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Volumn 27, Issue 6, 2007, Pages 574-583

Use of Quantitative Mass Spectrometry Analysis in Kidney Research

Author keywords

2D LC MS MS; liquid chromatography; Mass spectrometry; protein interactions; quantitative analysis

Indexed keywords

BIOTIN; CALMODULIN; CHYMOTRYPSIN; GLUTATHIONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; STREPTAVIDIN; TRYPSIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 36549055070     PISSN: 02709295     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semnephrol.2007.09.008     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 33646537802 scopus 로고    scopus 로고
    • Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes
    • Fleischer T.C., Weaver C.M., McAfee K.J., et al. Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev 20 (2006) 1294-1307
    • (2006) Genes Dev , vol.20 , pp. 1294-1307
    • Fleischer, T.C.1    Weaver, C.M.2    McAfee, K.J.3
  • 2
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link A.J., Eng J., Schieltz D.M., et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol 17 (1999) 676-682
    • (1999) Nat Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3
  • 3
    • 3543005925 scopus 로고    scopus 로고
    • Cluster analysis of mass spectrometry data reveals a novel component of SAGA
    • Powell D.W., Weaver C.M., Jennings J.L., et al. Cluster analysis of mass spectrometry data reveals a novel component of SAGA. Mol Cell Biol 24 (2004) 7249-7259
    • (2004) Mol Cell Biol , vol.24 , pp. 7249-7259
    • Powell, D.W.1    Weaver, C.M.2    Jennings, J.L.3
  • 4
    • 33745554756 scopus 로고    scopus 로고
    • Discovery of regulatory molecular events and biomarkers using 2D capillary chromatography and mass spectrometry
    • Powell D.W., Merchant M.L., and Link A.J. Discovery of regulatory molecular events and biomarkers using 2D capillary chromatography and mass spectrometry. Expert Rev Proteomics 3 (2006) 63-74
    • (2006) Expert Rev Proteomics , vol.3 , pp. 63-74
    • Powell, D.W.1    Merchant, M.L.2    Link, A.J.3
  • 5
  • 7
    • 33747170146 scopus 로고    scopus 로고
    • Using annotated peptide mass spectrum libraries for protein identification
    • Craig R., Cortens J.C., Fenyo D., et al. Using annotated peptide mass spectrum libraries for protein identification. J Proteome Res 5 (2006) 1843-1849
    • (2006) J Proteome Res , vol.5 , pp. 1843-1849
    • Craig, R.1    Cortens, J.C.2    Fenyo, D.3
  • 8
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • Listgarten J., and Emili A. Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 4 (2005) 419-434
    • (2005) Mol Cell Proteomics , vol.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 9
    • 33748312246 scopus 로고    scopus 로고
    • Analyzing proteomes and protein function using graphical comparative analysis of tandem mass spectrometry results
    • McAfee K.J., Duncan D.T., Assink M., et al. Analyzing proteomes and protein function using graphical comparative analysis of tandem mass spectrometry results. Mol Cell Proteomics 5 (2006) 1497-1513
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1497-1513
    • McAfee, K.J.1    Duncan, D.T.2    Assink, M.3
  • 10
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., et al. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75 (2003) 4646-4658
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3
  • 11
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1 (2002) 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 12
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17 (1999) 994-999
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3
  • 13
    • 6044226889 scopus 로고    scopus 로고
    • Differential mass spectrometry: a label-free LC-MS method for finding significant differences in complex peptide and protein mixtures
    • Wiener M.C., Sachs J.R., Deyanova E.G., et al. Differential mass spectrometry: a label-free LC-MS method for finding significant differences in complex peptide and protein mixtures. Anal Chem 76 (2004) 6085-6096
    • (2004) Anal Chem , vol.76 , pp. 6085-6096
    • Wiener, M.C.1    Sachs, J.R.2    Deyanova, E.G.3
  • 14
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old W.M., Meyer-Arendt K., Aveline-Wolf L., et al. Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol Cell Proteomics 4 (2005) 1487-1502
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1    Meyer-Arendt, K.2    Aveline-Wolf, L.3
  • 15
    • 33846129045 scopus 로고    scopus 로고
