메뉴 건너뛰기




Volumn 2, Issue 7-8, 2008, Pages 1153-1166

Identification of phosphoproteins in kidney tissues from patients with autosomal dominant polycystic kidney disease

Author keywords

2 DE; Autosomal dominant polycystic kidney disease; Phosphorylation

Indexed keywords

ANTIOXIDANT; CHAPERONE; CYTOSKELETON PROTEIN; LIPOCORTIN 2; MITOCHONDRIAL ENZYME; PHOSPHOPROTEIN; TRANSCRIPTION FACTOR; TROPOMYOSIN;

EID: 50849120066     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780172     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 0347357836 scopus 로고    scopus 로고
    • Polycystic kidney disease
    • Wilson, P. D., Polycystic kidney disease. N. Engl. J. Med. 2004, 350, 151-164.
    • (2004) N. Engl. J. Med , vol.350 , pp. 151-164
    • Wilson, P.D.1
  • 2
    • 0028278058 scopus 로고
    • The polycystic kidney disease 1 gene encodes a 14kb transcript and lies within a duplicated region on chromosme 16
    • The European Polycystic Kidney Disease Consortium
    • The European Polycystic Kidney Disease Consortium, The polycystic kidney disease 1 gene encodes a 14kb transcript and lies within a duplicated region on chromosme 16. Cell 1994, 77, 881-894.
    • (1994) Cell , vol.77 , pp. 881-894
  • 3
    • 0028942745 scopus 로고
    • Analysis of the genomic sequence for the autosomal dominant polycystic kidney disease gene (PKD1) predicts the presence of a leucine-rich repeat
    • The American PKD1 Consortium
    • The American PKD1 Consortium. Analysis of the genomic sequence for the autosomal dominant polycystic kidney disease gene (PKD1) predicts the presence of a leucine-rich repeat. Hum. Mol. Genet. 1995, 4, 575-582.
    • (1995) Hum. Mol. Genet , vol.4 , pp. 575-582
  • 4
    • 0029002967 scopus 로고
    • Polycystic kidney disease: The complete structure of the PKD1 gene and its protein
    • The International Polycystic Kidney Disease Consortium
    • The International Polycystic Kidney Disease Consortium, Polycystic kidney disease: the complete structure of the PKD1 gene and its protein. Cell 1995, 81, 289-298.
    • (1995) Cell , vol.81 , pp. 289-298
  • 5
    • 15844385078 scopus 로고    scopus 로고
    • PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein
    • Mochizuki, T., Wu, G., Hayashi, T., Xenophontos, S. L. et al., PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein. Science 1996, 272, 1339-1342.
    • (1996) Science , vol.272 , pp. 1339-1342
    • Mochizuki, T.1    Wu, G.2    Hayashi, T.3    Xenophontos, S.L.4
  • 6
    • 1542283793 scopus 로고    scopus 로고
    • A polycystin-1 multiprotein complex is disrupted in polycystic kidney disease cells
    • Roitbak, T., Ward, C. J., Harris, P. C., Bacallao, R., A polycystin-1 multiprotein complex is disrupted in polycystic kidney disease cells. Mol. Biol. Cell 2004, 15, 1334-1346.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1334-1346
    • Roitbak, T.1    Ward, C.J.2    Harris, P.C.3    Bacallao, R.4
  • 7
    • 0033532582 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in the PKD1-encoded protein C-terminal domain
    • Li, H. P., Geng, L., Burrow, C. R., Wilson, P. D., Identification of phosphorylation sites in the PKD1-encoded protein C-terminal domain. Biochem. Biophys. Res. Commun. 1999, 259, 356-363.
