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Volumn 2, Issue 5, 2008, Pages 638-653

Proteomics-based investigations of animal models of disease

Author keywords

Animal models; Biomarkers; Post translational modifications; Protein interactions; Standard proteomes

Indexed keywords

ACETAZOLAMIDE; AMINOPEPTIDASE; BIOLOGICAL MARKER; CALMODULIN; CALPAIN 3; CARBONATE DEHYDRATASE I; COPPER ZINC SUPEROXIDE DISMUTASE; FLUORESCENT DYE; FRAGILE X MENTAL RETARDATION PROTEIN; HISTIDINE; IMATINIB; LEPTIN; LIPOCORTIN 1; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 1; OSTEOPONTIN; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; PROLACTIN; PROTEIN 14 3 3; PROTEIN A; PROTEOME; SOMATOMEDIN B; STREPTAVIDIN; TRASTUZUMAB;

EID: 44649105713     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780043     Document Type: Review
Times cited : (6)

References (174)
  • 1
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250, 4007-4021.
    • (1975) J. Biol. Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 2
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals
    • Klose, J., Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik 1975, 26, 231-243.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 3
    • 0041733300 scopus 로고    scopus 로고
    • Evaluation of shotgun sequencing for proteomic analysis of human plasma using HPLC coupled with either ion trap or Fourier transform mass spectrometry
    • Wu, S. L., Choudhary, G., Ramstrom, M., Bergquist, J. et al., Evaluation of shotgun sequencing for proteomic analysis of human plasma using HPLC coupled with either ion trap or Fourier transform mass spectrometry. J. Proteome Res. 2003, 2, 383-393.
    • (2003) J. Proteome Res , vol.2 , pp. 383-393
    • Wu, S.L.1    Choudhary, G.2    Ramstrom, M.3    Bergquist, J.4
  • 4
    • 34748866570 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins
    • Braun, R. J., Kinkl, N., Beer, M., Ueffing, M., Two-dimensional electrophoresis of membrane proteins. Anal. Bioanal. Chem. 2007, 389, 1033-1045.
    • (2007) Anal. Bioanal. Chem , vol.389 , pp. 1033-1045
    • Braun, R.J.1    Kinkl, N.2    Beer, M.3    Ueffing, M.4
  • 5
    • 21244495253 scopus 로고    scopus 로고
    • 2D fluorescence difference gel analysis technology
    • The development of the DIGE system
    • Marouga, R., David, S., Hawkins, E., The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal. Bioanal. Chem. 2005, 382, 669-678.
    • (2005) Anal. Bioanal. Chem , vol.382 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 6
    • 0025951229 scopus 로고
    • Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation
    • Michel, H., Griffin, P. R., Shabanowitz, J., Hunt, D. F. et al., Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation. J. Biol. Chem. 1991, 266, 17584-17591.
    • (1991) J. Biol. Chem , vol.266 , pp. 17584-17591
    • Michel, H.1    Griffin, P.R.2    Shabanowitz, J.3    Hunt, D.F.4
  • 7
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R.3rd, Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242-247.
    • (2001) Nat. Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates 3rd, J.R.3
  • 8
    • 30544447982 scopus 로고    scopus 로고
    • Analysis of glycosylphosphatidylinositol protein anchors: The prion protein
    • Baldwin, M. A., Analysis of glycosylphosphatidylinositol protein anchors: the prion protein. Methods Enzymol. 2005, 405, 172-187.
    • (2005) Methods Enzymol , vol.405 , pp. 172-187
    • Baldwin, M.A.1
  • 9
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., Yates, J. R.3rd, A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76, 4193-4201.
    • (2004) Anal. Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates 3rd, J.R.3
  • 10
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F. et al., Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4
  • 11
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas, M., Hillenkamp, F., Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 12
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., Mann, M., Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 2005, 1, 252-262.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 13
    • 33749523582 scopus 로고    scopus 로고
    • Organellar proteomics: Turning inventories into insights
    • Andersen, J. S., Mann, M. Organellar proteomics: turning inventories into insights. EMBO Rep. 2006, 7, 874-879.
    • (2006) EMBO Rep , vol.7 , pp. 874-879
    • Andersen, J.S.1    Mann, M.2
  • 14
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen, H., Mann, M., The ABC's (and XYZ's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 2004, 5, 699-711.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 15
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 16
    • 3042689578 scopus 로고    scopus 로고
    • R.3rd, Mass spectral analysis in proteomics
    • Yates, J. R.3rd, Mass spectral analysis in proteomics. Annu. Rev. Biophys. Biomol. Struct. 2004, 33, 297-316.
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 297-316
    • Yates, J.1
  • 18
    • 13244289812 scopus 로고    scopus 로고
    • Does the genotype predict the phenotype? Evaluations of the hemostatic proteome
    • Mann, K. G., Brummel-Ziedins, K., Undas, A., Butenas, S., Does the genotype predict the phenotype? Evaluations of the hemostatic proteome. J. Thromb. Haemost. 2004, 2, 1727-1734.
    • (2004) J. Thromb. Haemost , vol.2 , pp. 1727-1734
    • Mann, K.G.1    Brummel-Ziedins, K.2    Undas, A.3    Butenas, S.4
  • 19
    • 33845979055 scopus 로고    scopus 로고
    • Proteomic analysis of spinal cord of presymptomatic amyotrophic lateral sclerosis G93A SOD1 mouse
    • Massignan, T., Casoni, F., Basso, M., Stefanazzi, P. et al., Proteomic analysis of spinal cord of presymptomatic amyotrophic lateral sclerosis G93A SOD1 mouse. Biochem. Biophys. Res. Commun. 2007, 353, 719-725.
    • (2007) Biochem. Biophys. Res. Commun , vol.353 , pp. 719-725
    • Massignan, T.1    Casoni, F.2    Basso, M.3    Stefanazzi, P.4
  • 20
    • 33644828728 scopus 로고    scopus 로고
    • In vivo protein sampling using capillary ultrafiltration semi-permeable hollow fiber and protein identification via mass spectrometry-based proteomics
    • Huang, C. M., Wang, C. C., Kawai, M., Barnes, S. et al., In vivo protein sampling using capillary ultrafiltration semi-permeable hollow fiber and protein identification via mass spectrometry-based proteomics. J. Chromatogr. A 2006, 1109, 144-151.
    • (2006) J. Chromatogr. A , vol.1109 , pp. 144-151
    • Huang, C.M.1    Wang, C.C.2    Kawai, M.3    Barnes, S.4
  • 21
    • 20344389505 scopus 로고    scopus 로고
    • Evidence for downregulation of calcium signaling proteins in advanced mouse adenocarcinoma
    • Ruddat, V. C., Whitman, S., Klein, R. D., Fischer, S. M. et al., Evidence for downregulation of calcium signaling proteins in advanced mouse adenocarcinoma. Prostate 2005, 64, 128-138.
    • (2005) Prostate , vol.64 , pp. 128-138
    • Ruddat, V.C.1    Whitman, S.2    Klein, R.D.3    Fischer, S.M.4
  • 22
    • 2942529235 scopus 로고    scopus 로고
    • Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy
    • Oh, P., Li, Y., Yu, J., Durr, E. et al., Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy. Nature 2004, 429, 629-635.
    • (2004) Nature , vol.429 , pp. 629-635
    • Oh, P.1    Li, Y.2    Yu, J.3    Durr, E.4
  • 24
    • 15944383003 scopus 로고    scopus 로고
    • Protein expression profiling of the drosophila fragile X mutant brain reveals up-regulation of monoamine synthesis
    • Zhang, Y. Q., Friedman, D. B., Wang, Z., Woodruff, E.3rd et al., Protein expression profiling of the drosophila fragile X mutant brain reveals up-regulation of monoamine synthesis. Mol. Cell. Proteomics. 2005, 4, 278-290.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 278-290
    • Zhang, Y.Q.1    Friedman, D.B.2    Wang, Z.3    Woodruff 3rd, E.4
  • 25
    • 0032555598 scopus 로고    scopus 로고
    • Hesslinger, C., Kremmer, E., Hultner, L., Ueffing, M. et al., Phosphorylation of GTP cyclohydrolase I and modulation of its activity in rodent mast cells. GTP cyclohydrolase I hyperphosphorylation is coupled to high affinity IgE receptor signaling and involves protein kinase C. J. Biol. Chem. 1998, 273, 21616-21622.
    • Hesslinger, C., Kremmer, E., Hultner, L., Ueffing, M. et al., Phosphorylation of GTP cyclohydrolase I and modulation of its activity in rodent mast cells. GTP cyclohydrolase I hyperphosphorylation is coupled to high affinity IgE receptor signaling and involves protein kinase C. J. Biol. Chem. 1998, 273, 21616-21622.
  • 26
    • 0036301947 scopus 로고    scopus 로고
    • A decade of molecular studies of fragile X syndrome
    • O'Donnell, W. T., Warren, S. T., A decade of molecular studies of fragile X syndrome. Annu. Rev. Neurosci. 2002, 25, 315-338.
    • (2002) Annu. Rev. Neurosci , vol.25 , pp. 315-338
    • O'Donnell, W.T.1    Warren, S.T.2
  • 27
    • 0027253061 scopus 로고
    • Long-term complications of diabetes mellitus
    • Nathan, D. M., Long-term complications of diabetes mellitus. N. Engl. J. Med. 1993, 328, 1676-1685.
    • (1993) N. Engl. J. Med , vol.328 , pp. 1676-1685
    • Nathan, D.M.1
  • 28
    • 33846991924 scopus 로고    scopus 로고
    • Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation
    • Gao, B. B., Clermont, A., Rook, S., Fonda, S. J. et al., Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation. Nat. Med. 2007, 13, 181-188.
    • (2007) Nat. Med , vol.13 , pp. 181-188
    • Gao, B.B.1    Clermont, A.2    Rook, S.3    Fonda, S.J.4
  • 29
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard, I., Broux, O., Allamand, V., Fougerousse, F. et al., Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 1995, 81, 27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3    Fougerousse, F.4
  • 30
    • 33845230658 scopus 로고    scopus 로고
    • Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice
    • Cohen, N., Kudryashova, E., Kramerova, I., Anderson, L. V. et al., Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Proteomics 2006, 6, 6075-6084.