    • Stable isotope-free quantitative shotgun proteomics combined with sample pattern recognition for rapid diagnostics
    • Wienkoop S., Larrainzar E., Niemann M., et al. Stable isotope-free quantitative shotgun proteomics combined with sample pattern recognition for rapid diagnostics. J Sep Sci 29 (2006) 2793-2801
    • (2006) J Sep Sci , vol.29 , pp. 2793-2801
    • Wienkoop, S.1    Larrainzar, E.2    Niemann, M.3
  • 16
    • 14344250874 scopus 로고    scopus 로고
    • Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry
    • Radulovic D., Jelveh S., Ryu S., et al. Informatics platform for global proteomic profiling and biomarker discovery using liquid chromatography-tandem mass spectrometry. Mol Cell Proteomics 3 (2004) 984-997
    • (2004) Mol Cell Proteomics , vol.3 , pp. 984-997
    • Radulovic, D.1    Jelveh, S.2    Ryu, S.3
  • 17
    • 30744438115 scopus 로고    scopus 로고
    • Computational Proteomics Analysis System (CPAS): an extensible, open-source analytic system for evaluating and publishing proteomic data and high throughput biological experiments
    • Rauch A., Bellew M., Eng J., et al. Computational Proteomics Analysis System (CPAS): an extensible, open-source analytic system for evaluating and publishing proteomic data and high throughput biological experiments. J Proteome Res 5 (2006) 112-121
    • (2006) J Proteome Res , vol.5 , pp. 112-121
    • Rauch, A.1    Bellew, M.2    Eng, J.3
  • 18
    • 12144289400 scopus 로고    scopus 로고
    • A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway
    • Bouwmeester T., Bauch A., Ruffner H., et al. A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat Cell Biol 6 (2004) 97-105
    • (2004) Nat Cell Biol , vol.6 , pp. 97-105
    • Bouwmeester, T.1    Bauch, A.2    Ruffner, H.3
  • 19
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., Bosche M., Krause R., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3
  • 20
    • 0036269973 scopus 로고    scopus 로고
    • Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
    • Sanders S.L., Jennings J., Canutescu A., et al. Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry. Mol Cell Biol 22 (2002) 4723-4738
    • (2002) Mol Cell Biol , vol.22 , pp. 4723-4738
    • Sanders, S.L.1    Jennings, J.2    Canutescu, A.3
  • 21
    • 34147217542 scopus 로고    scopus 로고
    • Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
    • Collins S.R., Miller K.M., Maas N.L., et al. Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446 (2007) 806-810
    • (2007) Nature , vol.446 , pp. 806-810
    • Collins, S.R.1    Miller, K.M.2    Maas, N.L.3
  • 22
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G., Peregrin-Alvarez J.M., Li J., et al. Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 (2005) 531-537
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3
  • 23
    • 33947182552 scopus 로고    scopus 로고
    • An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
    • Rinner O., Mueller L.N., Hubalek M., et al. An integrated mass spectrometric and computational framework for the analysis of protein interaction networks. Nat Biotechnol 25 (2007) 345-352
    • (2007) Nat Biotechnol , vol.25 , pp. 345-352
    • Rinner, O.1    Mueller, L.N.2    Hubalek, M.3
  • 24
    • 33646473345 scopus 로고    scopus 로고
    • A mammalian organelle map by protein correlation profiling
    • Foster L.J., de Hoog C.L., Zhang Y., et al. A mammalian organelle map by protein correlation profiling. Cell 125 (2006) 187-199
    • (2006) Cell , vol.125 , pp. 187-199
    • Foster, L.J.1    de Hoog, C.L.2    Zhang, Y.3
  • 25
    • 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., et al. Global survey of organ and organelle protein expression in mouse: combined proteomic and transcriptomic profiling. Cell 125 (2006) 173-186
    • (2006) Cell , vol.125 , pp. 173-186
    • Kislinger, T.1    Cox, B.2    Kannan, A.3
  • 26
    • 0033949446 scopus 로고    scopus 로고
    • Cellular and molecular mediators in common pathway mechanisms of chronic renal disease progression
    • Taal M.W., Omer S.A., Nadim M.K., et al. Cellular and molecular mediators in common pathway mechanisms of chronic renal disease progression. Curr Opin Nephrol Hypertens 9 (2000) 323-331
    • (2000) Curr Opin Nephrol Hypertens , vol.9 , pp. 323-331
    • Taal, M.W.1    Omer, S.A.2    Nadim, M.K.3
  • 27
    • 12844277462 scopus 로고    scopus 로고
    • The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex
    • Lee K.K., Florens L., Swanson S.K., et al. The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex. Mol Cell Biol 25 (2005) 1173-1182