    • (1999) Biochem. Biophys. Res. Commun , vol.259 , pp. 356-363
    • Li, H.P.1    Geng, L.2    Burrow, C.R.3    Wilson, P.D.4
  • 8
    • 39149102488 scopus 로고    scopus 로고
    • Protein kinase X (PRKX) can rescue the effects of polycystic kidney disease-1 gene (PKD1) deficiency
    • Li, X., Burrow, C. R., Polgar, K., Hyink, D. P. et al., Protein kinase X (PRKX) can rescue the effects of polycystic kidney disease-1 gene (PKD1) deficiency. Biochim. Biophys. Acta 2008, 1782, 1-9.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 1-9
    • Li, X.1    Burrow, C.R.2    Polgar, K.3    Hyink, D.P.4
  • 9
    • 2442605494 scopus 로고    scopus 로고
    • Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812
    • Cai, Y., Anyatonwu, G., Okuhara, D., Lee, K. B. et al., Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812. J. Biol. Chem. 2004, 279, 19987-19995.
    • (2004) J. Biol. Chem , vol.279 , pp. 19987-19995
    • Cai, Y.1    Anyatonwu, G.2    Okuhara, D.3    Lee, K.B.4
  • 10
    • 0344527449 scopus 로고    scopus 로고
    • Functional activity of epidermal growth factor receptors in autosomal recessive polycystic kidney disease
    • Sweeney, W. E., Jr., Avner, E. D., Functional activity of epidermal growth factor receptors in autosomal recessive polycystic kidney disease. Am. J. Physiol. 1998, 275, F387-394.
    • (1998) Am. J. Physiol , vol.275
    • Sweeney Jr., W.E.1    Avner, E.D.2
  • 11
    • 0037249699 scopus 로고    scopus 로고
    • Renal activation of extracellular signal-regulated kinase in rats with autosomal-dominant polycystic kidney disease
    • Nagao, S., Yamaguchi, T., Kusaka, M., Maser, R. L. et al., Renal activation of extracellular signal-regulated kinase in rats with autosomal-dominant polycystic kidney disease. Kidney Int. 2003, 63, 427-437.
    • (2003) Kidney Int , vol.63 , pp. 427-437
    • Nagao, S.1    Yamaguchi, T.2    Kusaka, M.3    Maser, R.L.4
  • 12
    • 0037513435 scopus 로고    scopus 로고
    • Cyclic AMP activates B-Raf and ERK in cyst epithelial cells from autosamal-dominant polycystic kidneys
    • Yamaguchi, T., Nagao, S., Wallace, D. P., Belibi, F. A. et al., Cyclic AMP activates B-Raf and ERK in cyst epithelial cells from autosamal-dominant polycystic kidneys. Kidney Int 2003, 63, 1983-1994.
    • (2003) Kidney Int , vol.63 , pp. 1983-1994
    • Yamaguchi, T.1    Nagao, S.2    Wallace, D.P.3    Belibi, F.A.4
  • 13
    • 4644367485 scopus 로고    scopus 로고
    • Calcium restriction allows cAMP activation of the B-Raf/ERK pathway, switching cells to a cAMP-dependent growth-stimulated phenotype
    • Yamaguchi, T., Wallace, D. P., Magenheimer, B. S., Hempson, S. J. et al., Calcium restriction allows cAMP activation of the B-Raf/ERK pathway, switching cells to a cAMP-dependent growth-stimulated phenotype. J. Biol. Chem. 2004, 279, 40419-40430.
    • (2004) J. Biol. Chem , vol.279 , pp. 40419-40430
    • Yamaguchi, T.1    Wallace, D.P.2    Magenheimer, B.S.3    Hempson, S.J.4
  • 14
    • 34447566918 scopus 로고    scopus 로고
    • Mitotic activation of Akt signalling pathway in Han:SPRD rats with polycystic kidney disease
    • Wahl, P. R., Le, Hir, M., Vogetseder, A., Arcaro, A. et al., Mitotic activation of Akt signalling pathway in Han:SPRD rats with polycystic kidney disease. Nephrology 2007, 12, 357-363.
