    • Lilley, K.S.1    Razzaq, A.2    Dupree, P.3
  • 10
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1, 376-86 10.1074/mcp.M200025-MCP200
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 11
    • 77957355995 scopus 로고    scopus 로고
    • Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells
    • Emmott, E.; Wise, H.; Loucaides, E. M.; Matthews, D. A.; Digard, P.; Hiscox, J. A. Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells J. Proteome Res. 2010, 9, 5335-45 10.1021/pr100593g
    • (2010) J. Proteome Res. , vol.9 , pp. 5335-5345
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4    Digard, P.5    Hiscox, J.A.6
  • 12
    • 43549083241 scopus 로고    scopus 로고
    • Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells
    • Liu, N.; Song, W.; Wang, P.; Lee, K.; Chan, W.; Chen, H.; Cai, Z. Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells Proteomics 2008, 8, 1851-8 10.1002/pmic.200700757
    • (2008) Proteomics , vol.8 , pp. 1851-1858
    • Liu, N.1    Song, W.2    Wang, P.3    Lee, K.4    Chan, W.5    Chen, H.6    Cai, Z.7
  • 14
    • 67650713700 scopus 로고    scopus 로고
    • Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines
    • Vester, D.; Rapp, E.; Gade, D.; Genzel, Y.; Reichl, U. Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines Proteomics 2009, 9, 3316-27 10.1002/pmic.200800893
    • (2009) Proteomics , vol.9 , pp. 3316-3327
    • Vester, D.1    Rapp, E.2    Gade, D.3    Genzel, Y.4    Reichl, U.5
  • 15
    • 84904876332 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of the influenza A virus nonstructural proteins NS1 and NS2 during natural cell infection identifies PACT as an NS1 target protein and antiviral host factor
    • Tawaratsumida, K.; Phan, V.; Hrincius, E. R.; High, A. A.; Webby, R.; Redecke, V.; Hacker, H. Quantitative proteomic analysis of the influenza A virus nonstructural proteins NS1 and NS2 during natural cell infection identifies PACT as an NS1 target protein and antiviral host factor J. Virol. 2014, 88, 9038-48 10.1128/JVI.00830-14
    • (2014) J. Virol. , vol.88 , pp. 9038-9048
    • Tawaratsumida, K.1    Phan, V.2    Hrincius, E.R.3    High, A.A.4    Webby, R.5    Redecke, V.6    Hacker, H.7
  • 16
    • 84887194533 scopus 로고    scopus 로고
    • Proteomic analysis at the subcellular level for host targets against influenza A virus (H1N1)
    • Zhao, H.; Yang, J.; Li, K.; Ding, X.; Lin, R.; Ma, Y.; Liu, J.; Zhong, Z.; Qian, X.; Bo, X.; Zhou, Z.; Wang, S. Proteomic analysis at the subcellular level for host targets against influenza A virus (H1N1) Antiviral Res. 2013, 100, 673-87 10.1016/j.antiviral.2013.10.005
    • (2013) Antiviral Res. , vol.100 , pp. 673-687
    • Zhao, H.1    Yang, J.2    Li, K.3    Ding, X.4    Lin, R.5    Ma, Y.6    Liu, J.7    Zhong, Z.8    Qian, X.9    Bo, X.10    Zhou, Z.11    Wang, S.12
  • 17
    • 84942895846 scopus 로고    scopus 로고
    • An Experimental Null method to guide the development of technical procedures and to control false positive discovery in quantitative proteomics
    • Shen, X.; Hu, Q.; Li, J.; Wang, J.; Qu, J. An Experimental Null method to guide the development of technical procedures and to control false positive discovery in quantitative proteomics J. Proteome Res. 2015, 14, 4147 10.1021/acs.jproteome.5b00200
    • (2015) J. Proteome Res. , vol.14 , pp. 4147
    • Shen, X.1    Hu, Q.2    Li, J.3    Wang, J.4    Qu, J.5
  • 19
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger, T.; Cox, J.; Ostasiewicz, P.; Wisniewski, J. R.; Mann, M. Super-SILAC mix for quantitative proteomics of human tumor tissue Nat. Methods 2010, 7, 383-385 10.1038/nmeth.1446
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 21
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese, S.; Reidegeld, K. A.; Meyer, H. E.; Warscheid, B. Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research Proteomics 2007, 7, 340-50 10.1002/pmic.200600422
    • (2007) Proteomics , vol.7 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3    Warscheid, B.4
  • 23
    • 77957957247 scopus 로고    scopus 로고
    • The mitochondrial proteome and human disease
    • Calvo, S. E.; Mootha, V. K. The mitochondrial proteome and human disease Annu. Rev. Genomics Hum. Genet. 2010, 11, 25-44 10.1146/annurev-genom-082509-141720
    • (2010) Annu. Rev. Genomics Hum. Genet. , vol.11 , pp. 25-44
    • Calvo, S.E.1    Mootha, V.K.2
  • 25
    • 33750586269 scopus 로고    scopus 로고
    • Aqueous polymer two-phase systems: Effective tools for plasma membrane proteomics
    • Schindler, J.; Nothwang, H. G. Aqueous polymer two-phase systems: effective tools for plasma membrane proteomics Proteomics 2006, 6, 5409-17 10.1002/pmic.200600243
    • (2006) Proteomics , vol.6 , pp. 5409-5417
    • Schindler, J.1    Nothwang, H.G.2
  • 26
    • 55349095003 scopus 로고    scopus 로고
    • Protein quantitation through targeted mass spectrometry: The way out of biomarker purgatory?