    • (2005) Mol Cell Biol , vol.25 , pp. 1173-1182
    • Lee, K.K.1    Florens, L.2    Swanson, S.K.3
  • 28
    • 0029053727 scopus 로고
    • Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE
    • Clauser K.R., Hall S.C., Smith D.M., et al. Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE. Proc Natl Acad Sci U S A 92 (1995) 5072-5076
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5072-5076
    • Clauser, K.R.1    Hall, S.C.2    Smith, D.M.3
  • 29
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with tandem mass spectra
    • Craig R., and Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 20 (2004) 1466-1467
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 30
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates III J.R., Eng J.K., McCormack A.L., et al. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem 67 (1995) 1426-1436
    • (1995) Anal Chem , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3
  • 31
    • 0029645432 scopus 로고
    • Mining genomes: correlating tandem mass spectra of modified and unmodified peptides to sequences in nucleotide databases
    • Yates III J.R., Eng J.K., and McCormack A.L. Mining genomes: correlating tandem mass spectra of modified and unmodified peptides to sequences in nucleotide databases. Anal Chem 67 (1995) 3202-3210
    • (1995) Anal Chem , vol.67 , pp. 3202-3210
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3
  • 32
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., et al. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3
  • 33
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han D.K., Eng J., Zhou H., et al. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol 19 (2001) 946-951
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3
  • 34
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb D.L., McDonald W.H., and Yates III J.R. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1 (2002) 21-26
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 35
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., and Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4 (2007) 207-214
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 36
    • 20844457100 scopus 로고    scopus 로고
    • Integrated approach for manual evaluation of peptides identified by searching protein sequence databases with tandem mass spectra
    • Chen Y., Kwon S.W., Kim S.C., et al. Integrated approach for manual evaluation of peptides identified by searching protein sequence databases with tandem mass spectra. J Proteome Res 4 (2005) 998-1005
    • (2005) J Proteome Res , vol.4 , pp. 998-1005
    • Chen, Y.1    Kwon, S.W.2    Kim, S.C.3
  • 37
    • 0034652301 scopus 로고    scopus 로고
    • Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry
    • Gatlin C.L., Eng J.K., Cross S.T., et al. Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry. Anal Chem 72 (2000) 757-763
    • (2000) Anal Chem , vol.72 , pp. 757-763
    • Gatlin, C.L.1    Eng, J.K.2    Cross, S.T.3
  • 38
    • 33646590920 scopus 로고    scopus 로고
    • Differential protein expression profiling by iTRAQ-2DLC-MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype
    • Keshamouni V.G., Michailidis G., Grasso C.S., et al. Differential protein expression profiling by iTRAQ-2DLC-MS/MS of lung cancer cells undergoing epithelial-mesenchymal transition reveals a migratory/invasive phenotype. J Proteome Res 5 (2006) 1143-1154
    • (2006) J Proteome Res , vol.5 , pp. 1143-1154
    • Keshamouni, V.G.1    Michailidis, G.2    Grasso, C.S.3
  • 39
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., and Yates III J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76 (2004) 4193-4201
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 40
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3 (2004) 1154-1169
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3
  • 41
    • 20944444686 scopus 로고    scopus 로고
    • Increased quantitative proteome coverage with (13)C/(12)C-based, acid-cleavable isotope-coded affinity tag reagent and modified data acquisition scheme
    • Yi E.C., Li X.J., Cooke K., et al. Increased quantitative proteome coverage with (13)C/(12)C-based, acid-cleavable isotope-coded affinity tag reagent and modified data acquisition scheme. Proteomics 5 (2005) 380-387
    • (2005) Proteomics , vol.5 , pp. 380-387
    • Yi, E.C.1    Li, X.J.2    Cooke, K.3
  • 42
    • 23044504789 scopus 로고    scopus 로고
    • Gao J, Friedrichs MS, Dongre AR, et al. Guidelines for the routine application of the peptide hits technique. J Am Soc Mass Spectrom. 205;16:1231-8.