    • (2006) Proteomics , vol.6 , pp. 6075-6084
    • Cohen, N.1    Kudryashova, E.2    Kramerova, I.3    Anderson, L.V.4
  • 31
    • 33644858832 scopus 로고    scopus 로고
    • Flagellar motility is required for the viability of the bloodstream trypanosome
    • Broadhead, R., Dawe, H. R., Farr, H., Griffiths, S. et al., Flagellar motility is required for the viability of the bloodstream trypanosome. Nature 2006, 440, 224-227.
    • (2006) Nature , vol.440 , pp. 224-227
    • Broadhead, R.1    Dawe, H.R.2    Farr, H.3    Griffiths, S.4
  • 32
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C. et al., A proteomics approach to understanding protein ubiquitination. Nat. Biotechnol. 2003, 21, 921-926.
    • (2003) Nat. Biotechnol , vol.21 , pp. 921-926
    • Peng, J.1    Schwartz, D.2    Elias, J.E.3    Thoreen, C.C.4
  • 33
    • 34247528121 scopus 로고    scopus 로고
    • A proteomics approach to identify the ubiquitinated proteins in mouse heart
    • Jeon, H. B., Choi, E. S., Yoon, J. H., Hwang, J. H. et al., A proteomics approach to identify the ubiquitinated proteins in mouse heart. Biochem. Biophys. Res. Commun. 2007, 357, 731-736.
    • (2007) Biochem. Biophys. Res. Commun , vol.357 , pp. 731-736
    • Jeon, H.B.1    Choi, E.S.2    Yoon, J.H.3    Hwang, J.H.4
  • 35
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B. et al., Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4
  • 36
    • 22544448129 scopus 로고    scopus 로고
    • Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice-a model of familial amyotrophic lateral sclerosis
    • Poon, H. F., Hensley, K., Thongboonkerd, V., Merchant, M. L. et al., Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice-a model of familial amyotrophic lateral sclerosis. Free Radic. Biol. Med. 2005, 39, 453-462.
    • (2005) Free Radic. Biol. Med , vol.39 , pp. 453-462
    • Poon, H.F.1    Hensley, K.2    Thongboonkerd, V.3    Merchant, M.L.4
  • 37
    • 22744455017 scopus 로고    scopus 로고
    • Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein
    • Poon, H. F., Farr, S. A., Banks, W. A., Pierce, W. M. et al., Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein. Brain Res. Mol. Brain Res. 2005, 138, 8-16.
    • (2005) Brain Res. Mol. Brain Res , vol.138 , pp. 8-16
    • Poon, H.F.1    Farr, S.A.2    Banks, W.A.3    Pierce, W.M.4
  • 38
    • 33644584055 scopus 로고    scopus 로고
    • Using proteomics and network analysis to elucidate the consequences of synaptic protein oxidation in a PS1 + AbetaPP mouse model of Alzheimer's disease
    • Soreghan, B. A., Lu, B. W., Thomas, S. N., Duff, K. et al., Using proteomics and network analysis to elucidate the consequences of synaptic protein oxidation in a PS1 + AbetaPP mouse model of Alzheimer's disease. J. Alzheimers Dis. 2005, 8, 227-241.
    • (2005) J. Alzheimers Dis , vol.8 , pp. 227-241
    • Soreghan, B.A.1    Lu, B.W.2    Thomas, S.N.3    Duff, K.4
  • 40
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M. et al., A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 1999, 17, 1030-1032.
    • (1999) Nat. Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4
  • 41
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan, N. J., Cagney, G., Yu, H., Zhong, G. et al., Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 2006, 440, 637-643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4
  • 42
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh, C., Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 2004, 381, 329-342.
    • (2004) Biochem. J , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 43
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand, P. O., Segura, I., Volkel, P., Ghidelli, S. et al., Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol. Cell. Proteomics 2006, 5, 2211-2227.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1    Segura, I.2    Volkel, P.3    Ghidelli, S.4
  • 44
    • 0037116832 scopus 로고    scopus 로고
    • Use of proteomic patterns in serum to identify ovarian cancer
    • Petricoin, E. F., Ardekani, A. M., Hitt, B. A., Levine, P. J. et al., Use of proteomic patterns in serum to identify ovarian cancer. Lancet 2002, 359, 572-577.
    • (2002) Lancet , vol.359 , pp. 572-577
    • Petricoin, E.F.1    Ardekani, A.M.2    Hitt, B.A.3    Levine, P.J.4
  • 45
    • 19644388098 scopus 로고    scopus 로고
    • Serum protein markers for early detection of ovarian cancer
    • Mor, G., Visintin, I., Lai, Y., Zhao, H. et al., Serum protein markers for early detection of ovarian cancer. Proc. Natl. Acad. Sci. USA 2005, 102, 7677-7682.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7677-7682
    • Mor, G.1    Visintin, I.2    Lai, Y.3    Zhao, H.4
  • 46
    • 34547197880 scopus 로고    scopus 로고
    • Identification of novel molecular candidates for acute liver failure in plasma of BALB/ c murine model
    • Lv, S., Wei, L., Wang, J. H., Wang, J. Y. et al., Identification of novel molecular candidates for acute liver failure in plasma of BALB/ c murine model. J. Proteome Res. 2007, 6, 2746-2752.
    • (2007) J. Proteome Res , vol.6 , pp. 2746-2752
    • Lv, S.1    Wei, L.2    Wang, J.H.3    Wang, J.Y.4
  • 47
    • 26844499100 scopus 로고    scopus 로고
    • Comparative plasma proteome analysis of lymphoma-bearing SJL mice
    • Bhat, V. B., Choi, M. H., Wishnok, J. S., Tannenbaum, S. R., Comparative plasma proteome analysis of lymphoma-bearing SJL mice. J. Proteome Res. 2005, 4, 1814-1825.
    • (2005) J. Proteome Res , vol.4 , pp. 1814-1825
    • Bhat, V.B.1    Choi, M.H.2    Wishnok, J.S.3    Tannenbaum, S.R.4
  • 48
    • 0034829648 scopus 로고    scopus 로고
    • Nitric oxide in gastrointestinal epithelial cell carcinogenesis: Linking inflammation to oncogenesis
    • Jaiswal, M., LaRusso, N. F., Gores, G. J., Nitric oxide in gastrointestinal epithelial cell carcinogenesis: linking inflammation to oncogenesis. Am. J. Physiol. Gastrointest. Liver Physiol. 2001, 281, G626-G634.
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol , vol.281
    • Jaiswal, M.1    LaRusso, N.F.2    Gores, G.J.3
  • 49
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L., Anderson, N. G., The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 50
    • 33745065543 scopus 로고    scopus 로고
    • Proteomic profiling of urinary protein excretion in the factor H-deficient mouse
    • Braun, M. C., Li, L., Ke, B., Dubinsky, W. P. et al., Proteomic profiling of urinary protein excretion in the factor H-deficient mouse. Am. J. Nephrol. 2006, 26, 127-135.
    • (2006) Am. J. Nephrol , vol.26 , pp. 127-135
    • Braun, M.C.1    Li, L.2    Ke, B.3    Dubinsky, W.P.4
  • 51
    • 33645993265 scopus 로고    scopus 로고
    • Global survey of organ and organelle protein expression in mouse: Combined proteomic and transcriptomic profiling
    • Kislinger, T., Cox, B., Kannan, A., Chung, C. et al., Global survey of organ and organelle protein expression in mouse: combined proteomic and transcriptomic profiling. Cell 2006, 125, 173-186.
    • (2006) Cell , vol.125 , pp. 173-186
    • Kislinger, T.1    Cox, B.2    Kannan, A.3    Chung, C.4
  • 52
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas, P. R., Vanhaesebroeck, B., Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol. Cell. Proteomics 2007.
    • (2007) Mol. Cell. Proteomics
    • Cutillas, P.R.1    Vanhaesebroeck, B.2
  • 53
    • 33646473345 scopus 로고    scopus 로고
    • A mammalian arganelle map by protein correlation profiling
    • Foster, L. J., de Hoog, C. L., Zhang, Y., Zhang, Y. et al., A mammalian arganelle map by protein correlation profiling. Cell 2006, 125, 187-199.
    • (2006) Cell , vol.125 , pp. 187-199
    • Foster, L.J.1    de Hoog, C.L.2    Zhang, Y.3    Zhang, Y.4
  • 54
    • 34548163934 scopus 로고    scopus 로고
    • Analysis of the mouse liver proteome using advanced mass spectrometry
    • Shi, R., Kumar, C., Zougman, A., Zhang, Y. et al., Analysis of the mouse liver proteome using advanced mass spectrometry. J. Proteome Res. 2007, 6, 2963-2972.
    • (2007) J. Proteome Res , vol.6 , pp. 2963-2972
    • Shi, R.1    Kumar, C.2    Zougman, A.3    Zhang, Y.4
  • 55
    • 33845500104 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of the secretory pathway
    • Gilchrist, A., Au, C. E., Hiding, J., Bell, A. W. et al., Quantitative proteomics analysis of the secretory pathway. Cell 2006, 127, 1265-1281.
    • (2006) Cell , vol.127 , pp. 1265-1281
    • Gilchrist, A.1    Au, C.E.2    Hiding, J.3    Bell, A.W.4
  • 56
    • 10744224439 scopus 로고    scopus 로고
    • Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria
    • Mootha, V. K., Bunkenborg, J., Olsen, J. V., Hjerrild, M. et al., Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 2003, 115, 629-640.
    • (2003) Cell , vol.115 , pp. 629-640
    • Mootha, V.K.1    Bunkenborg, J.2    Olsen, J.V.3    Hjerrild, M.4
  • 57
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer, E. C., Florens, L., Guan, T., Yates, J. R.3rd et al., Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 2003, 301, 1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates 3rd, J.R.4
  • 59
    • 34249089215 scopus 로고    scopus 로고
    • Integrated proteomic and transcriptomic profiling of mouse lung development and Nmyc target genes
    • Cox, B., Kislinger, T., Wigle, D. A., Kannan, A. et al., Integrated proteomic and transcriptomic profiling of mouse lung development and Nmyc target genes. Mol. Syst. Biol. 2007, 3, 109.
    • (2007) Mol. Syst. Biol , vol.3 , pp. 109
    • Cox, B.1    Kislinger, T.2    Wigle, D.A.3    Kannan, A.4
  • 61
    • 26844508449 scopus 로고    scopus 로고
    • Investigation of the mouse serum proteome
    • Hood, B. L., Zhou, M., Chan, K. C., Lucas, D. A. et al., Investigation of the mouse serum proteome. J. Proteome Res. 2005, 4, 1561-1568.