    • Carr, S. A.; Anderson, L. Protein quantitation through targeted mass spectrometry: the way out of biomarker purgatory? Clin. Chem. 2008, 54, 1749-52 10.1373/clinchem.2008.114686
    • (2008) Clin. Chem. , vol.54 , pp. 1749-1752
    • Carr, S.A.1    Anderson, L.2
  • 27
    • 77957833984 scopus 로고    scopus 로고
    • Cancer biomarkers: Can we turn recent failures into success?
    • Diamandis, E. P. Cancer biomarkers: can we turn recent failures into success? J. Natl. Cancer Inst 2010, 102, 1462-7 10.1093/jnci/djq306
    • (2010) J. Natl. Cancer Inst , vol.102 , pp. 1462-1467
    • Diamandis, E.P.1
  • 28
    • 33747030845 scopus 로고    scopus 로고
    • Protein biomarker discovery and validation: The long and uncertain path to clinical utility
    • Rifai, N.; Gillette, M. A.; Carr, S. A. Protein biomarker discovery and validation: the long and uncertain path to clinical utility Nat. Biotechnol. 2006, 24, 971-83 10.1038/nbt1235
    • (2006) Nat. Biotechnol. , vol.24 , pp. 971-983
    • Rifai, N.1    Gillette, M.A.2    Carr, S.A.3
  • 29
    • 84878053091 scopus 로고    scopus 로고
    • Normalization and missing value imputation for label-free LC-MS analysis
    • Karpievitch, Y. V.; Dabney, A. R.; Smith, R. D. Normalization and missing value imputation for label-free LC-MS analysis BMC Bioinf. 2012, 13, S5-S5 10.1186/1471-2105-13-S16-S5
    • (2012) BMC Bioinf. , vol.13 , pp. S5-S5
    • Karpievitch, Y.V.1    Dabney, A.R.2    Smith, R.D.3
  • 30
    • 84927130414 scopus 로고    scopus 로고
    • Surfactant-Aided Precipitation/on-Pellet-Digestion (SOD) Procedure Provides Robust and Rapid Sample Preparation for Reproducible, Accurate and Sensitive LC/MS Quantification of Therapeutic Protein in Plasma and Tissues
    • An, B.; Zhang, M.; Johnson, R. W.; Qu, J. Surfactant-Aided Precipitation/on-Pellet-Digestion (SOD) Procedure Provides Robust and Rapid Sample Preparation for Reproducible, Accurate and Sensitive LC/MS Quantification of Therapeutic Protein in Plasma and Tissues Anal. Chem. 2015, 87, 4023-9 10.1021/acs.analchem.5b00350
    • (2015) Anal. Chem. , vol.87 , pp. 4023-4029
    • An, B.1    Zhang, M.2    Johnson, R.W.3    Qu, J.4
  • 31
    • 67049119810 scopus 로고    scopus 로고
    • A straightforward and highly efficient precipitation/on-pellet digestion procedure coupled with a long gradient nano-LC separation and Orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome
    • Duan, X.; Young, R.; Straubinger, R. M.; Page, B.; Cao, J.; Wang, H.; Yu, H.; Canty, J. M.; Qu, J. A straightforward and highly efficient precipitation/on-pellet digestion procedure coupled with a long gradient nano-LC separation and Orbitrap mass spectrometry for label-free expression profiling of the swine heart mitochondrial proteome J. Proteome Res. 2009, 8, 2838-50 10.1021/pr900001t
    • (2009) J. Proteome Res. , vol.8 , pp. 2838-2850
    • Duan, X.1    Young, R.2    Straubinger, R.M.3    Page, B.4    Cao, J.5    Wang, H.6    Yu, H.7    Canty, J.M.8    Qu, J.9
  • 32
    • 84898719933 scopus 로고    scopus 로고
    • Systematic assessment of survey scan and MS2-based abundance strategies for label-free quantitative proteomics using high-resolution MS data
    • Tu, C.; Li, J.; Sheng, Q.; Zhang, M.; Qu, J. Systematic assessment of survey scan and MS2-based abundance strategies for label-free quantitative proteomics using high-resolution MS data J. Proteome Res. 2014, 13, 2069-79 10.1021/pr401206m
    • (2014) J. Proteome Res. , vol.13 , pp. 2069-2079
    • Tu, C.1    Li, J.2    Sheng, Q.3    Zhang, M.4    Qu, J.5
  • 33
    • 77949695293 scopus 로고    scopus 로고
    • Scaffold: A bioinformatic tool for validating MS/MS-based proteomic studies
    • Searle, B. C. Scaffold: a bioinformatic tool for validating MS/MS-based proteomic studies Proteomics 2010, 10, 1265-9 10.1002/pmic.200900437
    • (2010) Proteomics , vol.10 , pp. 1265-1269
    • Searle, B.C.1
  • 34
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias, J. E.; Haas, W.; Faherty, B. K.; Gygi, S. P. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations Nat. Methods 2005, 2, 667-75 10.1038/nmeth785