    • (2007) Nephrology , vol.12 , pp. 357-363
    • Wahl, P.1    Le, R.2    Hir, M.3    Vogetseder, A.4    Arcaro, A.5
  • 15
    • 33645458872 scopus 로고    scopus 로고
    • Polycystin-1 induces resistance to apoptosis through the phosphatidylinositol 3-kinase/Akt signaling pathway
    • Boca, M., Distefano, G., Qian, F., Bhunia, A. K. et al., Polycystin-1 induces resistance to apoptosis through the phosphatidylinositol 3-kinase/Akt signaling pathway. J. Am. Soc. Nephrol. 2006, 17, 637-647.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 637-647
    • Boca, M.1    Distefano, G.2    Qian, F.3    Bhunia, A.K.4
  • 16
    • 42649142332 scopus 로고    scopus 로고
    • Combined enzymatic and data mining approaches for comprehensive phosphoproteome analyses; application to cell signaling events of interferon-stimulated macrophages
    • Marcantonio, M., Trost, M., Courcelles, M., Desjardins, M. et al., Combined enzymatic and data mining approaches for comprehensive phosphoproteome analyses; application to cell signaling events of interferon-stimulated macrophages. Mol. Cell. Proteomics 2008, 7, 645-660.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 645-660
    • Marcantonio, M.1    Trost, M.2    Courcelles, M.3    Desjardins, M.4
  • 17
    • 3042818018 scopus 로고    scopus 로고
    • An integrated database for proteomics experiments
    • The International Protein Index
    • Kersey, P. J., Duarte, J., Williams, A., Karavidopoulou, Y. et al., The International Protein Index: An integrated database for proteomics experiments. Proteomics 2004, 4, 1985-1988.
    • (2004) Proteomics , vol.4 , pp. 1985-1988
    • Kersey, P.J.1    Duarte, J.2    Williams, A.3    Karavidopoulou, Y.4
  • 18
    • 0000857494 scopus 로고
    • Correlating tandem mass spectral data of peptides to sequences in protein database
    • Eng, J. K., Mecommck, A. L., Yates, J. R., Correlating tandem mass spectral data of peptides to sequences in protein database. J. Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    Mecommck, A.L.2    Yates, J.R.3
  • 19
    • 0035106351 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 20
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders, J., Sickmann, A., State-of-the-art in phosphoproteomics. Proteomics 2005, 5, 4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 21
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Grønborg, M., Steen., H. et al., Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 2002, 20, 261-268.
    • (2002) Trends Biotechnol , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Grønborg, M.3    Steen, H.4
  • 22
    • 0030200912 scopus 로고    scopus 로고
    • Coupling of MALDI-TOF mass analysis to the separation of biotinylated peptides by magnetic streptavidin beads
    • Girault, S., Chassaing, G., Blais, J. C., Brunot, A., Bolbach, G., Coupling of MALDI-TOF mass analysis to the separation of biotinylated peptides by magnetic streptavidin beads. Anal. Chem. 1996, 68, 2122-2126.
    • (1996) Anal. Chem , vol.68 , pp. 2122-2126
    • Girault, S.1    Chassaing, G.2    Blais, J.C.3    Brunot, A.4    Bolbach, G.5
  • 23
    • 0034868043 scopus 로고    scopus 로고
    • Selective analysis of phosphopeptides within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry
    • Adamczyk, M., Gebler, J. C., Wu, J., Selective analysis of phosphopeptides within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry. Rapid Commun. Mass Spectrom. 2001, 15, 1481-1488.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 1481-1488
    • Adamczyk, M.1    Gebler, J.C.2    Wu, J.3
  • 24
    • 0042861519 scopus 로고    scopus 로고
    • Phosphospecific proteolysis for mapping sites of protein phosphorylation
    • Knight, Z. A., Schilling, B., Row, R. H., Kenski, D. M. et al., Phosphospecific proteolysis for mapping sites of protein phosphorylation. Nat. Biotechnol. 2003, 21, 1047-1054.
    • (2003) Nat. Biotechnol , vol.21 , pp. 1047-1054
    • Knight, Z.A.1    Schilling, B.2    Row, R.H.3    Kenski, D.M.4
  • 25
    • 33745656830 scopus 로고    scopus 로고
    • Comparative proteomics analysis of differentially expressed phosphoproteins in adult rat ventricular myocytes subjected to diazoxide preconditioning
    • Li, H., Xiao, Y. B., Gao, Y. Q., Yang, T. D., Comparative proteomics analysis of differentially expressed phosphoproteins in adult rat ventricular myocytes subjected to diazoxide preconditioning. Drug Metab. Drug Interact. 2006, 21, 245-58.
