메뉴 건너뛰기




Volumn 10, Issue 2, 2016, Pages 110-125

Proteomics, biomarkers, and HIV-1: A current perspective

Author keywords

Biomarker; Body fluids; HIV; Macrophage; Systems biology; T cell

Indexed keywords

BIOLOGICAL MARKER; PROTEOME; VIRAL PROTEIN;

EID: 84956789227     PISSN: 18628346     EISSN: 18628354     Source Type: Journal    
DOI: 10.1002/prca.201500002     Document Type: Article
Times cited : (16)

References (99)
  • 1
    • 75149148831 scopus 로고    scopus 로고
    • Biomarkers of HIV-1-associated neurocognitive disorders: challenges of proteomic approaches
    • Ciborowski, P., Biomarkers of HIV-1-associated neurocognitive disorders: challenges of proteomic approaches. Biomark. Med. 2009, 3, 771-785.
    • (2009) Biomark. Med. , vol.3 , pp. 771-785
    • Ciborowski, P.1
  • 2
    • 33747749803 scopus 로고    scopus 로고
    • Blood-brain barrier genomics and proteomics: elucidating phenotype, identifying disease targets and enabling brain drug delivery
    • Calabria, A. R., Shusta, E. V., Blood-brain barrier genomics and proteomics: elucidating phenotype, identifying disease targets and enabling brain drug delivery. Drug Discov. Today 2006, 11, 792-799.
    • (2006) Drug Discov. Today , vol.11 , pp. 792-799
    • Calabria, A.R.1    Shusta, E.V.2
  • 4
    • 33745855899 scopus 로고    scopus 로고
    • Human immunodeficiency virus-mononuclear phagocyte interactions: emerging avenues of biomarker discovery, modes of viral persistence and disease pathogenesis
    • Ciborowski, P., Gendelman, H. E., Human immunodeficiency virus-mononuclear phagocyte interactions: emerging avenues of biomarker discovery, modes of viral persistence and disease pathogenesis. Curr. HIV Res. 2006, 4, 279-291.
    • (2006) Curr. HIV Res. , vol.4 , pp. 279-291
    • Ciborowski, P.1    Gendelman, H.E.2
  • 7
    • 84873420734 scopus 로고    scopus 로고
    • Proteomics as a novel HIV immune monitoring tool
    • Stein, D. R., Burgener, A., Ball, T. B., Proteomics as a novel HIV immune monitoring tool. Curr. Opin. HIV AIDS 2013, 8, 140-146.
    • (2013) Curr. Opin. HIV AIDS , vol.8 , pp. 140-146
    • Stein, D.R.1    Burgener, A.2    Ball, T.B.3
  • 8
    • 84857052591 scopus 로고    scopus 로고
    • Overcoming limitations in the systems vaccinology approach: a pathway for accelerated HIV vaccine development
    • Zak, D. E., Aderem, A., Overcoming limitations in the systems vaccinology approach: a pathway for accelerated HIV vaccine development. Curr. Opin. HIV AIDS 2012, 7, 58-63.
    • (2012) Curr. Opin. HIV AIDS , vol.7 , pp. 58-63
    • Zak, D.E.1    Aderem, A.2
  • 9
    • 84898732425 scopus 로고    scopus 로고
    • Quantitative proteomics by SWATH-MS reveals altered expression of nucleic acid binding and regulatory proteins in HIV-1-infected macrophages
    • Haverland, N. A., Fox, H. S., Ciborowski, P., Quantitative proteomics by SWATH-MS reveals altered expression of nucleic acid binding and regulatory proteins in HIV-1-infected macrophages. J. Proteome Res. 2014, 13, 2109-2119.
    • (2014) J. Proteome Res. , vol.13 , pp. 2109-2119
    • Haverland, N.A.1    Fox, H.S.2    Ciborowski, P.3
  • 10
    • 84901259449 scopus 로고    scopus 로고
    • The use of Nanotrap particles technology in capturing HIV-1 virions and viral proteins from infected cells
    • Jaworski, E., Saifuddin, M., Sampey, G., Shafagati, N. et al., The use of Nanotrap particles technology in capturing HIV-1 virions and viral proteins from infected cells. PloS One 2014, 9, e96778.
    • (2014) PloS One , vol.9 , pp. e96778
    • Jaworski, E.1    Saifuddin, M.2    Sampey, G.3    Shafagati, N.4
  • 11
    • 84921753734 scopus 로고    scopus 로고
    • Integrating proteomics profiling data sets: a network perspective
    • Bhat, A., Dakna, M., Mischak, H., Integrating proteomics profiling data sets: a network perspective. Methods Mol. Biol. 2015, 1243, 237-253.
    • (2015) Methods Mol. Biol. , vol.1243 , pp. 237-253
    • Bhat, A.1    Dakna, M.2    Mischak, H.3
  • 12
    • 84933500585 scopus 로고    scopus 로고
    • Integrating phosphoproteomics in systems biology
    • Liu, Y., Chance, M. R., Integrating phosphoproteomics in systems biology. Comput. Struct. Biotechnol. J. 2014, 10, 90-97.
    • (2014) Comput. Struct. Biotechnol. J. , vol.10 , pp. 90-97
    • Liu, Y.1    Chance, M.R.2
  • 13
    • 84908518716 scopus 로고    scopus 로고
    • Understanding the acetylome: translating targeted proteomics into meaningful physiology
    • Philp, A., Rowland, T., Perez-Schindler, J., Schenk, S., Understanding the acetylome: translating targeted proteomics into meaningful physiology. Am. J. Physiol. Cell Physiol. 2014, 307, C763-C773.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.307 , pp. C763-C773
    • Philp, A.1    Rowland, T.2    Perez-Schindler, J.3    Schenk, S.4
  • 14
    • 84872272080 scopus 로고    scopus 로고
    • Current algorithmic solutions for peptide-based proteomics data generation and identification
    • Hoopmann, M. R., Moritz, R. L., Current algorithmic solutions for peptide-based proteomics data generation and identification. Curr. Opin. Biotechnol. 2013, 24, 31-38.
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 31-38
    • Hoopmann, M.R.1    Moritz, R.L.2
  • 15
    • 84990629710 scopus 로고
    • New desorption strategies for the mass spectrometric analysis of macromolecules
    • Hutchens, T. W. a. Y., T.-T., New desorption strategies for the mass spectrometric analysis of macromolecules. Rapid Commun. Mass Spectrom. 1993, 7, 576-580.