    • (2005) Nat. Methods , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 35
    • 78649820507 scopus 로고    scopus 로고
    • Mass spectrometric discovery and selective reaction monitoring (SRM) of putative protein biomarker candidates in first trimester Trisomy 21 maternal serum
    • Lopez, M. F.; Kuppusamy, R.; Sarracino, D. A.; Prakash, A.; Athanas, M.; Krastins, B.; Rezai, T.; Sutton, J. N.; Peterman, S.; Nicolaides, K. Mass spectrometric discovery and selective reaction monitoring (SRM) of putative protein biomarker candidates in first trimester Trisomy 21 maternal serum J. Proteome Res. 2011, 10, 133-42 10.1021/pr100153j
    • (2011) J. Proteome Res. , vol.10 , pp. 133-142
    • Lopez, M.F.1    Kuppusamy, R.2    Sarracino, D.A.3    Prakash, A.4    Athanas, M.5    Krastins, B.6    Rezai, T.7    Sutton, J.N.8    Peterman, S.9    Nicolaides, K.10
  • 36
    • 79953184690 scopus 로고    scopus 로고
    • Multiple hypothesis testing in proteomics: A strategy for experimental work
    • Diz, A. P.; Carvajal-Rodriguez, A.; Skibinski, D. O. Multiple hypothesis testing in proteomics: a strategy for experimental work Mol. Cell. Proteomics 2011, 10, M110.004374 10.1074/mcp.M110.004374
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. M110004374
    • Diz, A.P.1    Carvajal-Rodriguez, A.2    Skibinski, D.O.3
  • 37
    • 84906243743 scopus 로고    scopus 로고
    • Highly multiplexed and reproducible ion-current-based strategy for large-scale quantitative proteomics and the application to protein expression dynamics induced by methylprednisolone in 60 rats
    • Nouri-Nigjeh, E.; Sukumaran, S.; Tu, C.; Li, J.; Shen, X.; Duan, X.; DuBois, D. C.; Almon, R. R.; Jusko, W. J.; Qu, J. Highly multiplexed and reproducible ion-current-based strategy for large-scale quantitative proteomics and the application to protein expression dynamics induced by methylprednisolone in 60 rats Anal. Chem. 2014, 86, 8149-57 10.1021/ac501380s
    • (2014) Anal. Chem. , vol.86 , pp. 8149-8157
    • Nouri-Nigjeh, E.1    Sukumaran, S.2    Tu, C.3    Li, J.4    Shen, X.5    Duan, X.6    DuBois, D.C.7    Almon, R.R.8    Jusko, W.J.9    Qu, J.10
  • 38
    • 84893852473 scopus 로고    scopus 로고
    • Large-scale, ion-current-based proteomics investigation of bronchoalveolar lavage fluid in chronic obstructive pulmonary disease patients
    • Tu, C.; Mammen, M. J.; Li, J.; Shen, X.; Jiang, X.; Hu, Q.; Wang, J.; Sethi, S.; Qu, J. Large-scale, ion-current-based proteomics investigation of bronchoalveolar lavage fluid in chronic obstructive pulmonary disease patients J. Proteome Res. 2014, 13, 627-39 10.1021/pr4007602
    • (2014) J. Proteome Res. , vol.13 , pp. 627-639
    • Tu, C.1    Mammen, M.J.2    Li, J.3    Shen, X.4    Jiang, X.5    Hu, Q.6    Wang, J.7    Sethi, S.8    Qu, J.9
  • 39
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox, J.; Hein, M. Y.; Luber, C. A.; Paron, I.; Nagaraj, N.; Mann, M. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ Mol. Cell. Proteomics 2014, 13, 2513-26 10.1074/mcp.M113.031591
    • (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
  • 40
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2008, 4, 44-57 10.1038/nprot.2008.211
    • (2008) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 41
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305, 567-80 10.1006/jmbi.2000.4315
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 43
    • 84881363980 scopus 로고    scopus 로고
    • High-Resolution Temporal Response Patterns to Influenza Vaccine Reveal a Distinct Human Plasma Cell Gene Signature
    • Henn, A. D.; Wu, S.; Qiu, X.; Ruda, M.; Stover, M.; Yang, H.; Liu, Z.; Welle, S. L.; Holden-Wiltse, J.; Wu, H.; Zand, M. S. High-Resolution Temporal Response Patterns to Influenza Vaccine Reveal a Distinct Human Plasma Cell Gene Signature Sci. Rep. 2013, 3, 2327 10.1038/srep02327
    • (2013) Sci. Rep. , vol.3 , pp. 2327
    • Henn, A.D.1    Wu, S.2    Qiu, X.3    Ruda, M.4    Stover, M.5    Yang, H.6    Liu, Z.7    Welle, S.L.8    Holden-Wiltse, J.9    Wu, H.10    Zand, M.S.11
  • 44
    • 84864011948 scopus 로고    scopus 로고