  • 43
    • 0348142993 scopus 로고    scopus 로고
    • Changes in the protein expression of yeast as a function of carbon source
    • Gao J., Opiteck G.J., Friedrichs M.S., et al. Changes in the protein expression of yeast as a function of carbon source. J Proteome Res 2 (2003) 643-649
    • (2003) J Proteome Res , vol.2 , pp. 643-649
    • Gao, J.1    Opiteck, G.J.2    Friedrichs, M.S.3
  • 44
    • 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., et al. Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal Chem 75 (2003) 4818-4826
    • (2003) Anal Chem , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3
  • 45
    • 33846635481 scopus 로고    scopus 로고
    • Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes
    • Hughes A.L., Powell D.W., Bard M., et al. Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes. Cell Metab 5 (2007) 143-149
    • (2007) Cell Metab , vol.5 , pp. 143-149
    • Hughes, A.L.1    Powell, D.W.2    Bard, M.3
  • 46
    • 0037008764 scopus 로고    scopus 로고
    • Transforming growth factor-beta 2 is a transcriptional target for Akt/protein kinase B via forkhead transcription factor
    • Samatar A.A., Wang L., Mirza A., et al. Transforming growth factor-beta 2 is a transcriptional target for Akt/protein kinase B via forkhead transcription factor. J Biol Chem 277 (2002) 28118-28126
    • (2002) J Biol Chem , vol.277 , pp. 28118-28126
    • Samatar, A.A.1    Wang, L.2    Mirza, A.3
  • 47
    • 4444251034 scopus 로고    scopus 로고
    • Angiotensin II regulation of TGF-beta in murine mesangial cells involves both PI3 kinase and MAP kinase
    • Perlman A., Lawsin L.M., Kolachana P., et al. Angiotensin II regulation of TGF-beta in murine mesangial cells involves both PI3 kinase and MAP kinase. Ann Clin Lab Sci 34 (2004) 277-286
    • (2004) Ann Clin Lab Sci , vol.34 , pp. 277-286
    • Perlman, A.1    Lawsin, L.M.2    Kolachana, P.3
  • 48
    • 0036786834 scopus 로고    scopus 로고
    • TGF-beta signaling in renal disease
    • Bottinger E.P., and Bitzer M. TGF-beta signaling in renal disease. J Am Soc Nephrol 13 (2002) 2600-2610
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2600-2610
    • Bottinger, E.P.1    Bitzer, M.2
  • 49
    • 33749523582 scopus 로고    scopus 로고
    • Organellar proteomics: turning inventories into insights
    • Andersen J.S., and Mann M. Organellar proteomics: turning inventories into insights. EMBO Rep 7 (2006) 874-879
    • (2006) EMBO Rep , vol.7 , pp. 874-879
    • Andersen, J.S.1    Mann, M.2
  • 50
    • 33751413316 scopus 로고    scopus 로고
    • LC-MS/MS analysis of apical and basolateral plasma membranes of rat renal collecting duct cells
    • Yu M.J., Pisitkun T., Wang G., et al. LC-MS/MS analysis of apical and basolateral plasma membranes of rat renal collecting duct cells. Mol Cell Proteomics 5 (2006) 2131-2145
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2131-2145
    • Yu, M.J.1    Pisitkun, T.2    Wang, G.3
  • 51
    • 0032731318 scopus 로고    scopus 로고
    • The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury?