    • (1993) Rapid Commun. Mass Spectrom. , vol.7 , pp. 576-580
    • Hutchens, T.W.A.Y.T.-T.1
  • 16
    • 84908618480 scopus 로고    scopus 로고
    • SELDI-TOF MS-based discovery of a biomarker in Cucumis sativus seeds exposed to CuO nanoparticles
    • Moon, Y. S., Park, E. S., Kim, T. O., Lee, H. S., Lee, S. E., SELDI-TOF MS-based discovery of a biomarker in Cucumis sativus seeds exposed to CuO nanoparticles. Environ. Toxicol. Pharmacol. 2014, 38, 922-931.
    • (2014) Environ. Toxicol. Pharmacol. , vol.38 , pp. 922-931
    • Moon, Y.S.1    Park, E.S.2    Kim, T.O.3    Lee, H.S.4    Lee, S.E.5
  • 17
    • 84912103107 scopus 로고    scopus 로고
    • Evidence for frozen-niche variation in a cosmopolitan parthenogenetic soil mite species (acari
    • von Saltzwedel, H., Maraun, M., Scheu, S., Schaefer, I., Evidence for frozen-niche variation in a cosmopolitan parthenogenetic soil mite species (acari, oribatida). PloS One 2014, 9, e113268.
    • (2014) oribatida). PloS One , vol.9 , pp. e113268
    • von Saltzwedel, H.1    Maraun, M.2    Scheu, S.3    Schaefer, I.4
  • 18
    • 1842559788 scopus 로고    scopus 로고
    • Reproducibility of SELDI-TOF protein patterns in serum: comparing datasets from different experiments
    • Baggerly, K. A., Morris, J. S., Coombes, K. R., Reproducibility of SELDI-TOF protein patterns in serum: comparing datasets from different experiments. Bioinformatics 2004, 20, 777-785.
    • (2004) Bioinformatics , vol.20 , pp. 777-785
    • Baggerly, K.A.1    Morris, J.S.2    Coombes, K.R.3
  • 19
    • 0038376330 scopus 로고    scopus 로고
    • Macrophage proteomic fingerprinting predicts HIV-1-associated cognitive impairment
    • Luo, X., Carlson, K. A., Wojna, V., Mayo, R. et al., Macrophage proteomic fingerprinting predicts HIV-1-associated cognitive impairment. Neurology 2003, 60, 1931-1937.
    • (2003) Neurology , vol.60 , pp. 1931-1937
    • Luo, X.1    Carlson, K.A.2    Wojna, V.3    Mayo, R.4
  • 20
    • 2342576176 scopus 로고    scopus 로고
    • Loss of macrophage-secreted lysozyme in HIV-1-associated dementia detected by SELDI-TOF mass spectrometry
    • Sun, B., Rempel, H. C., Pulliam, L., Loss of macrophage-secreted lysozyme in HIV-1-associated dementia detected by SELDI-TOF mass spectrometry. Aids 2004, 18, 1009-1012.
    • (2004) Aids , vol.18 , pp. 1009-1012
    • Sun, B.1    Rempel, H.C.2    Pulliam, L.3
  • 21
    • 41949111414 scopus 로고    scopus 로고
    • Expression of monocyte markers in HIV-1 infected individuals with or without HIV associated dementia and normal controls in Bangkok Thailand
    • Ratto-Kim, S., Chuenchitra, T., Pulliam, L., Paris, R. et al., Expression of monocyte markers in HIV-1 infected individuals with or without HIV associated dementia and normal controls in Bangkok Thailand. J. Neuroimmunol. 2008, 195, 100-107.
    • (2008) J. Neuroimmunol. , vol.195 , pp. 100-107
    • Ratto-Kim, S.1    Chuenchitra, T.2    Pulliam, L.3    Paris, R.4
  • 22
    • 61849101803 scopus 로고    scopus 로고
    • Proteomic analyses of monocyte-derived macrophages infected with human immunodeficiency virus type 1 primary isolates from Hispanic women with and without cognitive impairment
    • Toro-Nieves, D. M., Rodriguez, Y., Plaud, M., Ciborowski, P. et al., Proteomic analyses of monocyte-derived macrophages infected with human immunodeficiency virus type 1 primary isolates from Hispanic women with and without cognitive impairment. J. Neurovirol. 2009, 15, 36-50.
    • (2009) J. Neurovirol. , vol.15 , pp. 36-50
    • Toro-Nieves, D.M.1    Rodriguez, Y.2    Plaud, M.3    Ciborowski, P.4
  • 23
    • 64749112492 scopus 로고    scopus 로고
    • Biomarkers of HIV-1 associated dementia: proteomic investigation of sera
    • Wiederin, J., Rozek, W., Duan, F., Ciborowski, P., Biomarkers of HIV-1 associated dementia: proteomic investigation of sera. Proteome Sci. 2009, 7, 8.
    • (2009) Proteome Sci. , vol.7 , pp. 8
    • Wiederin, J.1    Rozek, W.2    Duan, F.3    Ciborowski, P.4
  • 24
    • 82355170214 scopus 로고    scopus 로고
    • Profiling cervical lavage fluid by SELDI-TOF mass spectrometry
    • Burgener, A., Profiling cervical lavage fluid by SELDI-TOF mass spectrometry. Methods Mol. Biol. 2012, 818, 143-152.
    • (2012) Methods Mol. Biol. , vol.818 , pp. 143-152
    • Burgener, A.1
  • 25
    • 36749096223 scopus 로고    scopus 로고
    • CSF proteomic fingerprints for HIV-associated cognitive impairment
    • Laspiur, J. P., Anderson, E. R., Ciborowski, P., Wojna, V. et al., CSF proteomic fingerprints for HIV-associated cognitive impairment. J. Neuroimmunol. 2007, 192, 157-170.
    • (2007) J. Neuroimmunol. , vol.192 , pp. 157-170
    • Laspiur, J.P.1    Anderson, E.R.2    Ciborowski, P.3    Wojna, V.4
  • 26
    • 31144467107 scopus 로고    scopus 로고
    • Cerebrospinal fluid proteomics and human immunodeficiency virus dementia: preliminary observations
    • Berger, J. R., Avison, M., Mootoor, Y., Beach, C., Cerebrospinal fluid proteomics and human immunodeficiency virus dementia: preliminary observations. J. Neurovirol. 2005, 11, 557-562.