    • Global Transcriptome Analysis in Influenza-Infected Mouse Lungs Reveals the Kinetics of Innate and Adaptive Host Immune Responses
    • Pommerenke, C.; Wilk, E.; Srivastava, B.; Schulze, A.; Novoselova, N.; Geffers, R.; Schughart, K. Global Transcriptome Analysis in Influenza-Infected Mouse Lungs Reveals the Kinetics of Innate and Adaptive Host Immune Responses PLoS One 2012, 7, e41169 10.1371/journal.pone.0041169
    • (2012) PLoS One , vol.7 , pp. e41169
    • Pommerenke, C.1    Wilk, E.2    Srivastava, B.3    Schulze, A.4    Novoselova, N.5    Geffers, R.6    Schughart, K.7
  • 45
    • 77953298848 scopus 로고    scopus 로고
    • Quantifying the early immune response and adaptive immune response kinetics in mice infected with influenza A virus
    • Miao, H.; Hollenbaugh, J. A.; Zand, M. S.; Holden-Wiltse, J.; Mosmann, T. R.; Perelson, A. S.; Wu, H.; Topham, D. J. Quantifying the early immune response and adaptive immune response kinetics in mice infected with influenza A virus J. Virol 2010, 84, 6687-98 10.1128/JVI.00266-10
    • (2010) J. Virol , vol.84 , pp. 6687-6698
    • Miao, H.1    Hollenbaugh, J.A.2    Zand, M.S.3    Holden-Wiltse, J.4    Mosmann, T.R.5    Perelson, A.S.6    Wu, H.7    Topham, D.J.8
  • 47
    • 80555154911 scopus 로고    scopus 로고
    • Modeling of influenza-specific CD8+ T cells during the primary response indicates that the spleen is a major source of effectors
    • Wu, H.; Kumar, A.; Miao, H.; Holden-Wiltse, J.; Mosmann, T. R.; Livingstone, A. M.; Belz, G. T.; Perelson, A. S.; Zand, M. S.; Topham, D. J. Modeling of influenza-specific CD8+ T cells during the primary response indicates that the spleen is a major source of effectors J. Immunol. 2011, 187, 4474-82 10.4049/jimmunol.1101443
    • (2011) J. Immunol. , vol.187 , pp. 4474-4482
    • Wu, H.1    Kumar, A.2    Miao, H.3    Holden-Wiltse, J.4    Mosmann, T.R.5    Livingstone, A.M.6    Belz, G.T.7    Perelson, A.S.8    Zand, M.S.9    Topham, D.J.10
  • 48
    • 77957232334 scopus 로고    scopus 로고
    • Advances in shotgun proteomics and the analysis of membrane proteomes
    • Gilmore, J. M.; Washburn, M. P. Advances in shotgun proteomics and the analysis of membrane proteomes J. Proteomics 2010, 73, 2078-91 10.1016/j.jprot.2010.08.005
    • (2010) J. Proteomics , vol.73 , pp. 2078-2091
    • Gilmore, J.M.1    Washburn, M.P.2
  • 49
    • 84899854225 scopus 로고    scopus 로고
    • Reproducible Ion-Current-Based Approach for 24-Plex Comparison of the Tissue Proteomes of Hibernating versus Normal Myocardium in Swine Models
    • Qu, J.; Young, R.; Page, B. J.; Shen, X.; Tata, N.; Li, J.; Duan, X.; Fallavollita, J. A.; Canty, J. M., Jr. Reproducible Ion-Current-Based Approach for 24-Plex Comparison of the Tissue Proteomes of Hibernating versus Normal Myocardium in Swine Models J. Proteome Res. 2014, 13, 2571 10.1021/pr5000472
    • (2014) J. Proteome Res. , vol.13 , pp. 2571
    • Qu, J.1    Young, R.2    Page, B.J.3    Shen, X.4    Tata, N.5    Li, J.6    Duan, X.7    Fallavollita, J.A.8    Canty, J.M.9
  • 50
    • 84890574613 scopus 로고    scopus 로고
    • Ion-current-based proteomic profiling of the retina in a rat model of Smith-Lemli-Opitz syndrome
    • Tu, C.; Li, J.; Jiang, X.; Sheflin, L. G.; Pfeffer, B. A.; Behringer, M.; Fliesler, S. J.; Qu, J. Ion-current-based proteomic profiling of the retina in a rat model of Smith-Lemli-Opitz syndrome Mol. Cell. Proteomics 2013, 12, 3583-98 10.1074/mcp.M113.027847
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3583-3598
    • Tu, C.1    Li, J.2    Jiang, X.3    Sheflin, L.G.4    Pfeffer, B.A.5    Behringer, M.6    Fliesler, S.J.7    Qu, J.8
  • 51
    • 84874602863 scopus 로고    scopus 로고
    • Integral membrane proteins and bilayer proteomics
    • Whitelegge, J. P. Integral membrane proteins and bilayer proteomics Anal. Chem. 2013, 85, 2558-68 10.1021/ac303064a
    • (2013) Anal. Chem. , vol.85 , pp. 2558-2568
    • Whitelegge, J.P.1
  • 52
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C.; Yates, J. R., 3rd The application of mass spectrometry to membrane proteomics Nat. Biotechnol. 2003, 21, 262-7 10.1038/nbt0303-262
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates, J.R.2