    • Gilbert R.E., and Cooper M.E. The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury?. Kidney Int 56 (1999) 1627-1637
    • (1999) Kidney Int , vol.56 , pp. 1627-1637
    • Gilbert, R.E.1    Cooper, M.E.2
  • 52
    • 33644638349 scopus 로고    scopus 로고
    • Renal fibrosis: new insights into the pathogenesis and therapeutics
    • Liu Y. Renal fibrosis: new insights into the pathogenesis and therapeutics. Kidney Int 69 (2006) 213-217
    • (2006) Kidney Int , vol.69 , pp. 213-217
    • Liu, Y.1
  • 53
    • 0347993932 scopus 로고    scopus 로고
    • Epithelial to mesenchymal transition in renal fibrogenesis: pathologic significance, molecular mechanism, and therapeutic intervention
    • Liu Y. Epithelial to mesenchymal transition in renal fibrogenesis: pathologic significance, molecular mechanism, and therapeutic intervention. J Am Soc Nephrol 15 (2004) 1-12
    • (2004) J Am Soc Nephrol , vol.15 , pp. 1-12
    • Liu, Y.1
  • 54
    • 0036318317 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition of tubular epithelial cells in human renal biopsies
    • Rastaldi M.P., Ferrario F., Giardino L., et al. Epithelial-mesenchymal transition of tubular epithelial cells in human renal biopsies. Kidney Int 62 (2002) 137-146
    • (2002) Kidney Int , vol.62 , pp. 137-146
    • Rastaldi, M.P.1    Ferrario, F.2    Giardino, L.3
  • 55
    • 34247533369 scopus 로고    scopus 로고
    • Phenotypic transitions and fibrosis in diabetic nephropathy
    • Simonson M.S. Phenotypic transitions and fibrosis in diabetic nephropathy. Kidney Int 71 (2007) 846-854
    • (2007) Kidney Int , vol.71 , pp. 846-854
    • Simonson, M.S.1
  • 56
    • 0034785496 scopus 로고    scopus 로고
    • Dissection of key events in tubular epithelial to myofibroblast transition and its implications in renal interstitial fibrosis
    • Yang J., and Liu Y. Dissection of key events in tubular epithelial to myofibroblast transition and its implications in renal interstitial fibrosis. Am J Pathol 159 (2001) 1465-1475
    • (2001) Am J Pathol , vol.159 , pp. 1465-1475
    • Yang, J.1    Liu, Y.2
  • 57
    • 0346724511 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition and its implications for fibrosis
    • Kalluri R., and Neilson E.G. Epithelial-mesenchymal transition and its implications for fibrosis. J Clin Invest 112 (2003) 1776-1784
    • (2003) J Clin Invest , vol.112 , pp. 1776-1784
    • Kalluri, R.1    Neilson, E.G.2
  • 58
    • 0037229290 scopus 로고    scopus 로고
    • Tubular epithelial-myofibroblast transdifferentiation mechanisms in proximal tubule cells
    • Lan H.Y. Tubular epithelial-myofibroblast transdifferentiation mechanisms in proximal tubule cells. Curr Opin Nephrol Hypertens 12 (2003) 25-29
    • (2003) Curr Opin Nephrol Hypertens , vol.12 , pp. 25-29
    • Lan, H.Y.1
  • 59
    • 24644487312 scopus 로고    scopus 로고
    • TGF-beta and epithelial-to-mesenchymal transitions
    • Zavadil J., and Bottinger E.P. TGF-beta and epithelial-to-mesenchymal transitions. Oncogene 24 (2005) 5764-5774
    • (2005) Oncogene , vol.24 , pp. 5764-5774
    • Zavadil, J.1    Bottinger, E.P.2
  • 60
    • 9444262472 scopus 로고    scopus 로고
    • Development of late-stage diabetic nephropathy in OVE26 diabetic mice
    • Zheng S., Noonan W.T., Metreveli N.S., et al. Development of late-stage diabetic nephropathy in OVE26 diabetic mice. Diabetes 53 (2004) 3248-3257
    • (2004) Diabetes , vol.53 , pp. 3248-3257
    • Zheng, S.1    Noonan, W.T.2    Metreveli, N.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.