    • (2005) J. Neurovirol. , vol.11 , pp. 557-562
    • Berger, J.R.1    Avison, M.2    Mootoor, Y.3    Beach, C.4
  • 27
    • 84857128392 scopus 로고    scopus 로고
    • Plasma proteomic profiling in HIV-1 infected methamphetamine abusers
    • Pottiez, G., Jagadish, T., Yu, F., Letendre, S. et al., Plasma proteomic profiling in HIV-1 infected methamphetamine abusers. PloS One 2012, 7, e31031.
    • (2012) PloS One , vol.7 , pp. e31031
    • Pottiez, G.1    Jagadish, T.2    Yu, F.3    Letendre, S.4
  • 28
    • 46749120184 scopus 로고    scopus 로고
    • A method of HIV-1 inactivation compatible with antibody-based depletion of abundant proteins from plasma
    • Bosley, A., Marshall, H. N., Badralmaa, Y., Natarajan, V., A method of HIV-1 inactivation compatible with antibody-based depletion of abundant proteins from plasma. Proteomics Clin. Appl. 2008, 2, 904-907.
    • (2008) Proteomics Clin. Appl. , vol.2 , pp. 904-907
    • Bosley, A.1    Marshall, H.N.2    Badralmaa, Y.3    Natarajan, V.4
  • 29
    • 36349014934 scopus 로고    scopus 로고
    • Cerebrospinal fluid proteomic profiling of HIV-1-infected patients with cognitive impairment
    • Rozek, W., Ricardo-Dukelow, M., Holloway, S., Gendelman, H. E. et al., Cerebrospinal fluid proteomic profiling of HIV-1-infected patients with cognitive impairment. J. Proteome Res. 2007, 6, 4189-4199.
    • (2007) J. Proteome Res. , vol.6 , pp. 4189-4199
    • Rozek, W.1    Ricardo-Dukelow, M.2    Holloway, S.3    Gendelman, H.E.4
  • 30
    • 64749112915 scopus 로고    scopus 로고
    • Sera proteomic biomarker profiling in HIV-1 infected subjects with cognitive impairment
    • Rozek, W., Horning, J., Anderson, J., Ciborowski, P., Sera proteomic biomarker profiling in HIV-1 infected subjects with cognitive impairment. Proteomics Clin. Appl. 2008, 2, 1498-1507.
    • (2008) Proteomics Clin. Appl. , vol.2 , pp. 1498-1507
    • Rozek, W.1    Horning, J.2    Anderson, J.3    Ciborowski, P.4
  • 31
    • 33846594732 scopus 로고    scopus 로고
    • Different isoforms of apolipoprotein AI present heterologous post-translational expression in HIV infected patients
    • Kim, S. S., Kim, M. H., Shin, B. K., Na, H. J. et al., Different isoforms of apolipoprotein AI present heterologous post-translational expression in HIV infected patients. J. Proteome Res. 2007, 6, 180-184.
    • (2007) J. Proteome Res. , vol.6 , pp. 180-184
    • Kim, S.S.1    Kim, M.H.2    Shin, B.K.3    Na, H.J.4
  • 32
    • 77958190741 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin variants in plasma from HIV-infected patients revealed by proteomic and glycoproteomic analysis
    • Zhang, L., Jia, X., Zhang, X., Cao, J. et al., Alpha-1 antitrypsin variants in plasma from HIV-infected patients revealed by proteomic and glycoproteomic analysis. Electrophoresis 2010, 31, 3437-3445.
    • (2010) Electrophoresis , vol.31 , pp. 3437-3445
    • Zhang, L.1    Jia, X.2    Zhang, X.3    Cao, J.4
  • 33
    • 34247553696 scopus 로고    scopus 로고
    • Investigating the human immunodeficiency virus type 1-infected monocyte-derived macrophage secretome
    • Ciborowski, P., Kadiu, I., Rozek, W., Smith, L. et al., Investigating the human immunodeficiency virus type 1-infected monocyte-derived macrophage secretome. Virology 2007, 363, 198-209.
    • (2007) Virology , vol.363 , pp. 198-209
    • Ciborowski, P.1    Kadiu, I.2    Rozek, W.3    Smith, L.4
  • 34
    • 84875522520 scopus 로고    scopus 로고
    • Comparative proteomic analysis of HIV-1 particles reveals a role for Ezrin and EHD4 in the Nef-dependent increase of virus infectivity
    • Bregnard, C., Zamborlini, A., Leduc, M., Chafey, P. et al., Comparative proteomic analysis of HIV-1 particles reveals a role for Ezrin and EHD4 in the Nef-dependent increase of virus infectivity. J. Virol. 2013, 87, 3729-3740.
    • (2013) J. Virol. , vol.87 , pp. 3729-3740
    • Bregnard, C.1    Zamborlini, A.2    Leduc, M.3    Chafey, P.4
  • 35
    • 81155137314 scopus 로고    scopus 로고
    • Proteomic signatures of human oral epithelial cells in HIV-infected subjects
    • Yohannes, E., Ghosh, S. K., Jiang, B., McCormick, T. S. et al., Proteomic signatures of human oral epithelial cells in HIV-infected subjects. PloS One 2011, 6, e27816.
    • (2011) PloS One , vol.6 , pp. e27816
    • Yohannes, E.1    Ghosh, S.K.2    Jiang, B.3    McCormick, T.S.4
  • 36
    • 78650462323 scopus 로고    scopus 로고
    • Proteomic analyses of monocytes obtained from Hispanic women with HIV-associated dementia show depressed antioxidants
    • Kraft-Terry, S., Gerena, Y., Wojna, V., Plaud-Valentin, M. et al., Proteomic analyses of monocytes obtained from Hispanic women with HIV-associated dementia show depressed antioxidants. Proteomics Clin. Appl. 2010, 4, 706-714.
    • (2010) Proteomics Clin. Appl. , vol.4 , pp. 706-714
    • Kraft-Terry, S.1    Gerena, Y.2    Wojna, V.3    Plaud-Valentin, M.4
  • 37
    • 77955676756 scopus 로고    scopus 로고
    • First evidence of overlaps between HIV-Associated Dementia (HAD) and non-viral neurodegenerative diseases: proteomic analysis of the frontal cortex from HIV+ patients with and without dementia
    • Zhou, L., Diefenbach, E., Crossett, B., Tran, S. L. et al., First evidence of overlaps between HIV-Associated Dementia (HAD) and non-viral neurodegenerative diseases: proteomic analysis of the frontal cortex from HIV+ patients with and without dementia. Mol. Neurodegener. 2010, 5, 27.