  • 53
    • 84915820357 scopus 로고    scopus 로고
    • ICan: An Optimized Ion-Current-Based Quantification Procedure with Enhanced Quantitative Accuracy and Sensitivity in Biomarker Discovery
    • Tu, C.; Sheng, Q.; Li, J.; Shen, X.; Zhang, M.; Shyr, Y.; Qu, J. ICan: An Optimized Ion-Current-Based Quantification Procedure with Enhanced Quantitative Accuracy and Sensitivity in Biomarker Discovery J. Proteome Res. 2014, 13, 5888-5897 10.1021/pr5008224
    • (2014) J. Proteome Res. , vol.13 , pp. 5888-5897
    • Tu, C.1    Sheng, Q.2    Li, J.3    Shen, X.4    Zhang, M.5    Shyr, Y.6    Qu, J.7
  • 54
    • 48049094159 scopus 로고    scopus 로고
    • The role of adherens junctions and VE-cadherin in the control of vascular permeability
    • Dejana, E.; Orsenigo, F.; Lampugnani, M. G. The role of adherens junctions and VE-cadherin in the control of vascular permeability J. Cell Sci. 2008, 121, 2115-22 10.1242/jcs.017897
    • (2008) J. Cell Sci. , vol.121 , pp. 2115-2122
    • Dejana, E.1    Orsenigo, F.2    Lampugnani, M.G.3
  • 56
    • 79957464589 scopus 로고    scopus 로고
    • Claudins in lung diseases
    • Soini, Y. Claudins in lung diseases Respir Res. 2011, 12, 70 10.1186/1465-9921-12-70
    • (2011) Respir Res. , vol.12 , pp. 70
    • Soini, Y.1
  • 57
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • Hu, J.; Van den Steen, P. E.; Sang, Q. X.; Opdenakker, G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases Nat. Rev. Drug Discovery 2007, 6, 480-98 10.1038/nrd2308
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 480-498
    • Hu, J.1    Van Den Steen, P.E.2    Sang, Q.X.3    Opdenakker, G.4
  • 58
    • 34548397756 scopus 로고    scopus 로고
    • Proteolytic degradation of VE-cadherin alters the blood-retinal barrier in diabetes
    • Navaratna, D.; McGuire, P. G.; Menicucci, G.; Das, A. Proteolytic degradation of VE-cadherin alters the blood-retinal barrier in diabetes Diabetes 2007, 56, 2380-7 10.2337/db06-1694
    • (2007) Diabetes , vol.56 , pp. 2380-2387
    • Navaratna, D.1    McGuire, P.G.2    Menicucci, G.3    Das, A.4
  • 61
    • 0032763782 scopus 로고    scopus 로고
    • Influenza A virus infection modulates the expression of type IV collagenase in epithelial cells
    • Yeo, S. J.; Kim, S. J.; Kim, J. H.; Lee, H. J.; Kook, Y. H. Influenza A virus infection modulates the expression of type IV collagenase in epithelial cells Arch. Virol. 1999, 144, 1361-70 10.1007/s007050050592
    • (1999) Arch. Virol. , vol.144 , pp. 1361-1370
    • Yeo, S.J.1    Kim, S.J.2    Kim, J.H.3    Lee, H.J.4    Kook, Y.H.5
  • 62
    • 84888204752 scopus 로고    scopus 로고
    • Influenza A virus induction of oxidative stress and MMP-9 is associated with severe lung pathology in a mouse model
    • Lee, Y. H.; Lai, C. L.; Hsieh, S. H.; Shieh, C. C.; Huang, L. M.; Wu-Hsieh, B. A. Influenza A virus induction of oxidative stress and MMP-9 is associated with severe lung pathology in a mouse model Virus Res. 2013, 178, 411-22 10.1016/j.virusres.2013.09.011
    • (2013) Virus Res. , vol.178 , pp. 411-422
    • Lee, Y.H.1    Lai, C.L.2    Hsieh, S.H.3    Shieh, C.C.4    Huang, L.M.5    Wu-Hsieh, B.A.6
  • 63
    • 30144439195 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-9 (MMP-9) in TNF-stimulated neutrophils: Novel pathways for tertiary granule release
    • Chakrabarti, S.; Zee, J. M.; Patel, K. D. Regulation of matrix metalloproteinase-9 (MMP-9) in TNF-stimulated neutrophils: novel pathways for tertiary granule release J. Leukocyte Biol. 2005, 79, 214-22 10.1189/jlb.0605353
    • (2005) J. Leukocyte Biol. , vol.79 , pp. 214-222
    • Chakrabarti, S.1    Zee, J.M.2    Patel, K.D.3
  • 64
    • 55249119840 scopus 로고    scopus 로고
    • Signaling pathway for TNF-alpha-induced MMP-9 expression: Mediation through p38 MAP kinase, and inhibition by anti-cancer molecule magnolol in human urinary bladder cancer 5637 cells
    • Lee, S. J.; Park, S. S.; Lee, U. S.; Kim, W. J.; Moon, S. K. Signaling pathway for TNF-alpha-induced MMP-9 expression: mediation through p38 MAP kinase, and inhibition by anti-cancer molecule magnolol in human urinary bladder cancer 5637 cells Int. Immunopharmacol. 2008, 8, 1821-6 10.1016/j.intimp.2008.08.018