    • (2005) J. Proteome Res , vol.4 , pp. 1561-1568
    • Hood, B.L.1    Zhou, M.2    Chan, K.C.3    Lucas, D.A.4
  • 62
    • 23944492134 scopus 로고    scopus 로고
    • results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Overview of the HUPO Plasma Proteome Project
    • Omenn, G. S., States, D. J., Adamski, M., Blackwell, T. W. et al., Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 2005, 5, 3226-3245.
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4
  • 63
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • Adachi, J., Kumar, C., Zhang, Y., Olsen, J. V. et al., The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol 2006, 7, R80.
    • (2006) Genome Biol , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4
  • 64
    • 30744464378 scopus 로고    scopus 로고
    • Proteome analysis of isolated perfused organ effluent as a novel model for protein biomarker discovery
    • Koomen, J. M., Wilson, C. R., Guthrie, P., Androlewicz, M.J. et al., Proteome analysis of isolated perfused organ effluent as a novel model for protein biomarker discovery. J. Proteome Res. 2006, 5, 177-182.
    • (2006) J. Proteome Res , vol.5 , pp. 177-182
    • Koomen, J.M.1    Wilson, C.R.2    Guthrie, P.3    Androlewicz, M.J.4
  • 65
    • 32844467463 scopus 로고    scopus 로고
    • Myocardial preconditioning and remote renal preconditioning-identifying a protective factor using proteomic methods?
    • Lang, S. C., Elsasser, A., Scheler, C., Vetter, S. et al., Myocardial preconditioning and remote renal preconditioning-identifying a protective factor using proteomic methods? Basic Res. Cardiol. 2006, 101, 149-158.
    • (2006) Basic Res. Cardiol , vol.101 , pp. 149-158
    • Lang, S.C.1    Elsasser, A.2    Scheler, C.3    Vetter, S.4
  • 66
    • 25444473426 scopus 로고    scopus 로고
    • Autophagy in chronically ischemic myocardium
    • Yan, L., Vatner, D. E., Kim, S. J., Ge, H. et al., Autophagy in chronically ischemic myocardium. Proc. Natl. Acad. Sci. USA 2005, 102, 13807-13812.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13807-13812
    • Yan, L.1    Vatner, D.E.2    Kim, S.J.3    Ge, H.4
  • 67
    • 22044445138 scopus 로고    scopus 로고
    • Proteomic changes in the pressure overloaded right ventricle after 6 weeks in young rats: Correlations with the degree of hypertrophy
    • Faber, M. J., Dalinghaus, M., Lankhuizen, I. M., Bezstarosti, K. et al., Proteomic changes in the pressure overloaded right ventricle after 6 weeks in young rats: correlations with the degree of hypertrophy. Proteomics 2005, 5, 2519-2530.
    • (2005) Proteomics , vol.5 , pp. 2519-2530
    • Faber, M.J.1    Dalinghaus, M.2    Lankhuizen, I.M.3    Bezstarosti, K.4
  • 68
    • 6044224889 scopus 로고    scopus 로고
    • Cardiac mitochondrial damage and biogenesis in a chronic model of type 1 diabetes
    • Shen, X., Zheng, S., Thongboonkerd, V., Xu, M. et al., Cardiac mitochondrial damage and biogenesis in a chronic model of type 1 diabetes. Am. J. Physiol. Endocrinol. Metab. 2004, 287, E896-E905.
    • (2004) Am. J. Physiol. Endocrinol. Metab , vol.287
    • Shen, X.1    Zheng, S.2    Thongboonkerd, V.3    Xu, M.4
  • 69
    • 0141839835 scopus 로고    scopus 로고
    • Proteomic analysis of Rac1 transgenic mice displaying dilated cardiomyopathy reveals an increase in creatine kinase M-chain protein abundance
    • Buscemi, N., Doherty-Kirby, A., Sussman, M. A., Lajoie, G. et al., Proteomic analysis of Rac1 transgenic mice displaying dilated cardiomyopathy reveals an increase in creatine kinase M-chain protein abundance. Mol. Cell Biochem. 2003, 251, 145-151.
    • (2003) Mol. Cell Biochem , vol.251 , pp. 145-151
    • Buscemi, N.1    Doherty-Kirby, A.2    Sussman, M.A.3    Lajoie, G.4
  • 71
    • 33749997319 scopus 로고    scopus 로고
    • Altered expression of serum protein in ginsenoside Re-treated diabetic rats detected by SELDI-TOF MS
    • Cho, W. C., Yip, T. T., Chung, W. S., Lee, S. K. et al., Altered expression of serum protein in ginsenoside Re-treated diabetic rats detected by SELDI-TOF MS. J. Ethnopharmacol 2006, 108, 272-279.
    • (2006) J. Ethnopharmacol , vol.108 , pp. 272-279
    • Cho, W.C.1    Yip, T.T.2    Chung, W.S.3    Lee, S.K.4
  • 72
    • 24044453711 scopus 로고    scopus 로고
    • Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia
    • Morand, J. P., Macri, J., Adeli, K., Proteomic profiling of hepatic endoplasmic reticulum-associated proteins in an animal model of insulin resistance and metabolic dyslipidemia. J. Biol. Chem. 2005, 280, 17626-17633.
    • (2005) J. Biol. Chem , vol.280 , pp. 17626-17633
    • Morand, J.P.1    Macri, J.2    Adeli, K.3
  • 73
    • 16344382397 scopus 로고    scopus 로고
    • Effect of thyroxine on abnormal pancreatic proteomes of the hypothyroid rdw rat
    • Satoh, M., Haruta-Satoh, E., Omori, A., Oh-Ishi, M. et al., Effect of thyroxine on abnormal pancreatic proteomes of the hypothyroid rdw rat. Proteomics 2005, 5, 1113-1124.
    • (2005) Proteomics , vol.5 , pp. 1113-1124
    • Satoh, M.1    Haruta-Satoh, E.2    Omori, A.3    Oh-Ishi, M.4
  • 74
    • 33750839046 scopus 로고    scopus 로고
    • Differential serum proteomic analysis in a model of metabolic disease
    • Matsumura, T., Suzuki, T., Kada, N., Aizawa, K. et al., Differential serum proteomic analysis in a model of metabolic disease. Biochem. Biophys. Res. Commun. 2006, 351, 965-971.
    • (2006) Biochem. Biophys. Res. Commun , vol.351 , pp. 965-971
    • Matsumura, T.1    Suzuki, T.2    Kada, N.3    Aizawa, K.4
  • 75
    • 0032951971 scopus 로고    scopus 로고
    • A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643
    • Edvardsson, U., Alexandersson, M., Brockenhuus von Lowenhielm, H., Nystrom, A. C. et al., A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643. Electrophoresis 1999, 20, 935-942.
    • (1999) Electrophoresis , vol.20 , pp. 935-942
    • Edvardsson, U.1    Alexandersson, M.2    Brockenhuus von Lowenhielm, H.3    Nystrom, A.C.4
  • 76
    • 1642325261 scopus 로고    scopus 로고
    • Oxidative modification of hepatic mitochondria protein thiols: Effect of chronic alcohol consumption
    • Venkatraman, A., Landar, A., Davis, A. J., Ulasova, E. et al., Oxidative modification of hepatic mitochondria protein thiols: effect of chronic alcohol consumption. Am. J. Physiol. Gastrointest. Liver Physiol. 2004, 288, G521-G527.
    • (2004) Am. J. Physiol. Gastrointest. Liver Physiol , vol.288
    • Venkatraman, A.1    Landar, A.2    Davis, A.J.3    Ulasova, E.4
  • 77
    • 2542450761 scopus 로고    scopus 로고
    • Identification of novel molecular candidates for fatty liver in the hyperlipidemic mouse model, HcB19
    • Van Greevenbroek, M. M., Vermeulen, V. M., De Bruin, T. W., Identification of novel molecular candidates for fatty liver in the hyperlipidemic mouse model, HcB19. J. Lipid Res. 2004, 45, 1148-1154.
    • (2004) J. Lipid Res , vol.45 , pp. 1148-1154
    • Van Greevenbroek, M.M.1    Vermeulen, V.M.2    De Bruin, T.W.3
  • 78
    • 29144487134 scopus 로고    scopus 로고
    • Steatosis-induced proteomic changes in liver mitochondria evidenced by two-dimensional differential in-gel electrophoresis
    • Douette, P., Navet, R., Gerkens, P., de Pauw, E. et al., Steatosis-induced proteomic changes in liver mitochondria evidenced by two-dimensional differential in-gel electrophoresis. J. Proteome Res. 2005, 4, 2024-2031.
    • (2005) J. Proteome Res , vol.4 , pp. 2024-2031
    • Douette, P.1    Navet, R.2    Gerkens, P.3    de Pauw, E.4
  • 79
    • 33846004164 scopus 로고    scopus 로고
    • Changes of the hepatic proteome in murine models for toxically induced fibrogenesis and sclerosing cholangitis
    • Henkel, C., Roderfeld, M., Weiskirchen, R., Berres, M. L. et al., Changes of the hepatic proteome in murine models for toxically induced fibrogenesis and sclerosing cholangitis. Proteomics 2006, 6, 6538-6548.
    • (2006) Proteomics , vol.6 , pp. 6538-6548
    • Henkel, C.1    Roderfeld, M.2    Weiskirchen, R.3    Berres, M.L.4
  • 80
    • 33847660139 scopus 로고    scopus 로고
    • A useful model to audit liver resolution from cirrhosis in rats using functional proteomics
    • Liu, E. H., Chen, M. F., Yeh, T. S., Ho, Y. P. et al., A useful model to audit liver resolution from cirrhosis in rats using functional proteomics. J. Surg. Res. 2007, 138, 214-223.
    • (2007) J. Surg. Res , vol.138 , pp. 214-223
    • Liu, E.H.1    Chen, M.F.2    Yeh, T.S.3    Ho, Y.P.4
  • 81
    • 33747368740 scopus 로고    scopus 로고
    • Identification and preliminary validation of novel biomarkers of acute hepatic ischaemia/reperfusion injury using dual-platform proteomic/ degradomic approaches
    • Svetlov, S. I., Xiang, Y., Oli, M. W., Foley, D. P. et al., Identification and preliminary validation of novel biomarkers of acute hepatic ischaemia/reperfusion injury using dual-platform proteomic/ degradomic approaches. Biomarkers 2006, 11, 355-369.