    • (2010) Mol. Neurodegener. , vol.5 , pp. 27
    • Zhou, L.1    Diefenbach, E.2    Crossett, B.3    Tran, S.L.4
  • 38
    • 67349121668 scopus 로고    scopus 로고
    • HIV-1 transforms the monocyte plasma membrane proteome
    • Kadiu, I., Wang, T., Schlautman, J. D., Dubrovsky, L. et al., HIV-1 transforms the monocyte plasma membrane proteome. Cell. Immunol. 2009, 258, 44-58.
    • (2009) Cell. Immunol. , vol.258 , pp. 44-58
    • Kadiu, I.1    Wang, T.2    Schlautman, J.D.3    Dubrovsky, L.4
  • 39
    • 33947694348 scopus 로고    scopus 로고
    • Proteomic analyses of methamphetamine (METH)-induced differential protein expression by immature dendritic cells (IDC)
    • Reynolds, J. L., Mahajan, S. D., Sykes, D. E., Schwartz, S. A., Nair, M. P., Proteomic analyses of methamphetamine (METH)-induced differential protein expression by immature dendritic cells (IDC). Biochim. Biophys. Acta 2007, 1774, 433-442.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 433-442
    • Reynolds, J.L.1    Mahajan, S.D.2    Sykes, D.E.3    Schwartz, S.A.4    Nair, M.P.5
  • 40
    • 65249146719 scopus 로고    scopus 로고
    • Heroin-induces differential protein expression by normal human astrocytes (NHA)
    • Reynolds, J. L., Mahajan, S. D., Sykes, D., Nair, M. P., Heroin-induces differential protein expression by normal human astrocytes (NHA). Am. J. Infectious Dis. 2006, 2, 49-57.
    • (2006) Am. J. Infectious Dis. , vol.2 , pp. 49-57
    • Reynolds, J.L.1    Mahajan, S.D.2    Sykes, D.3    Nair, M.P.4
  • 41
    • 33751169355 scopus 로고    scopus 로고
    • Proteomic analysis of the effects of cocaine on the enhancement of HIV-1 replication in normal human astrocytes (NHA)
    • Reynolds, J. L., Mahajan, S. D., Bindukumar, B., Sykes, D. et al., Proteomic analysis of the effects of cocaine on the enhancement of HIV-1 replication in normal human astrocytes (NHA). Brain Res. 2006, 1123, 226-236.
    • (2006) Brain Res. , vol.1123 , pp. 226-236
    • Reynolds, J.L.1    Mahajan, S.D.2    Bindukumar, B.3    Sykes, D.4
  • 42
    • 33947433457 scopus 로고    scopus 로고
    • Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression
    • Coiras, M., Camafeita, E., Urena, T., Lopez, J. A. et al., Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression. Proteomics 2006, 6 (Suppl 1), S63-S73.
    • (2006) Proteomics , vol.6 , pp. S63-S73
    • Coiras, M.1    Camafeita, E.2    Urena, T.3    Lopez, J.A.4
  • 43
    • 73649117166 scopus 로고    scopus 로고
    • Quantitative plasma proteomic profiling identifies the vitamin E binding protein afamin as a potential pathogenic factor in SIV induced CNS disease
    • Pendyala, G., Trauger, S. A., Siuzdak, G., Fox, H. S., Quantitative plasma proteomic profiling identifies the vitamin E binding protein afamin as a potential pathogenic factor in SIV induced CNS disease. J. Proteome Res. 2010, 9, 352-358.
    • (2010) J. Proteome Res. , vol.9 , pp. 352-358
    • Pendyala, G.1    Trauger, S.A.2    Siuzdak, G.3    Fox, H.S.4
  • 44
    • 84899840430 scopus 로고    scopus 로고
    • Increased Serpin A5 levels in the cervicovaginal fluid of HIV-1 exposed seronegatives suggest that a subtle balance between serine proteases and their inhibitors may determine susceptibility to HIV-1 infection
    • Van Raemdonck, G., Zegels, G., Coen, E., Vuylsteke, B. et al., Increased Serpin A5 levels in the cervicovaginal fluid of HIV-1 exposed seronegatives suggest that a subtle balance between serine proteases and their inhibitors may determine susceptibility to HIV-1 infection. Virology 2014, 458-459, 11-21.
    • (2014) Virology , vol.458-459 , pp. 11-21
    • Van Raemdonck, G.1    Zegels, G.2    Coen, E.3    Vuylsteke, B.4
  • 45
    • 78649865457 scopus 로고    scopus 로고
    • Functional proteomic analysis for regulatory T cell surveillance of the HIV-1-infected macrophage
    • Huang, X., Stone, D. K., Yu, F., Zeng, Y., Gendelman, H. E., Functional proteomic analysis for regulatory T cell surveillance of the HIV-1-infected macrophage. J. Proteome Res. 2010, 9, 6759-6773.
    • (2010) J. Proteome Res. , vol.9 , pp. 6759-6773
    • Huang, X.1    Stone, D.K.2    Yu, F.3    Zeng, Y.4    Gendelman, H.E.5
  • 46
    • 84861183219 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of HIV-1 infected CD4+ T cells reveals an early host response in important biological pathways: protein synthesis, cell proliferation, and T-cell activation
    • Navare, A. T., Sova, P., Purdy, D. E., Weiss, J. M. et al., Quantitative proteomic analysis of HIV-1 infected CD4+ T cells reveals an early host response in important biological pathways: protein synthesis, cell proliferation, and T-cell activation. Virology 2012, 429, 37-46.
    • (2012) Virology , vol.429 , pp. 37-46
    • Navare, A.T.1    Sova, P.2    Purdy, D.E.3    Weiss, J.M.4
  • 47
    • 80053995029 scopus 로고    scopus 로고
    • Investigation of plasma biomarkers in HIV-1/HCV mono- and coinfected individuals by multiplex iTRAQ quantitative proteomics
    • Shetty, V., Jain, P., Nickens, Z., Sinnathamby, G. et al., Investigation of plasma biomarkers in HIV-1/HCV mono- and coinfected individuals by multiplex iTRAQ quantitative proteomics. Omics 2011, 15, 705-717.
    • (2011) Omics , vol.15 , pp. 705-717
    • Shetty, V.1    Jain, P.2    Nickens, Z.3    Sinnathamby, G.4
  • 48
    • 84869216692 scopus 로고    scopus 로고
    • Nucleolar protein trafficking in response to HIV-1 Tat: rewiring the nucleolus
    • Jarboui, M. A., Bidoia, C., Woods, E., Roe, B. et al., Nucleolar protein trafficking in response to HIV-1 Tat: rewiring the nucleolus. PloS One 2012, 7, e48702.