    • (2008) Int. Immunopharmacol. , vol.8 , pp. 1821-1826
    • Lee, S.J.1    Park, S.S.2    Lee, U.S.3    Kim, W.J.4    Moon, S.K.5
  • 65
    • 33750331488 scopus 로고    scopus 로고
    • Wogonin suppresses TNF-alpha-induced MMP-9 expression by blocking the NF-kappaB activation via MAPK signaling pathways in human aortic smooth muscle cells
    • Lee, S. O.; Jeong, Y. J.; Yu, M. H.; Lee, J. W.; Hwangbo, M. H.; Kim, C. H.; Lee, I. S. Wogonin suppresses TNF-alpha-induced MMP-9 expression by blocking the NF-kappaB activation via MAPK signaling pathways in human aortic smooth muscle cells Biochem. Biophys. Res. Commun. 2006, 351, 118-25 10.1016/j.bbrc.2006.10.006
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 118-125
    • Lee, S.O.1    Jeong, Y.J.2    Yu, M.H.3    Lee, J.W.4    Hwangbo, M.H.5    Kim, C.H.6    Lee, I.S.7
  • 66
    • 0042235524 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells
    • Mizumura, K.; Hashimoto, S.; Maruoka, S.; Gon, Y.; Kitamura, N.; Matsumoto, K.; Hayashi, S.; Shimizu, K.; Horie, T. Role of mitogen-activated protein kinases in influenza virus induction of prostaglandin E2 from arachidonic acid in bronchial epithelial cells Clin. Exp. Allergy 2003, 33, 1244-51 10.1046/j.1365-2222.2003.01750.x
    • (2003) Clin. Exp. Allergy , vol.33 , pp. 1244-1251
    • Mizumura, K.1    Hashimoto, S.2    Maruoka, S.3    Gon, Y.4    Kitamura, N.5    Matsumoto, K.6    Hayashi, S.7    Shimizu, K.8    Horie, T.9
  • 68
    • 33746225582 scopus 로고    scopus 로고
    • Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-alpha in human monocytes
    • Nguyen, J.; Gogusev, J.; Knapnougel, P.; Bauvois, B. Protein tyrosine kinase and p38 MAP kinase pathways are involved in stimulation of matrix metalloproteinase-9 by TNF-alpha in human monocytes Immunol. Lett. 2006, 106, 34-41 10.1016/j.imlet.2006.04.003
    • (2006) Immunol. Lett. , vol.106 , pp. 34-41
    • Nguyen, J.1    Gogusev, J.2    Knapnougel, P.3    Bauvois, B.4
  • 70
    • 81555228707 scopus 로고    scopus 로고
    • Immune responses to influenza virus infection
    • Kreijtz, J. H.; Fouchier, R. A.; Rimmelzwaan, G. F. Immune responses to influenza virus infection Virus Res. 2011, 162, 19-30 10.1016/j.virusres.2011.09.022
    • (2011) Virus Res. , vol.162 , pp. 19-30
    • Kreijtz, J.H.1    Fouchier, R.A.2    Rimmelzwaan, G.F.3
  • 71
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins, J. W.; Rice, C. M. Interferon-stimulated genes and their antiviral effector functions Curr. Opin. Virol. 2011, 1, 519-25 10.1016/j.coviro.2011.10.008
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 72
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: A complex web of host defenses
    • Schneider, W. M.; Chevillotte, M. D.; Rice, C. M. Interferon-stimulated genes: a complex web of host defenses Annu. Rev. Immunol. 2014, 32, 513-45 10.1146/annurev-immunol-032713-120231
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 513-545
    • Schneider, W.M.1    Chevillotte, M.D.2    Rice, C.M.3
  • 73
    • 84863285086 scopus 로고    scopus 로고
    • Systematic identification of type i and type II interferon-induced antiviral factors
    • Liu, S. Y.; Sanchez, D. J.; Aliyari, R.; Lu, S.; Cheng, G. Systematic identification of type I and type II interferon-induced antiviral factors Proc. Natl. Acad. Sci. U. S. A. 2012, 109, 4239-44 10.1073/pnas.1114981109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 4239-4244
    • Liu, S.Y.1    Sanchez, D.J.2    Aliyari, R.3    Lu, S.4    Cheng, G.5
  • 74
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type i interferon antiviral response
    • Schoggins, J. W.; Wilson, S. J.; Panis, M.; Murphy, M. Y.; Jones, C. T.; Bieniasz, P.; Rice, C. M. A diverse range of gene products are effectors of the type I interferon antiviral response Nature 2011, 472, 481-5 10.1038/nature09907
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6    Rice, C.M.7
  • 75
    • 78651506340 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their protein products: What and how?