    • (2006) Biomarkers , vol.11 , pp. 355-369
    • Svetlov, S.I.1    Xiang, Y.2    Oli, M.W.3    Foley, D.P.4
  • 82
    • 25444517040 scopus 로고    scopus 로고
    • Use of proteomic methods to identify serum biomarkers associated with rat liver toxicity or hypertrophy
    • Amacher, D. E., Adler, R., Herath, A., Townsend, R. R., Use of proteomic methods to identify serum biomarkers associated with rat liver toxicity or hypertrophy. Clin. Chem. 2005, 51, 1796-1803.
    • (2005) Clin. Chem , vol.51 , pp. 1796-1803
    • Amacher, D.E.1    Adler, R.2    Herath, A.3    Townsend, R.R.4
  • 83
    • 21144438395 scopus 로고    scopus 로고
    • Proteomic identification of potential susceptibility factors in drug-induced liver disease
    • Welch, K. D., Wen, B., Goodlett, D. R., Yi, E. C. et al., Proteomic identification of potential susceptibility factors in drug-induced liver disease. Chem. Res. Toxicol. 2005, 18, 924-933.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 924-933
    • Welch, K.D.1    Wen, B.2    Goodlett, D.R.3    Yi, E.C.4
  • 84
    • 1242294371 scopus 로고    scopus 로고
    • Copper-associated liver disease: A proteomics study of copper challenge in a sheep model
    • Simpson, D. M., Beynon, R. J., Robertson, D. H., Loughran, M. J. et al., Copper-associated liver disease: a proteomics study of copper challenge in a sheep model. Proteomics 2004, 4, 524-536.
    • (2004) Proteomics , vol.4 , pp. 524-536
    • Simpson, D.M.1    Beynon, R.J.2    Robertson, D.H.3    Loughran, M.J.4
  • 85
    • 33644669952 scopus 로고    scopus 로고
    • New data analysis and mining approaches identify unique proteome and transcriptome markers of susceptibility to autoimmune diabetes
    • Gerling, I. C., Singh, S., Lenchik, N. I., Marshall, D. R. et al., New data analysis and mining approaches identify unique proteome and transcriptome markers of susceptibility to autoimmune diabetes. Mol. Cell. Proteomics 2006, 5, 293-305.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 293-305
    • Gerling, I.C.1    Singh, S.2    Lenchik, N.I.3    Marshall, D.R.4
  • 86
    • 33748551714 scopus 로고    scopus 로고
    • Proteomic analysis of the autoantibody response following immunization with a single autoantigen
    • Mouquet, H., Drouot, L., Charlionnet, R., Arnoult, C. et al., Proteomic analysis of the autoantibody response following immunization with a single autoantigen. Proteomics 2006, 6, 4829-4837.
    • (2006) Proteomics , vol.6 , pp. 4829-4837
    • Mouquet, H.1    Drouot, L.2    Charlionnet, R.3    Arnoult, C.4
  • 87
    • 26044462379 scopus 로고    scopus 로고
    • Identification of immunodominant autoantigens in rat autoimmune orchitis
    • Fijak, M., Iosub, R., Schneider, E., Linder, M. et al., Identification of immunodominant autoantigens in rat autoimmune orchitis. J. Pathol. 2005, 207, 127-138.
    • (2005) J. Pathol , vol.207 , pp. 127-138
    • Fijak, M.1    Iosub, R.2    Schneider, E.3    Linder, M.4
  • 88
    • 7044271217 scopus 로고    scopus 로고
    • Antigens up the nose: Identification of putative biomarkers for nasal tolerance induction functional studies combined with proteomics
    • Boots, A. M., Verhaert, P. D., te Poele, R. J., Evers, S. et al., Antigens up the nose: identification of putative biomarkers for nasal tolerance induction functional studies combined with proteomics. J. Proteome Res. 2004, 3, 1056-1062.
    • (2004) J. Proteome Res , vol.3 , pp. 1056-1062
    • Boots, A.M.1    Verhaert, P.D.2    te Poele, R.J.3    Evers, S.4
  • 89
    • 33745250733 scopus 로고    scopus 로고
    • A novel mechanism of regulatory T cell-mediated down-regulation of autoimmunity
    • Qin, H. Y., Mukherjee, R., Lee-Chan, E., Ewen, C. et al., A novel mechanism of regulatory T cell-mediated down-regulation of autoimmunity. Int. Immunol. 2006, 18, 1001-1015.
    • (2006) Int. Immunol , vol.18 , pp. 1001-1015
    • Qin, H.Y.1    Mukherjee, R.2    Lee-Chan, E.3    Ewen, C.4
  • 90
    • 33750362127 scopus 로고    scopus 로고
    • Integrated molecular signature of disease: Analysis of influenza virus-infected macaques through functional genomics and proteomics
    • Baas, T., Baskin, C. R., Diamond, D. L., Garcia-Sastre, A. et al., Integrated molecular signature of disease: analysis of influenza virus-infected macaques through functional genomics and proteomics. J. Virol. 2006, 80, 10813-10828.
    • (2006) J. Virol , vol.80 , pp. 10813-10828
    • Baas, T.1    Baskin, C.R.2    Diamond, D.L.3    Garcia-Sastre, A.4
  • 91
    • 17444392125 scopus 로고    scopus 로고
    • Application of isotope coded affinity tag (ICAT) analysis for the identification of differentially expressed proteins following infection of atlantic salmon (Salmo salar) with infectious hematopoietic necrosis virus (IHNV) or Renibacterium salmoninarum (BKD)
    • Booy, A. T., Haddow, J. D., Ohlund, L. B., Hardie, D. B. et al., Application of isotope coded affinity tag (ICAT) analysis for the identification of differentially expressed proteins following infection of atlantic salmon (Salmo salar) with infectious hematopoietic necrosis virus (IHNV) or Renibacterium salmoninarum (BKD). J. Proteome Res. 2005, 4, 325-334.
    • (2005) J. Proteome Res , vol.4 , pp. 325-334
    • Booy, A.T.1    Haddow, J.D.2    Ohlund, L.B.3    Hardie, D.B.4
  • 92
    • 33846304285 scopus 로고    scopus 로고
    • Proteomic identification and characterization of bacterial factors associated with Burkholderia cenocepacia survival in a murine host
    • Chung, J. W., Speert, D. P., Proteomic identification and characterization of bacterial factors associated with Burkholderia cenocepacia survival in a murine host. Microbiology 2007, 153, 206-214.
    • (2007) Microbiology , vol.153 , pp. 206-214
    • Chung, J.W.1    Speert, D.P.2
  • 93
    • 25844501950 scopus 로고    scopus 로고
    • Detection of intra-amniotic infection in a rabbit model by proteomics-based amniotic fluid analysis
    • Klein, L. L., Freitag, B. C., Gibbs, R. S., Reddy, A. P. et al., Detection of intra-amniotic infection in a rabbit model by proteomics-based amniotic fluid analysis. Am. J. Obstet. Gynecol. 2005, 193, 1302-1306.
    • (2005) Am. J. Obstet. Gynecol , vol.193 , pp. 1302-1306
    • Klein, L.L.1    Freitag, B.C.2    Gibbs, R.S.3    Reddy, A.P.4
  • 94
    • 31044440224 scopus 로고    scopus 로고
    • Identification of autoantibody clusters that best predict lupus disease activity using glomerular proteome arrays
    • Li, Q. Z., Xie, C., Wu, T., Mackay, M. et al., Identification of autoantibody clusters that best predict lupus disease activity using glomerular proteome arrays. J. Clin. Invest. 2005, 115, 3428-3439.
    • (2005) J. Clin. Invest , vol.115 , pp. 3428-3439
    • Li, Q.Z.1    Xie, C.2    Wu, T.3    Mackay, M.4
  • 95
    • 18144424963 scopus 로고    scopus 로고
    • Proteomic analysis of anti-Francisella tularensis LVS antibody response in murine model of tularemia
    • Havlasova, J., Hernychova, L., Brychta, M., Hubalek, M. et al., Proteomic analysis of anti-Francisella tularensis LVS antibody response in murine model of tularemia. Proteomics 2005, 5, 2090-2103.
    • (2005) Proteomics , vol.5 , pp. 2090-2103
    • Havlasova, J.1    Hernychova, L.2    Brychta, M.3    Hubalek, M.4
  • 96
    • 33746537718 scopus 로고    scopus 로고
    • Biomarker and drug-target discovery using proteomics in a new rat model of sepsis-induced acute renal failure
    • Holly, M. K., Dear, J. W., Hu, X., Schechter, A. N. et al., Biomarker and drug-target discovery using proteomics in a new rat model of sepsis-induced acute renal failure. Kidney Int. 2006, 70, 496-506.
    • (2006) Kidney Int , vol.70 , pp. 496-506
    • Holly, M.K.1    Dear, J.W.2    Hu, X.3    Schechter, A.N.4
  • 97
    • 22344442393 scopus 로고    scopus 로고
    • Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation
    • Rosca, M. G., Mustata, T. G., Kinter, M. T., Ozdemir, A. M. et al., Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation. Am. J. Physiol. Renal Physiol. 2005, 289, F420-F430.
    • (2005) Am. J. Physiol. Renal Physiol , vol.289
    • Rosca, M.G.1    Mustata, T.G.2    Kinter, M.T.3    Ozdemir, A.M.4
  • 98
    • 34548152121 scopus 로고    scopus 로고
    • Markedly increased urinary preprohaptoglobin and haptoglobin in passive heymann nephritis: A differential proteomics approach
    • Ngai, H. H., Sit, W. H., Jiang, P. P., Thongboonkerd, V. et al., Markedly increased urinary preprohaptoglobin and haptoglobin in passive heymann nephritis: a differential proteomics approach. J. Proteome Res. 2007, 6, 3313-3320.
    • (2007) J. Proteome Res , vol.6 , pp. 3313-3320
    • Ngai, H.H.1    Sit, W.H.2    Jiang, P.P.3    Thongboonkerd, V.4
  • 99
    • 33645660388 scopus 로고    scopus 로고
    • Proteomic identification of alterations in metabolic enzymes and signaling proteins in hypokalemic nephropathy
    • Thongboonkerd. V., Chutipongtanate, S., Kanlaya, R., Songtawee, N. et al., Proteomic identification of alterations in metabolic enzymes and signaling proteins in hypokalemic nephropathy. Proteomics 2006, 6, 2273-2285.