    • (2012) PloS One , vol.7 , pp. e48702
    • Jarboui, M.A.1    Bidoia, C.2    Woods, E.3    Roe, B.4
  • 49
    • 84880081958 scopus 로고    scopus 로고
    • HIV-1 Vpr modulates macrophage metabolic pathways: a SILAC-based quantitative analysis
    • Barrero, C. A., Datta, P. K., Sen, S., Deshmane, S. et al., HIV-1 Vpr modulates macrophage metabolic pathways: a SILAC-based quantitative analysis. PloS One 2013, 8, e68376.
    • (2013) PloS One , vol.8 , pp. e68376
    • Barrero, C.A.1    Datta, P.K.2    Sen, S.3    Deshmane, S.4
  • 50
    • 79958222242 scopus 로고    scopus 로고
    • Pulsed stable isotope labeling of amino acids in cell culture uncovers the dynamic interactions between HIV-1 and the monocyte-derived macrophage
    • Kraft-Terry, S. D., Engebretsen, I. L., Bastola, D. K., Fox, H. S. et al., Pulsed stable isotope labeling of amino acids in cell culture uncovers the dynamic interactions between HIV-1 and the monocyte-derived macrophage. J. Proteome Res. 2011, 10, 2852-2862.
    • (2011) J. Proteome Res. , vol.10 , pp. 2852-2862
    • Kraft-Terry, S.D.1    Engebretsen, I.L.2    Bastola, D.K.3    Fox, H.S.4
  • 51
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W., Zhou, H., Lin, H., Roy, S. et al., Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal. Chem. 2003, 75, 4818-4826.
    • (2003) Anal. Chem. , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4
  • 53
    • 33644768131 scopus 로고    scopus 로고
    • Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages
    • Ryzhova, E. V., Vos, R. M., Albright, A. V., Harrist, A. V. et al., Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages. J. Virol. 2006, 80, 2694-2704.
    • (2006) J. Virol. , vol.80 , pp. 2694-2704
    • Ryzhova, E.V.1    Vos, R.M.2    Albright, A.V.3    Harrist, A.V.4
  • 54
    • 79955669430 scopus 로고    scopus 로고
    • Annexin A6-linking Ca(2+) signaling with cholesterol transport
    • Enrich, C., Rentero, C., deMuga, S. V., Reverter, M. et al., Annexin A6-linking Ca(2+) signaling with cholesterol transport. Biochim. Biophys. Acta 2011, 1813, 935-947.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 935-947
    • Enrich, C.1    Rentero, C.2    de Muga, S.V.3    Reverter, M.4
  • 55
    • 84855998457 scopus 로고    scopus 로고
    • Global landscape of HIV-human protein complexes
    • Jager, S., Cimermancic, P., Gulbahce, N., Johnson, J. R. et al., Global landscape of HIV-human protein complexes. Nature 2012, 481, 365-370.
    • (2012) Nature , vol.481 , pp. 365-370
    • Jager, S.1    Cimermancic, P.2    Gulbahce, N.3    Johnson, J.R.4
  • 56
    • 41349097097 scopus 로고    scopus 로고
    • STAT1 signaling modulates HIV-1-induced inflammatory responses and leukocyte transmigration across the blood-brain barrier
    • Chaudhuri, A., Yang, B., Gendelman, H. E., Persidsky, Y., Kanmogne, G. D., STAT1 signaling modulates HIV-1-induced inflammatory responses and leukocyte transmigration across the blood-brain barrier. Blood 2008, 111, 2062-2072.
    • (2008) Blood , vol.111 , pp. 2062-2072
    • Chaudhuri, A.1    Yang, B.2    Gendelman, H.E.3    Persidsky, Y.4    Kanmogne, G.D.5
  • 57
    • 0029894760 scopus 로고    scopus 로고
    • Virologic markers of human immunodeficiency virus type 1 in cerebrospinal fluid of infected children
    • Pratt, R. D., Nichols, S., McKinney, N., Kwok, S. et al., Virologic markers of human immunodeficiency virus type 1 in cerebrospinal fluid of infected children. J. Infectious Dis. 1996, 174, 288-293.
    • (1996) J. Infectious Dis. , vol.174 , pp. 288-293
    • Pratt, R.D.1    Nichols, S.2    McKinney, N.3    Kwok, S.4
  • 58
    • 0034025075 scopus 로고    scopus 로고
    • Detection of the human immunodeficiency virus regulatory protein tat in CNS tissues
    • Hudson, L., Liu, J., Nath, A., Jones, M. et al., Detection of the human immunodeficiency virus regulatory protein tat in CNS tissues. J. Neurovirol. 2000, 6, 145-155.
    • (2000) J. Neurovirol. , vol.6 , pp. 145-155
    • Hudson, L.1    Liu, J.2    Nath, A.3    Jones, M.4
  • 59
    • 0034633618 scopus 로고    scopus 로고
    • Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1
    • Xiao, H., Neuveut, C., Tiffany, H. L., Benkirane, M. et al., Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1. Proc. Natl. Acad. Sci. USA 2000, 97, 11466-11471.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11466-11471
    • Xiao, H.1    Neuveut, C.2    Tiffany, H.L.3    Benkirane, M.4
  • 60
    • 33845764425 scopus 로고    scopus 로고
    • HIV-1 gp120 compromises blood-brain barrier integrity and enhances monocyte migration across blood-brain barrier: implication for viral neuropathogenesis
    • Kanmogne, G. D., Schall, K., Leibhart, J., Knipe, B. et al., HIV-1 gp120 compromises blood-brain barrier integrity and enhances monocyte migration across blood-brain barrier: implication for viral neuropathogenesis. J. Cerebral Blood Flow Metab. 2007, 27, 123-134.
    • (2007) J. Cerebral Blood Flow Metab. , vol.27 , pp. 123-134
    • Kanmogne, G.D.1    Schall, K.2    Leibhart, J.3    Knipe, B.4
  • 61
    • 0035914008 scopus 로고    scopus 로고
    • Evidence that the HIV-1 coat protein gp120 causes neuronal apoptosis in the neocortex of rat via a mechanism involving CXCR4 chemokine receptor
    • Corasaniti, M. T., Piccirilli, S., Paoletti, A., Nistico, R. et al., Evidence that the HIV-1 coat protein gp120 causes neuronal apoptosis in the neocortex of rat via a mechanism involving CXCR4 chemokine receptor. Neurosci. Lett. 2001, 312, 67-70.