    • Borden, E. C.; Williams, B. R. Interferon-stimulated genes and their protein products: what and how? J. Interferon Cytokine Res. 2011, 31, 1-4 10.1089/jir.2010.0129
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 1-4
    • Borden, E.C.1    Williams, B.R.2
  • 76
    • 79951671973 scopus 로고    scopus 로고
    • New developments in the induction and antiviral effectors of type i interferon
    • Liu, S. Y.; Sanchez, D. J.; Cheng, G. New developments in the induction and antiviral effectors of type I interferon Curr. Opin. Immunol. 2011, 23, 57-64 10.1016/j.coi.2010.11.003
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 57-64
    • Liu, S.Y.1    Sanchez, D.J.2    Cheng, G.3
  • 77
    • 77951481221 scopus 로고    scopus 로고
    • Antiviral activity of innate immune protein ISG15
    • Harty, R. N.; Pitha, P. M.; Okumura, A. Antiviral activity of innate immune protein ISG15 J. Innate Immun. 2009, 1, 397-404 10.1159/000226245
    • (2009) J. Innate Immun. , vol.1 , pp. 397-404
    • Harty, R.N.1    Pitha, P.M.2    Okumura, A.3
  • 78
    • 58149502576 scopus 로고    scopus 로고
    • Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection
    • Lai, C.; Struckhoff, J. J.; Schneider, J.; Martinez-Sobrido, L.; Wolff, T.; Garcia-Sastre, A.; Zhang, D. E.; Lenschow, D. J. Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection J. Virol 2009, 83, 1147-51 10.1128/JVI.00105-08
    • (2009) J. Virol , vol.83 , pp. 1147-1151
    • Lai, C.1    Struckhoff, J.J.2    Schneider, J.3    Martinez-Sobrido, L.4    Wolff, T.5    Garcia-Sastre, A.6    Zhang, D.E.7    Lenschow, D.J.8
  • 79
    • 79251564770 scopus 로고    scopus 로고
    • RIG-I/MDA5/MAVS are required to signal a protective IFN response in rotavirus-infected intestinal epithelium
    • Broquet, A. H.; Hirata, Y.; McAllister, C. S.; Kagnoff, M. F. RIG-I/MDA5/MAVS are required to signal a protective IFN response in rotavirus-infected intestinal epithelium J. Immunol. 2011, 186, 1618-26 10.4049/jimmunol.1002862
    • (2011) J. Immunol. , vol.186 , pp. 1618-1626
    • Broquet, A.H.1    Hirata, Y.2    McAllister, C.S.3    Kagnoff, M.F.4
  • 80
    • 84897952004 scopus 로고    scopus 로고
    • Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5′-terminal regions of cap0-, cap1- and 5′ppp- mRNAs
    • Kumar, P.; Sweeney, T. R.; Skabkin, M. A.; Skabkina, O. V.; Hellen, C. U.; Pestova, T. V. Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5′-terminal regions of cap0-, cap1- and 5′ppp- mRNAs Nucleic Acids Res. 2014, 42, 3228-45 10.1093/nar/gkt1321
    • (2014) Nucleic Acids Res. , vol.42 , pp. 3228-3245
    • Kumar, P.1    Sweeney, T.R.2    Skabkin, M.A.3    Skabkina, O.V.4    Hellen, C.U.5    Pestova, T.V.6
  • 81
    • 84871484827 scopus 로고    scopus 로고
    • The broad-spectrum antiviral functions of IFIT and IFITM proteins
    • Diamond, M. S.; Farzan, M. The broad-spectrum antiviral functions of IFIT and IFITM proteins Nat. Rev. Immunol. 2012, 13, 46-57 10.1038/nri3344
    • (2012) Nat. Rev. Immunol. , vol.13 , pp. 46-57
    • Diamond, M.S.1    Farzan, M.2
  • 82
    • 84901337841 scopus 로고    scopus 로고
    • IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion
    • Desai, T. M.; Marin, M.; Chin, C. R.; Savidis, G.; Brass, A. L.; Melikyan, G. B. IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion PLoS Pathog. 2014, 10, e1004048 10.1371/journal.ppat.1004048
    • (2014) PLoS Pathog. , vol.10 , pp. e1004048
    • Desai, T.M.1    Marin, M.2    Chin, C.R.3    Savidis, G.4    Brass, A.L.5    Melikyan, G.B.6
  • 83
    • 79957945853 scopus 로고    scopus 로고
    • Viral-mediated inhibition of antioxidant enzymes contributes to the pathogenesis of severe respiratory syncytial virus bronchiolitis
    • Hosakote, Y. M.; Jantzi, P. D.; Esham, D. L.; Spratt, H.; Kurosky, A.; Casola, A.; Garofalo, R. P. Viral-mediated inhibition of antioxidant enzymes contributes to the pathogenesis of severe respiratory syncytial virus bronchiolitis Am. J. Respir. Crit. Care Med. 2011, 183, 1550-60 10.1164/rccm.201010-1755OC
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , pp. 1550-1560
    • Hosakote, Y.M.1    Jantzi, P.D.2    Esham, D.L.3    Spratt, H.4    Kurosky, A.5    Casola, A.6    Garofalo, R.P.7
  • 84
    • 69449093559 scopus 로고    scopus 로고
    • Respiratory syncytial virus induces oxidative stress by modulating antioxidant enzymes
    • Hosakote, Y. M.; Liu, T.; Castro, S. M.; Garofalo, R. P.; Casola, A. Respiratory syncytial virus induces oxidative stress by modulating antioxidant enzymes Am. J. Respir. Cell Mol. Biol. 2009, 41, 348-57 10.1165/rcmb.2008-0330OC