    • (2006) Drug Metab. Drug Interact , vol.21 , pp. 245-258
    • Li, H.1    Xiao, Y.B.2    Gao, Y.Q.3    Yang, T.D.4
  • 26
    • 33645472678 scopus 로고    scopus 로고
    • Identification of novel phosphoproteins in signaling pathways triggered by latent membrane protein 1 using functional proteomics technology
    • Yan, G., Li, L., Tao, Y., Liu, S. et al., Identification of novel phosphoproteins in signaling pathways triggered by latent membrane protein 1 using functional proteomics technology. Proteomics 2006, 6, 1810-1821.
    • (2006) Proteomics , vol.6 , pp. 1810-1821
    • Yan, G.1    Li, L.2    Tao, Y.3    Liu, S.4
  • 27
    • 33747886382 scopus 로고    scopus 로고
    • Towards the identification of late-embryogenic abundant phosphoproteome in Arabidopsis by 2-DE and MS
    • Sami, I., Eliandre, O., Montserrat, P., Adela, G., Towards the identification of late-embryogenic abundant phosphoproteome in Arabidopsis by 2-DE and MS. Proteomics 2006, 6, S175-S185.
    • (2006) Proteomics , vol.6
    • Sami, I.1    Eliandre, O.2    Montserrat, P.3    Adela, G.4
  • 28
    • 34547863477 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of neuronal cell death by glutamate-induced oxidative stress
    • Kang, T. H., Bae, K. H., Yu, M. J., Kim, W. K. et al., Phosphoproteomic analysis of neuronal cell death by glutamate-induced oxidative stress. Proteomics 2007, 7, 2624-2635.
    • (2007) Proteomics , vol.7 , pp. 2624-2635
    • Kang, T.H.1    Bae, K.H.2    Yu, M.J.3    Kim, W.K.4
  • 29
    • 4444334954 scopus 로고    scopus 로고
    • Comparative analysis of phosphoprotein-enriched myocyte proteomes reveals widespread alterations during differentiation
    • Puente, L. G., Carrière, J. F., Kelly, J. F., Megeney, L. A., Comparative analysis of phosphoprotein-enriched myocyte proteomes reveals widespread alterations during differentiation. FEBS Lett. 2004, 574, 138-144
    • (2004) FEBS Lett , vol.574 , pp. 138-144
    • Puente, L.G.1    Carrière, J.F.2    Kelly, J.F.3    Megeney, L.A.4
  • 30
    • 2442471739 scopus 로고    scopus 로고
    • Differential phosphoproteome profiling by affinity capture and tandem matrix-assisted laser desorption/ionization mass spectrometry
    • Metodiev, M. V., Timanova, A., Stone, D. E., Differential phosphoproteome profiling by affinity capture and tandem matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 2004, 4, 1433-1438.
    • (2004) Proteomics , vol.4 , pp. 1433-1438
    • Metodiev, M.V.1    Timanova, A.2    Stone, D.E.3
  • 31
    • 17644361916 scopus 로고    scopus 로고
    • Rapid enrichment and analysis of yeast phosphoproteins using affinity chromatography, 2D-PAGE and peptide mass fingerprinting
    • Makrantoni, V., Antrobus, R., Botting, C. H., Coote, P. J., Rapid enrichment and analysis of yeast phosphoproteins using affinity chromatography, 2D-PAGE and peptide mass fingerprinting. Yeast 2005, 22, 401-414.
    • (2005) Yeast , vol.22 , pp. 401-414
    • Makrantoni, V.1    Antrobus, R.2    Botting, C.H.3    Coote, P.J.4
  • 33
    • 0028244667 scopus 로고
    • Characterization of the Han:SPRD rat model for hereditary polycystic kidney disease
    • Schäfer, K., Gretz, N., Bader, M., Oberbäumer, I. et al., Characterization of the Han:SPRD rat model for hereditary polycystic kidney disease. Kidney Int. 1994, 46, 134-152.