    • (2001) Neurosci. Lett. , vol.312 , pp. 67-70
    • Corasaniti, M.T.1    Piccirilli, S.2    Paoletti, A.3    Nistico, R.4
  • 62
    • 0033461203 scopus 로고    scopus 로고
    • Genetic markers on HIV-1 gp120 C2-V3 region associated with the expression or absence of cognitive motor complex in HIV/AIDS
    • Jurado, A., Rahimi-Moghaddam, P., Bar-Jurado, S., Richardson, J. S. et al., Genetic markers on HIV-1 gp120 C2-V3 region associated with the expression or absence of cognitive motor complex in HIV/AIDS. J. Neuro AIDS 1999, 2, 15-28.
    • (1999) J. Neuro AIDS , vol.2 , pp. 15-28
    • Jurado, A.1    Rahimi-Moghaddam, P.2    Bar-Jurado, S.3    Richardson, J.S.4
  • 63
    • 0026032735 scopus 로고
    • Enzyme-linked immunoassay for human immunodeficiency virus type 1 envelope glycoprotein 120
    • Gilbert, M., Kirihara, J., Mills, J., Enzyme-linked immunoassay for human immunodeficiency virus type 1 envelope glycoprotein 120. J. Clin. Microbiol. 1991, 29, 142-147.
    • (1991) J. Clin. Microbiol. , vol.29 , pp. 142-147
    • Gilbert, M.1    Kirihara, J.2    Mills, J.3
  • 64
    • 0026588930 scopus 로고
    • Identification of HIV-1 envelope glycoprotein in the serum of AIDS and ARC patients
    • Oh, S. K., Cruikshank, W. W., Raina, J., Blanchard, G. C. et al., Identification of HIV-1 envelope glycoprotein in the serum of AIDS and ARC patients. J. Acquir. Immune Defic. Syndr. 1992, 5, 251-256.
    • (1992) J. Acquir. Immune Defic. Syndr. , vol.5 , pp. 251-256
    • Oh, S.K.1    Cruikshank, W.W.2    Raina, J.3    Blanchard, G.C.4
  • 65
    • 2542502473 scopus 로고    scopus 로고
    • Is there enough gp120 in the body fluids of HIV-1-infected individuals to have biologically significant effects?
    • Klasse, P. J., Moore, J. P., Is there enough gp120 in the body fluids of HIV-1-infected individuals to have biologically significant effects? Virology 2004, 323, 1-8.
    • (2004) Virology , vol.323 , pp. 1-8
    • Klasse, P.J.1    Moore, J.P.2
  • 67
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go, E. P., Irungu, J., Zhang, Y., Dalpathado, D. S. et al., Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J. Proteome Res. 2008, 7, 1660-1674.
    • (2008) J. Proteome Res. , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4
  • 68
    • 48349109797 scopus 로고    scopus 로고
    • Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein
    • Irungu, J., Go, E. P., Zhang, Y., Dalpathado, D. S. et al., Comparison of HPLC/ESI-FTICR MS versus MALDI-TOF/TOF MS for glycopeptide analysis of a highly glycosylated HIV envelope glycoprotein. J. Am. Soc. Mass Spectrom. 2008, 19, 1209-1220.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1209-1220
    • Irungu, J.1    Go, E.P.2    Zhang, Y.3    Dalpathado, D.S.4
  • 69
    • 61849171106 scopus 로고    scopus 로고
    • Selection of HIV variants with signature genotypic characteristics during heterosexual transmission
    • Sagar, M., Laeyendecker, O., Lee, S., Gamiel, J. et al., Selection of HIV variants with signature genotypic characteristics during heterosexual transmission. J. Infectious Dis. 2009, 199, 580-589.
    • (2009) J. Infectious Dis. , vol.199 , pp. 580-589
    • Sagar, M.1    Laeyendecker, O.2    Lee, S.3    Gamiel, J.4
  • 70
    • 79961184231 scopus 로고    scopus 로고
    • Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry
    • Go, E. P., Hewawasam, G., Liao, H. X., Chen, H. et al., Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J. Virol. 2011, 85, 8270-8284.
    • (2011) J. Virol. , vol.85 , pp. 8270-8284
    • Go, E.P.1    Hewawasam, G.2    Liao, H.X.3    Chen, H.4
  • 71
    • 84883478286 scopus 로고    scopus 로고
    • Characterizing O-linked glycopeptides by electron transfer dissociation: fragmentation rules and applications in data analysis
    • Zhu, Z., Su, X., Clark, D. F., Go, E. P., Desaire, H., Characterizing O-linked glycopeptides by electron transfer dissociation: fragmentation rules and applications in data analysis. Anal. Chem. 2013, 85, 8403-8411.
    • (2013) Anal. Chem. , vol.85 , pp. 8403-8411
    • Zhu, Z.1    Su, X.2    Clark, D.F.3    Go, E.P.4    Desaire, H.5
  • 72
    • 70349923632 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of clade C HIV-1 envelope proteins
    • Go, E. P., Chang, Q., Liao, H. X., Sutherland, L. L. et al., Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. J. Proteome Res. 2009, 8, 4231-4242.
    • (2009) J. Proteome Res. , vol.8 , pp. 4231-4242
    • Go, E.P.1    Chang, Q.2    Liao, H.X.3    Sutherland, L.L.4
  • 73
    • 79955403717 scopus 로고    scopus 로고
    • Analysis of the disulfide bond arrangement of the HIV-1 envelope protein CON-S gp140 DeltaCFI shows variability in the V1 and V2 regions
    • Go, E. P., Zhang, Y., Menon, S., Desaire, H., Analysis of the disulfide bond arrangement of the HIV-1 envelope protein CON-S gp140 DeltaCFI shows variability in the V1 and V2 regions. J. Proteome Res. 2011, 10, 578-591.
    • (2011) J. Proteome Res. , vol.10 , pp. 578-591
    • Go, E.P.1    Zhang, Y.2    Menon, S.3    Desaire, H.4
  • 74
    • 80053459912 scopus 로고    scopus 로고
    • Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies
    • Ma, B. J., Alam, S. M., Go, E. P., Lu, X. et al., Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies. PLoS Pathogens 2011, 7, e1002200.