    • (2006) Proteomics , vol.6 , pp. 2273-2285
    • Thongboonkerd, V.1    Chutipongtanate, S.2    Kanlaya, R.3    Songtawee, N.4
  • 100
    • 33947146170 scopus 로고    scopus 로고
    • Excreted urinary mediators in an animal model of experimental immune nephritis with potential pathogenic significance
    • Wu, T., Xie, C., Bhaskarabhatla, M., Yan, M. et al., Excreted urinary mediators in an animal model of experimental immune nephritis with potential pathogenic significance. Arthritis Rheum. 2007, 56, 949-959.
    • (2007) Arthritis Rheum , vol.56 , pp. 949-959
    • Wu, T.1    Xie, C.2    Bhaskarabhatla, M.3    Yan, M.4
  • 101
    • 33751004998 scopus 로고    scopus 로고
    • Serial changes in urinary proteome profile of membranous nephropathy: Implications for pathophysiology and biomarker discovery
    • Ngai, H. H., Sit, W. H.,.Jiang, P. P., Xu, R. J. et al., Serial changes in urinary proteome profile of membranous nephropathy: implications for pathophysiology and biomarker discovery. J. Proteome Res. 2006, 5, 3038-3047.
    • (2006) J. Proteome Res , vol.5 , pp. 3038-3047
    • Ngai, H.H.1    Sit, W.H.2    Jiang, P.P.3    Xu, R.J.4
  • 102
    • 33846248808 scopus 로고    scopus 로고
    • Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis
    • Curthoys, N. P., Taylor, L., Hoffert, J. D., Knepper, M. A., Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis. Am. J. Physiol. Renal Physiol. 2007, 292, F140-F147.
    • (2007) Am. J. Physiol. Renal Physiol , vol.292
    • Curthoys, N.P.1    Taylor, L.2    Hoffert, J.D.3    Knepper, M.A.4
  • 103
    • 33746300107 scopus 로고    scopus 로고
    • Informatics-assisted protein profiling in a transgenic mouse model of amyotrophic lateral sclerosis
    • Lukas, T. J., Luo, W. W., Mao, H., Cole, N. et al., Informatics-assisted protein profiling in a transgenic mouse model of amyotrophic lateral sclerosis. Mol. Cell. Proteomics 2006, 5, 1233-1244.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1233-1244
    • Lukas, T.J.1    Luo, W.W.2    Mao, H.3    Cole, N.4
  • 104
    • 14644400490 scopus 로고    scopus 로고
    • Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice - a model of familial amyotrophic lateral sclerosis
    • Perluigi, M., Fai Poon, H., Hensley, K., Pierce, W. M. et al., Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice - a model of familial amyotrophic lateral sclerosis. Free Radic. Biol. Med. 2005, 38, 960-968.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 960-968
    • Perluigi, M.1    Fai Poon, H.2    Hensley, K.3    Pierce, W.M.4
  • 105
    • 33846019607 scopus 로고    scopus 로고
    • Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes
    • David, D. C., Ittner, L. M., Gehrig, P., Nergenau, D. et al., Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes. Proteomics 2006, 6, 6566-6577.
    • (2006) Proteomics , vol.6 , pp. 6566-6577
    • David, D.C.1    Ittner, L.M.2    Gehrig, P.3    Nergenau, D.4
  • 106
    • 33846658032 scopus 로고    scopus 로고
    • Proteomic analysis of brain tissue from an Alzheimer's disease mouse model by two-dimensional difference gel electrophoresis
    • Sizova, D., Charbaut, E., Delalande, F., Poirier, F. et al., Proteomic analysis of brain tissue from an Alzheimer's disease mouse model by two-dimensional difference gel electrophoresis. Neurobiol. Aging 2007, 28, 357-370.
    • (2007) Neurobiol. Aging , vol.28 , pp. 357-370
    • Sizova, D.1    Charbaut, E.2    Delalande, F.3    Poirier, F.4
  • 107
    • 27144527588 scopus 로고    scopus 로고
    • Comparative proteomic analysis using samples obtained with laser microdissection and saturation dye labelling
    • Wilson, K. E., Marouga, R., Prime, J. E., Pashby, D. P. et al., Comparative proteomic analysis using samples obtained with laser microdissection and saturation dye labelling. Proteomics 2005, 5, 3851-3858.
    • (2005) Proteomics , vol.5 , pp. 3851-3858
    • Wilson, K.E.1    Marouga, R.2    Prime, J.E.3    Pashby, D.P.4
  • 108
    • 33745990556 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): Implications for Alzheimer's disease
    • Boyd-Kimball, D., Poon, H. F., Lynn, B. C., Cai, J. et al., Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta(1-42): implications for Alzheimer's disease. Neurobiol. Aging 2006, 27, 1239-1249.
    • (2006) Neurobiol. Aging , vol.27 , pp. 1239-1249
    • Boyd-Kimball, D.1    Poon, H.F.2    Lynn, B.C.3    Cai, J.4
  • 109
    • 18844440651 scopus 로고    scopus 로고
    • Proteomic identification of proteins oxidized by Abeta(1-42) in synaptosomes: Implications for Alzheimer's disease
    • Boyd-Kimball, D., Castegna, A., Sultana, R., Poon, H. F. et al., Proteomic identification of proteins oxidized by Abeta(1-42) in synaptosomes: implications for Alzheimer's disease. Brain Res. 2005, 1044, 206-215.
    • (2005) Brain Res , vol.1044 , pp. 206-215
    • Boyd-Kimball, D.1    Castegna, A.2    Sultana, R.3    Poon, H.F.4
  • 110
    • 21244486781 scopus 로고    scopus 로고
    • Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice
    • David, D. C., Hauptmann, S., Scherping, I., Schuessel, K. et al., Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice. J. Biol. Chem. 2005, 280, 23802-23814.
    • (2005) J. Biol. Chem , vol.280 , pp. 23802-23814
    • David, D.C.1    Hauptmann, S.2    Scherping, I.3    Schuessel, K.4
  • 111
    • 14544284095 scopus 로고    scopus 로고
    • Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: Implications for aging and age-related neurodegenerative disorders
    • Poon, H. F., Farr, S. A., Thongboonkerd, V., Lynn, B. C. et al., Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: implications for aging and age-related neurodegenerative disorders. Neurochem. Int. 2005, 46, 159-168.
    • (2005) Neurochem. Int , vol.46 , pp. 159-168
    • Poon, H.F.1    Farr, S.A.2    Thongboonkerd, V.3    Lynn, B.C.4
  • 112
    • 19944428309 scopus 로고    scopus 로고
    • Proteomics analysis of rat brain protein modulations by grape seed extract
    • Deshane, J., Chaves, L., Sarikonda, K. V., Isbell, S. et al., Proteomics analysis of rat brain protein modulations by grape seed extract. J. Agric. Food Chem. 2004, 52, 7872-7883.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 7872-7883
    • Deshane, J.1    Chaves, L.2    Sarikonda, K.V.3    Isbell, S.4
  • 113
    • 9744239546 scopus 로고    scopus 로고
    • Early dysregulation of hippocampal proteins in transgenic rats with Alzheimer's disease-linked mutations in amyloid precursor protein and presenilin 1
    • Vercauteren, F. G., Clerens, S., Roy, L., Hamel, N. et al., Early dysregulation of hippocampal proteins in transgenic rats with Alzheimer's disease-linked mutations in amyloid precursor protein and presenilin 1. Brain Res. Mol. Brain Res. 2004, 132, 241-259.
    • (2004) Brain Res. Mol. Brain Res , vol.132 , pp. 241-259
    • Vercauteren, F.G.1    Clerens, S.2    Roy, L.3    Hamel, N.4
  • 114
    • 8744315404 scopus 로고    scopus 로고
    • Profiling proteins related to amyloid deposited brain of Tg2576 mice
    • Shin, S. J., Lee, S. E., Boo, J. H., Kim, M. et al., Profiling proteins related to amyloid deposited brain of Tg2576 mice. Proteomics 2004, 4, 3359-3368.
    • (2004) Proteomics , vol.4 , pp. 3359-3368
    • Shin, S.J.1    Lee, S.E.2    Boo, J.H.3    Kim, M.4
  • 115
    • 1842634504 scopus 로고    scopus 로고
    • Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer's disease
    • Choi, J., Forster, M. J., McDonald, S. R., Weintraub, S. T. et al., Proteomic identification of specific oxidized proteins in ApoE-knockout mice: relevance to Alzheimer's disease. Free Radic. Biol. Med. 2004, 36, 1155-1162.
    • (2004) Free Radic. Biol. Med , vol.36 , pp. 1155-1162
    • Choi, J.1    Forster, M.J.2    McDonald, S.R.3    Weintraub, S.T.4
  • 117
    • 0036202915 scopus 로고    scopus 로고
    • Differential expression of brain proteins in glycogen synthase kinase-3 transgenic mice: A proteomics point of view
    • Tilleman, K., Stevens, I., Spittaels, K., Haute, C. V. et al., Differential expression of brain proteins in glycogen synthase kinase-3 transgenic mice: a proteomics point of view. Proteomics 2002, 2, 94-104.
    • (2002) Proteomics , vol.2 , pp. 94-104
    • Tilleman, K.1    Stevens, I.2    Spittaels, K.3    Haute, C.V.4
  • 118
    • 20944449099 scopus 로고    scopus 로고
    • Identification of glyoxalase-I as a protein marker in a mouse model of extremes in trait anxiety
    • Kromer, S. A., Kessler, M. S., Milfay, D., Birg, I. N. et al., Identification of glyoxalase-I as a protein marker in a mouse model of extremes in trait anxiety. J. Neurosci. 2005, 25, 4375-4384.
    • (2005) J. Neurosci , vol.25 , pp. 4375-4384
    • Kromer, S.A.1    Kessler, M.S.2    Milfay, D.3    Birg, I.N.4
  • 119
    • 20544442753 scopus 로고    scopus 로고
    • Rapid discovery of putative protein biomarkers of traumatic brain injury by SDS-PAGE-capillary liquid chromatography-tandem mass spectrometry
    • Haskins, W. E., Kobeissy, F. H., Wolper, R. A., Ottens, A. K. et al., Rapid discovery of putative protein biomarkers of traumatic brain injury by SDS-PAGE-capillary liquid chromatography-tandem mass spectrometry. J. Neurotrauma 2005, 22, 629-644.