    • (2009) Am. J. Respir. Cell Mol. Biol. , vol.41 , pp. 348-357
    • Hosakote, Y.M.1    Liu, T.2    Castro, S.M.3    Garofalo, R.P.4    Casola, A.5
  • 85
    • 17644373481 scopus 로고    scopus 로고
    • Pulmonary and systemic oxidant/antioxidant imbalance in chronic obstructive pulmonary disease
    • MacNee, W. Pulmonary and systemic oxidant/antioxidant imbalance in chronic obstructive pulmonary disease Proc. Am. Thorac. Soc. 2005, 2, 50-60 10.1513/pats.200411-056SF
    • (2005) Proc. Am. Thorac. Soc. , vol.2 , pp. 50-60
    • MacNee, W.1
  • 86
    • 84857081426 scopus 로고    scopus 로고
    • Major Shifts in the Spatio-Temporal Distribution of Lung Antioxidant Enzymes during Influenza Pneumonia
    • Yamada, Y.; Limmon, G. V.; Zheng, D.; Li, N.; Li, L.; Yin, L.; Chow, V. T. K.; Chen, J.; Engelward, B. P. Major Shifts in the Spatio-Temporal Distribution of Lung Antioxidant Enzymes during Influenza Pneumonia PLoS One 2012, 7, e31494 10.1371/journal.pone.0031494
    • (2012) PLoS One , vol.7 , pp. e31494
    • Yamada, Y.1    Limmon, G.V.2    Zheng, D.3    Li, N.4    Li, L.5    Yin, L.6    Chow, V.T.K.7    Chen, J.8    Engelward, B.P.9
  • 87
    • 0034721815 scopus 로고    scopus 로고
    • Modulation of glutathione S-transferase alpha by hepatitis B virus and the chemopreventive drug oltipraz
    • Jaitovitch-Groisman, I.; Fotouhi-Ardakani, N.; Schecter, R. L.; Woo, A.; Alaoui-Jamali, M. A.; Batist, G. Modulation of glutathione S-transferase alpha by hepatitis B virus and the chemopreventive drug oltipraz J. Biol. Chem. 2000, 275, 33395-33403 10.1074/jbc.M003754200
    • (2000) J. Biol. Chem. , vol.275 , pp. 33395-33403
    • Jaitovitch-Groisman, I.1    Fotouhi-Ardakani, N.2    Schecter, R.L.3    Woo, A.4    Alaoui-Jamali, M.A.5    Batist, G.6
  • 91
    • 70349174605 scopus 로고    scopus 로고
    • Influenza as a trigger for acute myocardial infarction or death from cardiovascular disease: A systematic review
    • Warren-Gash, C.; Smeeth, L.; Hayward, A. C. Influenza as a trigger for acute myocardial infarction or death from cardiovascular disease: a systematic review Lancet Infect. Dis. 2009, 9, 601-610 10.1016/S1473-3099(09)70233-6
    • (2009) Lancet Infect. Dis. , vol.9 , pp. 601-610
    • Warren-Gash, C.1    Smeeth, L.2    Hayward, A.C.3
  • 96
    • 0035826840 scopus 로고    scopus 로고
    • High-density lipoprotein loses its anti-inflammatory properties during acute influenza a infection
    • Van Lenten, B. J.; Wagner, A. C.; Nayak, D. P.; Hama, S.; Navab, M.; Fogelman, A. M. High-density lipoprotein loses its anti-inflammatory properties during acute influenza a infection Circulation 2001, 103, 2283-8 10.1161/01.CIR.103.18.2283
    • (2001) Circulation , vol.103 , pp. 2283-2288
    • Van Lenten, B.J.1    Wagner, A.C.2    Nayak, D.P.3    Hama, S.4    Navab, M.5    Fogelman, A.M.6
  • 97
    • 78650815261 scopus 로고    scopus 로고
    • The three-gene paraoxonase family: Physiologic roles, actions and regulation
    • Precourt, L. P.; Amre, D.; Denis, M. C.; Lavoie, J. C.; Delvin, E.; Seidman, E.; Levy, E. The three-gene paraoxonase family: physiologic roles, actions and regulation Atherosclerosis 2011, 214, 20-36 10.1016/j.atherosclerosis.2010.08.076
    • (2011) Atherosclerosis , vol.214 , pp. 20-36
    • Precourt, L.P.1    Amre, D.2    Denis, M.C.3    Lavoie, J.C.4    Delvin, E.5    Seidman, E.6    Levy, E.7
  • 98
    • 33745964245 scopus 로고    scopus 로고
    • Human paraoxonase-1 overexpression inhibits atherosclerosis in a mouse model of metabolic syndrome
    • Mackness, B.; Quarck, R.; Verreth, W.; Mackness, M.; Holvoet, P. Human paraoxonase-1 overexpression inhibits atherosclerosis in a mouse model of metabolic syndrome Arterioscler., Thromb., Vasc. Biol. 2006, 26, 1545-50 10.1161/01.ATV.0000222924.62641.aa
    • (2006) Arterioscler., Thromb., Vasc. Biol. , vol.26 , pp. 1545-1550
    • Mackness, B.1    Quarck, R.2    Verreth, W.3    Mackness, M.4    Holvoet, P.5
  • 101
    • 0028859490 scopus 로고
    • Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures
    • Van Lenten, B. J.; Hama, S. Y.; de Beer, F. C.; Stafforini, D. M.; McIntyre, T. M.; Prescott, S. M.; La Du, B. N.; Fogelman, A. M.; Navab, M. Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures J. Clin. Invest. 1995, 96, 2758-67 10.1172/JCI118345
    • (1995) J. Clin. Invest. , vol.96 , pp. 2758-2767
    • Van Lenten, B.J.1    Hama, S.Y.2    De Beer, F.C.3    Stafforini, D.M.4    McIntyre, T.M.5    Prescott, S.M.6    La Du, B.N.7    Fogelman, A.M.8    Navab, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.