    • (2011) PLoS Pathogens , vol.7 , pp. e1002200
    • Ma, B.J.1    Alam, S.M.2    Go, E.P.3    Lu, X.4
  • 75
    • 84874622598 scopus 로고    scopus 로고
    • Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins
    • Go, E. P., Liao, H. X., Alam, S. M., Hua, D. et al., Characterization of host-cell line specific glycosylation profiles of early transmitted/founder HIV-1 gp120 envelope proteins. J. Proteome Res. 2013, 12, 1223-1234.
    • (2013) J. Proteome Res. , vol.12 , pp. 1223-1234
    • Go, E.P.1    Liao, H.X.2    Alam, S.M.3    Hua, D.4
  • 76
    • 84873395169 scopus 로고    scopus 로고
    • Isotype-switched immunoglobulin G antibodies to HIV Gag proteins may provide alternative or additional immune responses to 'protective' human leukocyte antigen-B alleles in HIV controllers
    • French, M. A., Center, R. J., Wilson, K. M., Fleyfel, I. et al., Isotype-switched immunoglobulin G antibodies to HIV Gag proteins may provide alternative or additional immune responses to 'protective' human leukocyte antigen-B alleles in HIV controllers. Aids 2013, 27, 519-528.
    • (2013) Aids , vol.27 , pp. 519-528
    • French, M.A.1    Center, R.J.2    Wilson, K.M.3    Fleyfel, I.4
  • 77
    • 81155159842 scopus 로고    scopus 로고
    • Multiple HIV-1-specific IgG3 responses decline during acute HIV-1: implications for detection of incident HIV infection
    • Yates, N. L., Lucas, J. T., Nolen, T. L., Vandergrift, N. A. et al., Multiple HIV-1-specific IgG3 responses decline during acute HIV-1: implications for detection of incident HIV infection. Aids 2011, 25, 2089-2097.
    • (2011) Aids , vol.25 , pp. 2089-2097
    • Yates, N.L.1    Lucas, J.T.2    Nolen, T.L.3    Vandergrift, N.A.4
  • 78
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus
    • Chertova, E., Bess, J. W., Jr., Crise, B. J., Sowder, I. R. et al., Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus. J. Virol. 2002, 76, 5315-5325.
    • (2002) J. Virol. , vol.76 , pp. 5315-5325
    • Chertova, E.1    Bess, J.W.2    Crise, B.J.3    Sowder, I.R.4
  • 79
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews, A., Kramer, B., Marsh, M., Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 2003, 162, 443-455.
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 80
    • 84877104776 scopus 로고    scopus 로고
    • The conserved set of host proteins incorporated into HIV-1 virions suggests a common egress pathway in multiple cell types
    • Linde, M. E., Colquhoun, D. R., Ubaida Mohien, C., Kole, T. et al., The conserved set of host proteins incorporated into HIV-1 virions suggests a common egress pathway in multiple cell types. J. Proteome Res. 2013, 12, 2045-2054.
    • (2013) J. Proteome Res. , vol.12 , pp. 2045-2054
    • Linde, M.E.1    Colquhoun, D.R.2    Ubaida Mohien, C.3    Kole, T.4
  • 81
    • 0036776606 scopus 로고    scopus 로고
    • Three isoforms of cyclophilin A associated with human immunodeficiency virus type 1 were found by proteomics by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight mass spectrometry
    • Misumi, S., Fuchigami, T., Takamune, N., Takahashi, I. et al., Three isoforms of cyclophilin A associated with human immunodeficiency virus type 1 were found by proteomics by using two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time of flight mass spectrometry. J. Virol. 2002, 76, 10000-10008.
    • (2002) J. Virol. , vol.76 , pp. 10000-10008
    • Misumi, S.1    Fuchigami, T.2    Takamune, N.3    Takahashi, I.4
  • 82
    • 70349947190 scopus 로고    scopus 로고
    • The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors
    • Mascarenhas, A. P., Musier-Forsyth, K., The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors. FEBS J. 2009, 276, 6118-6127.
    • (2009) FEBS J. , vol.276 , pp. 6118-6127
    • Mascarenhas, A.P.1    Musier-Forsyth, K.2
  • 83
    • 33644834758 scopus 로고    scopus 로고
    • Proteomic analysis of human immunodeficiency virus using liquid chromatography/tandem mass spectrometry effectively distinguishes specific incorporated host proteins
    • Saphire, A. C., Gallay, P. A., Bark, S. J., Proteomic analysis of human immunodeficiency virus using liquid chromatography/tandem mass spectrometry effectively distinguishes specific incorporated host proteins. J. Proteome Res. 2006, 5, 530-538.
    • (2006) J. Proteome Res. , vol.5 , pp. 530-538
    • Saphire, A.C.1    Gallay, P.A.2    Bark, S.J.3
  • 84
    • 84903779338 scopus 로고    scopus 로고
    • Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma
    • Yang, W., Zhou, J. Y., Chen, L., Ao, M. et al., Glycoproteomic analysis identifies human glycoproteins secreted from HIV latently infected T cells and reveals their presence in HIV+ plasma. Clin. Proteomics 2014, 11, 9.
    • (2014) Clin. Proteomics , vol.11 , pp. 9
    • Yang, W.1    Zhou, J.Y.2    Chen, L.3    Ao, M.4
  • 85
    • 84891537689 scopus 로고    scopus 로고
    • Proteomic landscape of bronchoalveolar lavage fluid in human immunodeficiency virus infection
    • Nguyen, E. V., Gharib, S. A., Crothers, K., Chow, Y. H. et al., Proteomic landscape of bronchoalveolar lavage fluid in human immunodeficiency virus infection. Am. J. Physiol. Lung Cell. Mol. Physiol. 2014, 306, L35-L42.
    • (2014) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.306 , pp. L35-L42
    • Nguyen, E.V.1    Gharib, S.A.2    Crothers, K.3    Chow, Y.H.4
  • 86
    • 84893394396 scopus 로고    scopus 로고
    • Saliva : a fluid of study for OMICS
    • Cuevas-Cordoba, B., Santiago-Garcia, J., Saliva : a fluid of study for OMICS. Omics 2014, 18, 87-97.
    • (2014) Omics , vol.18 , pp. 87-97
    • Cuevas-Cordoba, B.1    Santiago-Garcia, J.2
  • 87
    • 84910144160 scopus 로고    scopus 로고
    • Identification of putative biomarkers for HIV-associated neurocognitive impairment in the CSF of HIV-infected patients under cART therapy determined by mass spectrometry
    • Bora, A., Ubaida Mohien, C., Chaerkady, R., Chang, L. et al., Identification of putative biomarkers for HIV-associated neurocognitive impairment in the CSF of HIV-infected patients under cART therapy determined by mass spectrometry. J. Neurovirol. 2014, 20, 457-465.