    • (2005) J. Neurotrauma , vol.22 , pp. 629-644
    • Haskins, W.E.1    Kobeissy, F.H.2    Wolper, R.A.3    Ottens, A.K.4
  • 120
    • 33748776575 scopus 로고    scopus 로고
    • Proteomics of cerebral injury in a neonatal model of cardiopulmonary bypass with deep hypothermic circulatory arrest
    • Sheikh, A. M., Barrett, C., Villamizar, N., Alzate, O. et al., Proteomics of cerebral injury in a neonatal model of cardiopulmonary bypass with deep hypothermic circulatory arrest. J. Thorac. Cardiovasc. Surg. 2006, 132, 820-828.
    • (2006) J. Thorac. Cardiovasc. Surg , vol.132 , pp. 820-828
    • Sheikh, A.M.1    Barrett, C.2    Villamizar, N.3    Alzate, O.4
  • 121
    • 33947721589 scopus 로고    scopus 로고
    • Neurogenesis and major depression: Implications from proteomic analyses of hippocampal proteins in a rat depression model
    • Mu, J., Xie, P., Yang, Z. S., Yang, D. L. et al., Neurogenesis and major depression: implications from proteomic analyses of hippocampal proteins in a rat depression model. Neurosci. Lett. 2007, 416, 252-256.
    • (2007) Neurosci. Lett , vol.416 , pp. 252-256
    • Mu, J.1    Xie, P.2    Yang, Z.S.3    Yang, D.L.4
  • 122
    • 3042518994 scopus 로고    scopus 로고
    • Altered expression of hypothetical proteins in hippocampus of transgenic mice overexpressing human Cu/Zn-superoxide dismutase 1
    • Shin, J. H., Yang, J. W., Le Pecheur, M., London, J. et al., Altered expression of hypothetical proteins in hippocampus of transgenic mice overexpressing human Cu/Zn-superoxide dismutase 1. Proteome Sci. 2004, 2, 2.
    • (2004) Proteome Sci , vol.2 , pp. 2
    • Shin, J.H.1    Yang, J.W.2    Le Pecheur, M.3    London, J.4
  • 123
    • 20144365266 scopus 로고    scopus 로고
    • Proteomic identification of the involvement of the mitochondrial rieske protein in epilepsy
    • Junker, H., Spate, K., Suofu, Y., Walther, R. et al., Proteomic identification of the involvement of the mitochondrial rieske protein in epilepsy. Epilepsia 2005, 46, 339-343.
    • (2005) Epilepsia , vol.46 , pp. 339-343
    • Junker, H.1    Spate, K.2    Suofu, Y.3    Walther, R.4
  • 124
    • 17844379952 scopus 로고    scopus 로고
    • Analysis of cerebellum proteomics in the hydrocephalic H-Tx rat
    • Li, X., Miyajima, M., Mineki, R., Taka, H. et al., Analysis of cerebellum proteomics in the hydrocephalic H-Tx rat. Neuroreport 2005, 16, 571-574.
    • (2005) Neuroreport , vol.16 , pp. 571-574
    • Li, X.1    Miyajima, M.2    Mineki, R.3    Taka, H.4
  • 125
    • 19344364786 scopus 로고    scopus 로고
    • Comparative proteomic analysis of the rat spinal cord in inflammatory and neuropathic pain models
    • Kunz, S., Tegeder, I., Coste, O., Marian, C. et al., Comparative proteomic analysis of the rat spinal cord in inflammatory and neuropathic pain models. Neurosci. Lett. 2005, 381, 289-293.
    • (2005) Neurosci. Lett , vol.381 , pp. 289-293
    • Kunz, S.1    Tegeder, I.2    Coste, O.3    Marian, C.4
  • 126
    • 8644228438 scopus 로고    scopus 로고
    • The nonerythropoietic asialoerythropoietin protects against neonatal hypoxia-ischemia as potently as erythropoietin
    • Wang, X., Zhu, C., Wang, X., Gerwien, J. G. et al., The nonerythropoietic asialoerythropoietin protects against neonatal hypoxia-ischemia as potently as erythropoietin. J. Neurochem. 2004, 91, 900-910.
    • (2004) J. Neurochem , vol.91 , pp. 900-910
    • Wang, X.1    Zhu, C.2    Wang, X.3    Gerwien, J.G.4
  • 127
    • 14744280985 scopus 로고    scopus 로고
    • Effect of chronic morphine exposure on the synaptic plasma-membrane subproteome of rats: A quantitative protein profiling study based on isotope-coded affinity tags and liquid chromatography/mass spectrometry
    • Prokai, L., Zharikova, A. D., Stevens, S. M., Jr., Effect of chronic morphine exposure on the synaptic plasma-membrane subproteome of rats: a quantitative protein profiling study based on isotope-coded affinity tags and liquid chromatography/mass spectrometry. J. Mass Spectrom. 2005, 40, 169-175.
    • (2005) J. Mass Spectrom , vol.40 , pp. 169-175
    • Prokai, L.1    Zharikova, A.D.2    Stevens Jr., S.M.3
  • 128
    • 33745727818 scopus 로고    scopus 로고
    • Impairment of mitochondrial anti-oxidant defence in SOD1-related motor neuron injury and amelioration by ebselen
    • Wood-Allum, C. A., Barber, S. C., Kirby, J., Heath, P. et al., Impairment of mitochondrial anti-oxidant defence in SOD1-related motor neuron injury and amelioration by ebselen. Brain 2006, 129, 1693-1709.
    • (2006) Brain , vol.129 , pp. 1693-1709
    • Wood-Allum, C.A.1    Barber, S.C.2    Kirby, J.3    Heath, P.4
  • 129
    • 33747791792 scopus 로고    scopus 로고
    • Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags
    • Hu, J., Qian, J., Borisov, O., Pan, S. et al., Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags. Proteomics 2006, 6, 4321-4334.
    • (2006) Proteomics , vol.6 , pp. 4321-4334
    • Hu, J.1    Qian, J.2    Borisov, O.3    Pan, S.4
  • 130
    • 33747164766 scopus 로고    scopus 로고
    • Comparative proteomics in neurodegenerative and non-neuro-degenerative diseases suggest nodal point proteins in regulatory networking
    • Zabel, C., Sagi, D., Kaindl, A. M., Steireif, N. et al., Comparative proteomics in neurodegenerative and non-neuro-degenerative diseases suggest nodal point proteins in regulatory networking. J. Proteome Res. 2006, 5, 1948-1958.
    • (2006) J. Proteome Res , vol.5 , pp. 1948-1958
    • Zabel, C.1    Sagi, D.2    Kaindl, A.M.3    Steireif, N.4
  • 131
    • 0034826237 scopus 로고    scopus 로고
    • Changes in the levels of low-abundance brain proteins induced by kainic acid
    • Krapfenbauer, K., Berger, M., Friedlein, A., Lubec, G. et al., Changes in the levels of low-abundance brain proteins induced by kainic acid. Eur. J. Biochem. 2001, 268, 3532-3537.
    • (2001) Eur. J. Biochem , vol.268 , pp. 3532-3537
    • Krapfenbauer, K.1    Berger, M.2    Friedlein, A.3    Lubec, G.4
  • 132
    • 4444242850 scopus 로고    scopus 로고
    • Proteomic identification of brainstem cytosolic proteins in a neuropathic pain model
    • Alzate, O., Hussain, S. R., Goettl, V. M., Tewari, A. K. et al., Proteomic identification of brainstem cytosolic proteins in a neuropathic pain model. Brain Res. Mol. Brain Res. 2004, 128, 193-200.
    • (2004) Brain Res. Mol. Brain Res , vol.128 , pp. 193-200
    • Alzate, O.1    Hussain, S.R.2    Goettl, V.M.3    Tewari, A.K.4
  • 133
    • 4444296075 scopus 로고    scopus 로고
    • Proteomic analysis of differential protein expression in neuropathic pain and electroacupuncture treatment models
    • Sung, H. J., Kim, Y. S., Kim, I. S., Jang, S. W. et al., Proteomic analysis of differential protein expression in neuropathic pain and electroacupuncture treatment models. Proteomics 2004, 4, 2805-2813.
    • (2004) Proteomics , vol.4 , pp. 2805-2813
    • Sung, H.J.1    Kim, Y.S.2    Kim, I.S.3    Jang, S.W.4
  • 134
    • 32344443679 scopus 로고    scopus 로고
    • Decreased striatal levels of PEP-19 following MPTP lesion in the mouse
    • Skold, K., Svensson, M., Nilsson, A., Zhang, X. et al., Decreased striatal levels of PEP-19 following MPTP lesion in the mouse. J. Proteome Res. 2006, 5, 262-269.
    • (2006) J. Proteome Res , vol.5 , pp. 262-269
    • Skold, K.1    Svensson, M.2    Nilsson, A.3    Zhang, X.4
  • 135
    • 28844439032 scopus 로고    scopus 로고
    • Proteomic analysis of parkin knockout mice: Alterations in energy metabolism, protein handling and synaptic function
    • Periquet, M., Corti, O., Jacquier, S., Brice, A., Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J. Neurochem. 2005, 95, 1259-1276.
    • (2005) J. Neurochem , vol.95 , pp. 1259-1276
    • Periquet, M.1    Corti, O.2    Jacquier, S.3    Brice, A.4
  • 136
    • 21244475585 scopus 로고    scopus 로고
    • A proteomic approach in the study of an animal model of Parkinson's disease
    • De Iuliis, A., Grigoletto, J., Recchia, A., Giusti, P. et al., A proteomic approach in the study of an animal model of Parkinson's disease. Clin. Chim. Acta. 2005, 357, 202-209.
    • (2005) Clin. Chim. Acta , vol.357 , pp. 202-209
    • De Iuliis, A.1    Grigoletto, J.2    Recchia, A.3    Giusti, P.4
  • 137
    • 15544374722 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondrial proteins: Relevance to Lewy body formation and Parkinson's disease
    • Jin, J., Meredith, G. E., Chen, L., Zhou, Y. et al., Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease. Brain Res. Mol. Brain Res. 2005, 134, 119-138.
    • (2005) Brain Res. Mol. Brain Res , vol.134 , pp. 119-138
    • Jin, J.1    Meredith, G.E.2    Chen, L.3    Zhou, Y.4
  • 138
    • 33749065106 scopus 로고    scopus 로고
    • La, Y., Wan, C., Zhu, H., Yang, Y. et al., Hippocampus protein profiling reveals aberration of malate dehydrogenase in chlorpromazine/ clozapine treated rats. Neurosci. Lett. 2006, 408, 29-34.