    • (1994) Kidney Int , vol.46 , pp. 134-152
    • Schäfer, K.1    Gretz, N.2    Bader, M.3    Oberbäumer, I.4
  • 34
    • 0028846248 scopus 로고
    • Modulation of annexin II tetramer by tyrosine phosphorylation
    • Hubaishy, I., Jones, P. G., Bjorge, J., Bellagamba, C. et al., Modulation of annexin II tetramer by tyrosine phosphorylation. Biochemistry 1995, 34, 14527-14534.
    • (1995) Biochemistry , vol.34 , pp. 14527-14534
    • Hubaishy, I.1    Jones, P.G.2    Bjorge, J.3    Bellagamba, C.4
  • 35
    • 0032846088 scopus 로고    scopus 로고
    • Specific dawn-regulation of annexin II expression in human cells interferes with cell proliferation
    • Chiang, Y., Rizzino, A., Sibenaller, Z. A., Wold, M. S., Vishwanatha, J. K., Specific dawn-regulation of annexin II expression in human cells interferes with cell proliferation. Mol. Cell. Biochem. 1999, 199, 139-147.
    • (1999) Mol. Cell. Biochem , vol.199 , pp. 139-147
    • Chiang, Y.1    Rizzino, A.2    Sibenaller, Z.A.3    Wold, M.S.4    Vishwanatha, J.K.5
  • 36
    • 0025766346 scopus 로고
    • Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet derived growth factor
    • Brambilla, R., Zippel, R., Sturani, E., Morello, L. et al., Characterization of the tyrosine phosphorylation of calpactin I (annexin II) induced by platelet derived growth factor. Biochem. J. 1991, 278, 447-452.
    • (1991) Biochem. J , vol.278 , pp. 447-452
    • Brambilla, R.1    Zippel, R.2    Sturani, E.3    Morello, L.4
  • 37
    • 0345304730 scopus 로고    scopus 로고
    • Molecular genetics of autosomal dominant polycystic kidney disease
    • Pei, Y., Molecular genetics of autosomal dominant polycystic kidney disease. Clin. Invest. Med. 2003, 26, 252-258.
    • (2003) Clin. Invest. Med , vol.26 , pp. 252-258
    • Pei, Y.1
  • 38
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase dependent regulation of glycogen synthase kinase 3 and protein kinaseB/AKT by the integrin-linked kinase
    • Delcommenne, M., Tan, C., Gray, V., Rue, L. et al., Phosphoinositide-3-OH kinase dependent regulation of glycogen synthase kinase 3 and protein kinaseB/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA 1998, 95, 11211-11216.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4
  • 39
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad, S., Attwell, S., Gray, V., Mawji, N. et al., Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 2001, 276, 27462-27469.
    • (2001) J. Biol. Chem , vol.276 , pp. 27462-27469
    • Persad, S.1    Attwell, S.2    Gray, V.3    Mawji, N.4
  • 40
    • 1642587815 scopus 로고    scopus 로고
    • Regulation of E-cadherin expression and beta-catenin/Tcf transcriptional activity by the integrin-linked kinase
    • Oloumi, A., McPhee, T., Dedhar, S., Regulation of E-cadherin expression and beta-catenin/Tcf transcriptional activity by the integrin-linked kinase. Biochim. Biophys. Acta 2004, 1691, 1-15.
    • (2004) Biochim. Biophys. Acta , vol.1691 , pp. 1-15
    • Oloumi, A.1    McPhee, T.2    Dedhar, S.3
  • 41
    • 0032831465 scopus 로고    scopus 로고
    • The PKD1 gene product, polycystin-1, is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia
    • Wilson, P. D., Geng, L., Li, X., Burrow, C. R., The PKD1 gene product, "polycystin-1, is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia. Lab. Invest. 1999, 79, 1311-1323.
    • (1999) Lab. Invest , vol.79 , pp. 1311-1323
    • Wilson, P.D.1    Geng, L.2    Li, X.3    Burrow, C.R.4
  • 42
    • 0033401358 scopus 로고    scopus 로고
    • The cytoskeleton of digestive epithelia in health and disease
    • Ku, N. O., Zhou, X., Toivola, D. M., Omary, M. B., The cytoskeleton of digestive epithelia in health and disease. Am. J. Physiol. 1999, 277, G1108-G1137.