    • (2014) J. Neurovirol. , vol.20 , pp. 457-465
    • Bora, A.1    Ubaida Mohien, C.2    Chaerkady, R.3    Chang, L.4
  • 88
    • 70349617072 scopus 로고    scopus 로고
    • Comparative analysis to guide quality improvements in proteomics
    • Mann, M., Comparative analysis to guide quality improvements in proteomics. Nat. Methods 2009, 6, 717-719.
    • (2009) Nat. Methods , vol.6 , pp. 717-719
    • Mann, M.1
  • 89
    • 67650351489 scopus 로고    scopus 로고
    • A comparison of labeling and label-free mass spectrometry-based proteomics approaches
    • Patel, V. J., Thalassinos, K., Slade, S. E., Connolly, J. B. et al., A comparison of labeling and label-free mass spectrometry-based proteomics approaches. J. Proteome Res. 2009, 8, 3752-3759.
    • (2009) J. Proteome Res. , vol.8 , pp. 3752-3759
    • Patel, V.J.1    Thalassinos, K.2    Slade, S.E.3    Connolly, J.B.4
  • 90
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present
    • Bantscheff, M., Lemeer, S., Savitski, M. M., Kuster, B., Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal. Bioanal. Chem. 2012, 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
  • 91
    • 84875819017 scopus 로고    scopus 로고
    • Quantitative analysis of differentially expressed saliva proteins in human immunodeficiency virus type 1 (HIV-1) infected individuals
    • Zhang, N., Zhang, Z., Feng, S., Wang, Q. et al., Quantitative analysis of differentially expressed saliva proteins in human immunodeficiency virus type 1 (HIV-1) infected individuals. Anal. Chim. Acta 2013, 774, 61-66.
    • (2013) Anal. Chim. Acta , vol.774 , pp. 61-66
    • Zhang, N.1    Zhang, Z.2    Feng, S.3    Wang, Q.4
  • 92
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis
    • Gillet, L. C., Navarro, P., Tate, S., Rost, H. et al., Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis. Mol. Cell. Proteomics 2012, 11, O111 016717.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Rost, H.4
  • 93
    • 84905400274 scopus 로고    scopus 로고
    • Proteomic analysis of the mitochondria from embryonic and postnatal rat brains reveals response to developmental changes in energy demands
    • Villeneuve, L. M., Stauch, K. L., Fox, H. S., Proteomic analysis of the mitochondria from embryonic and postnatal rat brains reveals response to developmental changes in energy demands. J. Proteomics 2014, 109C, 228-239.
    • (2014) J. Proteomics , vol.109C , pp. 228-239
    • Villeneuve, L.M.1    Stauch, K.L.2    Fox, H.S.3
  • 94
    • 77956304903 scopus 로고    scopus 로고
    • Plasma proteomic analysis of simian immunodeficiency virus infection of rhesus macaques
    • Wiederin, J. L., Donahoe, R. M., Anderson, J. R., Yu, F. et al., Plasma proteomic analysis of simian immunodeficiency virus infection of rhesus macaques. J. Proteome Res. 2010, 9, 4721-4731.
    • (2010) J. Proteome Res. , vol.9 , pp. 4721-4731
    • Wiederin, J.L.1    Donahoe, R.M.2    Anderson, J.R.3    Yu, F.4
  • 95
    • 84155164730 scopus 로고    scopus 로고
    • Changes in the plasma proteome follows chronic opiate administration in simian immunodeficiency virus infected rhesus macaques
    • Wiederin, J. L., Yu, F., Donahoe, R. M., Fox, H. S. et al., Changes in the plasma proteome follows chronic opiate administration in simian immunodeficiency virus infected rhesus macaques. Drug Alcohol Depend. 2012, 120, 105-112.
    • (2012) Drug Alcohol Depend. , vol.120 , pp. 105-112
    • Wiederin, J.L.1    Yu, F.2    Donahoe, R.M.3    Fox, H.S.4
  • 96
    • 84865677957 scopus 로고    scopus 로고
    • The cerebrospinal fluid proteome in HIV infection: change associated with disease severity
    • Angel, T. E., Jacobs, J. M., Spudich, S. S., Gritsenko, M. A. et al., The cerebrospinal fluid proteome in HIV infection: change associated with disease severity. Clin. Proteomics 2012, 9, 3.
    • (2012) Clin. Proteomics , vol.9 , pp. 3
    • Angel, T.E.1    Jacobs, J.M.2    Spudich, S.S.3    Gritsenko, M.A.4
  • 97
    • 84905010861 scopus 로고    scopus 로고
    • Identification of fatigue biomarkers in treated and treatment-naive HIV patients: preliminary results
    • Jensen, K., Goo, Y. A., Yahiaoui, A., Bajwa, S. et al., Identification of fatigue biomarkers in treated and treatment-naive HIV patients: preliminary results. Biol. Res. Nurs. 2013, 16, 278-287.
    • (2013) Biol. Res. Nurs. , vol.16 , pp. 278-287
    • Jensen, K.1    Goo, Y.A.2    Yahiaoui, A.3    Bajwa, S.4
  • 98
    • 84862269346 scopus 로고    scopus 로고
    • Isobaric tagging-based quantification by mass spectrometry of differentially regulated proteins in synaptosomes of HIV/gp120 transgenic mice: implications for HIV-associated neurodegeneration
    • Banerjee, S., Liao, L., Russo, R., Nakamura, T. et al., Isobaric tagging-based quantification by mass spectrometry of differentially regulated proteins in synaptosomes of HIV/gp120 transgenic mice: implications for HIV-associated neurodegeneration. Exp. Neurol. 2012, 236, 298-306.
    • (2012) Exp. Neurol. , vol.236 , pp. 298-306
    • Banerjee, S.1    Liao, L.2    Russo, R.3    Nakamura, T.4
  • 99
    • 55949121329 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins in the cervical mucosa of HIV-1-resistant sex workers
    • Burgener, A., Boutilier, J., Wachihi, C., Kimani, J. et al., Identification of differentially expressed proteins in the cervical mucosa of HIV-1-resistant sex workers. J. Proteome Res. 2008, 7, 4446-4454.
    • (2008) J. Proteome Res. , vol.7 , pp. 4446-4454
    • Burgener, A.1    Boutilier, J.2    Wachihi, C.3    Kimani, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.