    • La, Y., Wan, C., Zhu, H., Yang, Y. et al., Hippocampus protein profiling reveals aberration of malate dehydrogenase in chlorpromazine/ clozapine treated rats. Neurosci. Lett. 2006, 408, 29-34.
  • 139
    • 4644306986 scopus 로고    scopus 로고
    • Analysis of pathological events at the onset of brain damage in stroke-prone rats: A proteomics and magnetic resonance imaging approach
    • Sironi, L., Guerrini, U., Tremoli, E., Miller, I. et al., Analysis of pathological events at the onset of brain damage in stroke-prone rats: a proteomics and magnetic resonance imaging approach. J. Neurosci. Res. 2004, 78, 115-122.
    • (2004) J. Neurosci. Res , vol.78 , pp. 115-122
    • Sironi, L.1    Guerrini, U.2    Tremoli, E.3    Miller, I.4
  • 140
    • 1842614423 scopus 로고    scopus 로고
    • Putative endogenous mediators of preconditioning-induced ischemic tolerance in rat brain identified by genomic and proteomic analysis
    • Dhodda, V. K., Sailor, K. A., Bowen, K. K., Vemuganti, R., Putative endogenous mediators of preconditioning-induced ischemic tolerance in rat brain identified by genomic and proteomic analysis. J. Neurochem. 2004, 89, 73-89.
    • (2004) J. Neurochem , vol.89 , pp. 73-89
    • Dhodda, V.K.1    Sailor, K.A.2    Bowen, K.K.3    Vemuganti, R.4
  • 141
    • 0347133172 scopus 로고    scopus 로고
    • Gene expression profiling and functional proteomic analysis reveal perturbed kinase-mediated signaling in genetic stroke susceptibility
    • Fornage, M., Swank, M. W., Boerwinkle, E., Doris, P. A., Gene expression profiling and functional proteomic analysis reveal perturbed kinase-mediated signaling in genetic stroke susceptibility. Physiol. Genomics 2003, 15, 75-83.
    • (2003) Physiol. Genomics , vol.15 , pp. 75-83
    • Fornage, M.1    Swank, M.W.2    Boerwinkle, E.3    Doris, P.A.4
  • 142
    • 0034745247 scopus 로고    scopus 로고
    • Acute-phase proteins before cerebral ischemia in stroke-prone rats: Identification by proteomics
    • Sironi, L., Tremoli, E., Miller, I., Guerrini, U. et al., Acute-phase proteins before cerebral ischemia in stroke-prone rats: identification by proteomics. Stroke 2001, 32, 753-760.
    • (2001) Stroke , vol.32 , pp. 753-760
    • Sironi, L.1    Tremoli, E.2    Miller, I.3    Guerrini, U.4
  • 143
    • 33748142538 scopus 로고    scopus 로고
    • Gel-based hippocampal proteomic analysis 2 weeks following traumatic brain injury to immature rats using controlled cortical impact
    • Kochanek, A. R., Kline, A. E., Gao, W. M., Chadha, M. et al., Gel-based hippocampal proteomic analysis 2 weeks following traumatic brain injury to immature rats using controlled cortical impact. Dev. Neurosci. 2006, 28, 410-419.
    • (2006) Dev. Neurosci , vol.28 , pp. 410-419
    • Kochanek, A.R.1    Kline, A.E.2    Gao, W.M.3    Chadha, M.4
  • 144
    • 2942560510 scopus 로고    scopus 로고
    • Proteins released from degenerating neurons are surrogate markers for acute brain damage
    • Siman, R., McIntosh, T. K., Soltesz, K. M., Chen, Z. et al., Proteins released from degenerating neurons are surrogate markers for acute brain damage. Neurobiol. Dis. 2004, 16, 311-320.
    • (2004) Neurobiol. Dis , vol.16 , pp. 311-320
    • Siman, R.1    McIntosh, T.K.2    Soltesz, K.M.3    Chen, Z.4
  • 145
    • 8744300809 scopus 로고    scopus 로고
    • Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness
    • Ge, Y., Rajkumar, L., Guzman, R. C., Nandi, S. et al., Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness. Proteomics 2004, 4, 3464-3467.
    • (2004) Proteomics , vol.4 , pp. 3464-3467
    • Ge, Y.1    Rajkumar, L.2    Guzman, R.C.3    Nandi, S.4
  • 146
    • 33845193926 scopus 로고    scopus 로고
    • Mass spectrometric proteomics profiles of in vivo tumor secretomes: Capillary ultrafiltration sampling of regressive tumor masses
    • Huang, C. M., Ananthaswamy, H. N., Barnes, S., Ma, Y. et al., Mass spectrometric proteomics profiles of in vivo tumor secretomes: capillary ultrafiltration sampling of regressive tumor masses. Proteomics 2006, 6, 6107-6116.
    • (2006) Proteomics , vol.6 , pp. 6107-6116
    • Huang, C.M.1    Ananthaswamy, H.N.2    Barnes, S.3    Ma, Y.4
  • 147
    • 20144364629 scopus 로고    scopus 로고
    • A proteomics approach to identify changes in protein profiles in pre-cancerous colon
    • Drew, J. E., Rucklidge, G. J., Duncan, G., Lufty, A. et al., A proteomics approach to identify changes in protein profiles in pre-cancerous colon. Biochem. Biophys. Res. Commun. 2005, 330, 81-87.
    • (2005) Biochem. Biophys. Res. Commun , vol.330 , pp. 81-87
    • Drew, J.E.1    Rucklidge, G.J.2    Duncan, G.3    Lufty, A.4
  • 148
    • 20044377211 scopus 로고    scopus 로고
    • Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans
    • Block, T. M., Comunale, M. A., Lowman, M., Steel, L. F. et al., Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans. Proc. Natl. Acad. Sci. USA 2005, 102, 779-784.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 779-784
    • Block, T.M.1    Comunale, M.A.2    Lowman, M.3    Steel, L.F.4
  • 149
    • 33745225174 scopus 로고    scopus 로고
    • Plasma proteame analysis reveals the geographical origin and liver tumor status of Dab (Limanda limanda) from UK marine waters
    • Ward, D. G., Wei, W., Cheng, Y., Billingham, L. J. et al., Plasma proteame analysis reveals the geographical origin and liver tumor status of Dab (Limanda limanda) from UK marine waters. Environ. Sci. Technol. 2006, 40, 4031-4036.
    • (2006) Environ. Sci. Technol , vol.40 , pp. 4031-4036
    • Ward, D.G.1    Wei, W.2    Cheng, Y.3    Billingham, L.J.4
  • 150
    • 23044514276 scopus 로고    scopus 로고
    • Quantitative analysis of the low molecular weight serum proteome using 18O stable isotope labeling in a lung tumor xenograft mouse model
    • Hood, B. L., Lucas, D. A., Kim, G., Chan, K. C. et al., Quantitative analysis of the low molecular weight serum proteome using 18O stable isotope labeling in a lung tumor xenograft mouse model. J. Am. Soc. Mass Spectrom. 2005, 16, 1221-1230.
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1221-1230
    • Hood, B.L.1    Lucas, D.A.2    Kim, G.3    Chan, K.C.4
  • 151
    • 33750093232 scopus 로고    scopus 로고
    • Statistically integrated metabonomic-proteomic studies on a human prostate cancer xenograft model in mice
    • Rantalainen, M., Cloarec, O., Beckonert, O., Wilson, I. D. et al., Statistically integrated metabonomic-proteomic studies on a human prostate cancer xenograft model in mice. J. Proteome Res. 2006, 5, 2642-2655.
    • (2006) J. Proteome Res , vol.5 , pp. 2642-2655
    • Rantalainen, M.1    Cloarec, O.2    Beckonert, O.3    Wilson, I.D.4
  • 152
    • 33746441661 scopus 로고    scopus 로고
    • AlphaA-crystallin expression prevents gamma-crystallin insolubility and cataract formation in the zebrafish cloche mutant lens
    • Goishi, K., Shimizu, A., Najarro, G., Watanabe, S. et al., AlphaA-crystallin expression prevents gamma-crystallin insolubility and cataract formation in the zebrafish cloche mutant lens. Development 2006, 133, 2585-2593.
    • (2006) Development , vol.133 , pp. 2585-2593
    • Goishi, K.1    Shimizu, A.2    Najarro, G.3    Watanabe, S.4
  • 153
    • 34249654462 scopus 로고    scopus 로고
    • Application of two-dimensional electrophoresis in the research of retinal proteins of diabetic rat
    • Liu, S., Zhang, Y., Xie, X., Hu, W. et al., Application of two-dimensional electrophoresis in the research of retinal proteins of diabetic rat. Cell. Mol. Immunol. 2007, 4, 65-70.
    • (2007) Cell. Mol. Immunol , vol.4 , pp. 65-70
    • Liu, S.1    Zhang, Y.2    Xie, X.3    Hu, W.4
  • 154
    • 33745650746 scopus 로고    scopus 로고
    • Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis
    • Bhattacharya, S. K., Crabb, J. S., Bonilha, V. L., Gu, X. et al., Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. Invest. Ophthalmol. Vis. Sci. 2006, 47, 2508-2514.
    • (2006) Invest. Ophthalmol. Vis. Sci , vol.47 , pp. 2508-2514
    • Bhattacharya, S.K.1    Crabb, J.S.2    Bonilha, V.L.3    Gu, X.4
  • 155
    • 27244444388 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified retinal proteins in a chronic pressure-induced rat model of glaucoma
    • Tezel, G., Yang, X., Cai, J., Proteomic identification of oxidatively modified retinal proteins in a chronic pressure-induced rat model of glaucoma. Invest. Ophthalmol. Vis. Sci. 2005, 46, 3177-3187.
    • (2005) Invest. Ophthalmol. Vis. Sci , vol.46 , pp. 3177-3187
    • Tezel, G.1    Yang, X.2    Cai, J.3
  • 156
    • 33751418375 scopus 로고    scopus 로고
    • Identification of apolipoprotein A-I as a "STOP" signal for myopia
    • Bertrand, E., Fritsch, C., Diether, S., Lambrou, G. et al. Identification of apolipoprotein A-I as a "STOP" signal for myopia. Mol. Cell. Proteomics 2006, 5, 2158-2166.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2158-2166
    • Bertrand, E.1    Fritsch, C.2    Diether, S.3    Lambrou, G.4
  • 157
    • 26444583909 scopus 로고    scopus 로고
    • Molecular composition of drusen and possible involvement of anti-retinal autoimmunity in two different forms of macular degeneration in cynomolgus monkey (Macaca fascicularis)
    • Umeda, S., Suzuki, M. T., Okamoto, H., Ono, F. et al., Molecular composition of drusen and possible involvement of anti-retinal autoimmunity in two different forms of macular degeneration in cynomolgus monkey (Macaca fascicularis). FASEB J. 2005, 19, 1683-1685.