    • (1999) Am. J. Physiol , vol.277
    • Ku, N.O.1    Zhou, X.2    Toivola, D.M.3    Omary, M.B.4
  • 43
    • 0035824508 scopus 로고    scopus 로고
    • Polycystin-1 interacts with intermediate filaments
    • Xu, G. M., Sikaneta, T., Sullivan, B. M., Zhang, Q. et al., Polycystin-1 interacts with intermediate filaments. J. Biol. Chem. 2001, 276, 46544-46552.
    • (2001) J. Biol. Chem , vol.276 , pp. 46544-46552
    • Xu, G.M.1    Sikaneta, T.2    Sullivan, B.M.3    Zhang, Q.4
  • 44
    • 36248956949 scopus 로고    scopus 로고
    • DAP kinase mediates the phosphorylation of tropomyosin-1 down-stream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress
    • Houle, F., Poirier, A., Dumaresq, J., Huot, J., DAP kinase mediates the phosphorylation of tropomyosin-1 down-stream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress. J. Cell Sci. 2007, 120, 3666-3677.
    • (2007) J. Cell Sci , vol.120 , pp. 3666-3677
    • Houle, F.1    Poirier, A.2    Dumaresq, J.3    Huot, J.4
  • 45
    • 0038032832 scopus 로고    scopus 로고
    • Extra-cellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: Impact on membrane blebbing
    • Houle, F., Rousseau, S., Morrice, N., Luc, M. et al., Extra-cellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing. Mol. Biol. Cell 2003, 14, 1418-1432.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1418-1432
    • Houle, F.1    Rousseau, S.2    Morrice, N.3    Luc, M.4
  • 46
    • 0037474534 scopus 로고    scopus 로고
    • Polycystin-2 associates with tropomyosin-1, an actin microfilament component
    • Li, Q., Dai, Y., Guo, L, Liu, Y. et al., Polycystin-2 associates with tropomyosin-1, an actin microfilament component. J. Mol. Biol. 2003, 325, 949-962.
    • (2003) J. Mol. Biol , vol.325 , pp. 949-962
    • Li, Q.1    Dai, Y.2    Guo, L.3    Liu, Y.4
  • 47
    • 0032454433 scopus 로고    scopus 로고
    • The effect of dietary flaxseed supplementation on organic anion and osmolyte content and excretion in rat polycystic kidney disease
    • Ogborn, M. R., Nitschmann, E., Bankovic-Calic, N., Buist, R., Peeling, J., The effect of dietary flaxseed supplementation on organic anion and osmolyte content and excretion in rat polycystic kidney disease. Biochem. Cell Biol. 1998, 76, 553-559.
    • (1998) Biochem. Cell Biol , vol.76 , pp. 553-559
    • Ogborn, M.R.1    Nitschmann, E.2    Bankovic-Calic, N.3    Buist, R.4    Peeling, J.5
  • 48
    • 0036208924 scopus 로고    scopus 로고
    • Oxidant stress and reduced antioxidant enzyme protection in polycystic kidney disease
    • Maser, R. L., Vassmer, D., Magenheimer, B. S., Calvet, J. P., Oxidant stress and reduced antioxidant enzyme protection in polycystic kidney disease. J. Am. Soc. Nephrol. 2002, 13, 991-999.
    • (2002) J. Am. Soc. Nephrol , vol.13 , pp. 991-999
    • Maser, R.L.1    Vassmer, D.2    Magenheimer, B.S.3    Calvet, J.P.4
  • 50
    • 0034132730 scopus 로고    scopus 로고
    • Developmental changes in antioxidant enzymes and oxidative damage in kidneys, liver and brain of bcl-2 knockout mice
    • Hochman, A., Liang, H., Offen, D., Melamed, E., Sternin, H., Developmental changes in antioxidant enzymes and oxidative damage in kidneys, liver and brain of bcl-2 knockout mice. Cell Mol. Biol. 2000, 46, 41-52.
    • (2000) Cell Mol. Biol , vol.46 , pp. 41-52
    • Hochman, A.1    Liang, H.2    Offen, D.3    Melamed, E.4    Sternin, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.