    • (2005) FASEB J , vol.19 , pp. 1683-1685
    • Umeda, S.1    Suzuki, M.T.2    Okamoto, H.3    Ono, F.4
  • 158
    • 0346097946 scopus 로고    scopus 로고
    • Proteome analysis of diseased joints from mice suffering from collagen-induced arthritis
    • Lorenz, P., Bantscheff, M., Ibrahim, S, M., Thiesen, H. J. et al., Proteome analysis of diseased joints from mice suffering from collagen-induced arthritis. Clin. Chem. Lab. Med. 2003, 41, 1622-1632.
    • (2003) Clin. Chem. Lab. Med , vol.41 , pp. 1622-1632
    • Lorenz, P.1    Bantscheff, M.2    Ibrahim, S.M.3    Thiesen, H.J.4
  • 159
    • 18144392652 scopus 로고    scopus 로고
    • Response of apolipoprotein E*3-Leiden transgenic mice to dietary fatty acids: Combining liver proteomics with physiological data
    • de Roos, B., Duivenvoorden, I., Rucklidge, G., Reid, M. et al., Response of apolipoprotein E*3-Leiden transgenic mice to dietary fatty acids: combining liver proteomics with physiological data. FASEB J. 2005, 19, 813-815.
    • (2005) FASEB J , vol.19 , pp. 813-815
    • de Roos, B.1    Duivenvoorden, I.2    Rucklidge, G.3    Reid, M.4
  • 160
    • 33747203986 scopus 로고    scopus 로고
    • A proteomic analysis of liver mitochondria during acute endotoxemia
    • Crouser, E. D., Julian, M. W., Huff, J. E., Mandich, D. V. et al., A proteomic analysis of liver mitochondria during acute endotoxemia. Intensive Care Med. 2006, 32, 1252-1262.
    • (2006) Intensive Care Med , vol.32 , pp. 1252-1262
    • Crouser, E.D.1    Julian, M.W.2    Huff, J.E.3    Mandich, D.V.4
  • 161
    • 18844461709 scopus 로고    scopus 로고
    • Synergism of Helicobacter pylori infection and stress on the augmentation of gastric mucosal damage and its prevention with alpha-tocopherol
    • Oh, T. Y., Yeo, M., Han, S. U., Cho, Y. K. et al., Synergism of Helicobacter pylori infection and stress on the augmentation of gastric mucosal damage and its prevention with alpha-tocopherol. Free Radic. Biol. Med. 2005, 38, 1447-1457.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1447-1457
    • Oh, T.Y.1    Yeo, M.2    Han, S.U.3    Cho, Y.K.4
  • 162
    • 33749024739 scopus 로고    scopus 로고
    • Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C)
    • Fan, X., Zhang, H., Zhang, S., Bagshaw, R. D. et al., Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C). Am. J. Hum. Genet. 2006, 79, 738-744.
    • (2006) Am. J. Hum. Genet , vol.79 , pp. 738-744
    • Fan, X.1    Zhang, H.2    Zhang, S.3    Bagshaw, R.D.4
  • 163
    • 33845440787 scopus 로고    scopus 로고
    • Proteomic identification of altered proteins in skeletal muscle during chronic potassium depletion: Implications for hypokalemic myopathy
    • Thongboonkerd, V., Kanlaya, R., Sinchaikul, S., Parichatikanond, P. et al., Proteomic identification of altered proteins in skeletal muscle during chronic potassium depletion: Implications for hypokalemic myopathy. J. Proteome Res. 2006, 5, 3326-3335.
    • (2006) J. Proteome Res , vol.5 , pp. 3326-3335
    • Thongboonkerd, V.1    Kanlaya, R.2    Sinchaikul, S.3    Parichatikanond, P.4
  • 164
    • 0038045723 scopus 로고    scopus 로고
    • High-throughput proteomics and protein biomarker discovery in an experimental model of inflammatory hyperalgesia: Effects of nimesulide
    • Gineste, C., Ho, L., Pompl, P., Bianchi, M. et al., High-throughput proteomics and protein biomarker discovery in an
    • (2003) Drugs , vol.63 , Issue.SUPPL. 1 , pp. 23-29
    • Gineste, C.1    Ho, L.2    Pompl, P.3    Bianchi, M.4
  • 165
    • 33847278485 scopus 로고    scopus 로고
    • Identification of novel peptide safety markers for exocrine pancreatic toxicity induced by cyanohydroxybutene
    • Walgren, J. L., Mitchell, M. D., Whiteley, L. O., Thompson, D. C., Identification of novel peptide safety markers for exocrine pancreatic toxicity induced by cyanohydroxybutene. Toxicol. Sci. 2007, 96, 174-183.
    • (2007) Toxicol. Sci , vol.96 , pp. 174-183
    • Walgren, J.L.1    Mitchell, M.D.2    Whiteley, L.O.3    Thompson, D.C.4
  • 166
    • 5644247158 scopus 로고    scopus 로고
    • Exploring the context of the lung proteome within the airway mucosa following allergen challenge
    • Fehniger, T. E., Sato-Folatre, J. G., Malmstrom, J., Berglund, M. et al., Exploring the context of the lung proteome within the airway mucosa following allergen challenge. J. Proteome Res. 2004, 3, 307-320.
    • (2004) J. Proteome Res , vol.3 , pp. 307-320
    • Fehniger, T.E.1    Sato-Folatre, J.G.2    Malmstrom, J.3    Berglund, M.4
  • 167
    • 24644494883 scopus 로고    scopus 로고
    • Proteomic analysis of differently expressed proteins in a mouse model for allergic asthma
    • Jeong, H., Rhim, T., Ahn, M. H., Yoon, P. O. et al., Proteomic analysis of differently expressed proteins in a mouse model for allergic asthma. J. Korean Med. Sci. 2005, 20, 579-585.
    • (2005) J. Korean Med. Sci , vol.20 , pp. 579-585
    • Jeong, H.1    Rhim, T.2    Ahn, M.H.3    Yoon, P.O.4
  • 168
    • 23044466028 scopus 로고    scopus 로고
    • Increased lungkine and chitinase levels in allergic airway inflammation: A proteomics approach
    • Zhao, J., Zhu, H., Wong, C. H., Leung, K. Y. et al., Increased lungkine and chitinase levels in allergic airway inflammation: a proteomics approach. Proteomics 2005, 5, 2799-2807.
    • (2005) Proteomics , vol.5 , pp. 2799-2807
    • Zhao, J.1    Zhu, H.2    Wong, C.H.3    Leung, K.Y.4
  • 169
    • 8744262741 scopus 로고    scopus 로고
    • Proteome analysis of differential protein expression in allergen-induced asthmatic mice lung after dexamethasone treatment
    • Roh, G. S., Shin, Y., Seo, S. W., Yoon, B. R. et al., Proteome analysis of differential protein expression in allergen-induced asthmatic mice lung after dexamethasone treatment. Proteomics 2004, 4, 3318-3327.
    • (2004) Proteomics , vol.4 , pp. 3318-3327
    • Roh, G.S.1    Shin, Y.2    Seo, S.W.3    Yoon, B.R.4
  • 170
    • 0142246989 scopus 로고    scopus 로고
    • Lung proteome alterations in a mouse model for non-allergic asthma
    • Houtman, R., Krijgsveld, J., Kool, M., Romijn, E. P. et al., Lung proteome alterations in a mouse model for non-allergic asthma. Proteomics 2003, 3, 2008-2018.
    • (2003) Proteomics , vol.3 , pp. 2008-2018
    • Houtman, R.1    Krijgsveld, J.2    Kool, M.3    Romijn, E.P.4
  • 171
    • 34447099094 scopus 로고    scopus 로고
    • Alterations in cytoskeletal and immune function-related proteome profiles in whole rat lung following intratracheal instillation of heparin
    • Gabr, A. A., Reed, M., Newman, D. R., Pohl, J. et al., Alterations in cytoskeletal and immune function-related proteome profiles in whole rat lung following intratracheal instillation of heparin. Respir. Res. 2007, 8, 36.
    • (2007) Respir. Res , vol.8 , pp. 36
    • Gabr, A.A.1    Reed, M.2    Newman, D.R.3    Pohl, J.4
  • 172
    • 34247174019 scopus 로고    scopus 로고
    • Pulmonary biomarkers based on alterations in protein expression after exposure to arsenic
    • Lantz, R. C., Lynch, B. J., Boitano, S., Poplin, G. S. et al., Pulmonary biomarkers based on alterations in protein expression after exposure to arsenic. Environ. Health Perspect. 2007, 115, 586-591.
    • (2007) Environ. Health Perspect , vol.115 , pp. 586-591
    • Lantz, R.C.1    Lynch, B.J.2    Boitano, S.3    Poplin, G.S.4
  • 173
    • 23744512044 scopus 로고    scopus 로고
    • Effects of formaldehyde inhalation on lung of rats
    • Yang, Y. H., Xi, Z. G., Chao, F. H., Yang, D. F., Effects of formaldehyde inhalation on lung of rats. Biomed. Environ. Sci. 2005, 18, 164-168.
    • (2005) Biomed. Environ. Sci , vol.18 , pp. 164-168
    • Yang, Y.H.1    Xi, Z.G.2    Chao, F.H.3    Yang, D.F.4
  • 174
    • 20044368981 scopus 로고    scopus 로고
    • S100AB chemotactic protein is abundantly increased, but only a minor contributor to LPS-induced, steroid resistant neutrophilic lung inflammation in vivo
    • Bozinovski, S., Cross, M., Vlahos, R., Jones, J. E. et al., S100AB chemotactic protein is abundantly increased, but only a minor contributor to LPS-induced, steroid resistant neutrophilic lung inflammation in vivo. J. Proteome Res. 2005, 4, 136-145.
    • (2005) J. Proteome Res , vol.4 , pp. 136-145
    • Bozinovski, S.1    Cross, M.2    Vlahos, R.3    Jones, J.E.4


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