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Volumn 292, Issue 2, 2007, Pages

Proteomics in renal research

Author keywords

DIGE; Glomerulus; Mass spectrometry; Nephron; Renal tubule; Two dimensional gel electrophoresis

Indexed keywords

ALBUMIN; ALPHA2 GLYCOPROTEIN; APOLIPOPROTEIN A4; BETA 2 MICROGLOBULIN; CARBONATE DEHYDRATASE; CONNEXIN 43; GENTAMICIN; GLUTATHIONE TRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; HYBRID PROTEIN; LEAD; LITHOSTATHINE; PREALBUMIN; SNARE PROTEIN; STREPTOZOCIN; TOXIN; VITAMIN D BINDING PROTEIN;

EID: 33846869763     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00298.2006     Document Type: Review
Times cited : (55)

References (140)
  • 1
    • 2942729565 scopus 로고    scopus 로고
    • Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines
    • Afjehi-Sadat L, Krapfenbauer K, Slavc I, Fountoulakis M, Lubec G. Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines. Biochim Biophys Acta 1700: 65-74, 2004.
    • (2004) Biochim Biophys Acta , vol.1700 , pp. 65-74
    • Afjehi-Sadat, L.1    Krapfenbauer, K.2    Slavc, I.3    Fountoulakis, M.4    Lubec, G.5
  • 3
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L, Hunter CL. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 5: 573-588, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 4
    • 0018606770 scopus 로고
    • Proteins of human urine. I. Concentration and analysis by two-dimensional electrophoresis
    • Anderson NG, Anderson NL, Tollaksen SL. Proteins of human urine. I. Concentration and analysis by two-dimensional electrophoresis. Clin Chem 25: 1199-1210, 1979.
    • (1979) Clin Chem , vol.25 , pp. 1199-1210
    • Anderson, N.G.1    Anderson, N.L.2    Tollaksen, S.L.3
  • 5
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L, Seilhamer J. A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 18: 533-537, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 6
    • 0025637631 scopus 로고
    • Alteration in protein synthesis in primary cultures of rat kidney proximal tubule epithelial cells by exposure to gallium, indium, and arsenite
    • Aoki Y, Lipsky MM, Fowler BA. Alteration in protein synthesis in primary cultures of rat kidney proximal tubule epithelial cells by exposure to gallium, indium, and arsenite. Toxicol Appl Pharmacol 106: 462-468, 1990.
    • (1990) Toxicol Appl Pharmacol , vol.106 , pp. 462-468
    • Aoki, Y.1    Lipsky, M.M.2    Fowler, B.A.3
  • 7
    • 0033692842 scopus 로고    scopus 로고
    • The MDCK cell line is made up of populations of cells with diverse resistive and transport properties
    • Arthur JM. The MDCK cell line is made up of populations of cells with diverse resistive and transport properties. Tissue Cell 32: 446-450, 2000.
    • (2000) Tissue Cell , vol.32 , pp. 446-450
    • Arthur, J.M.1
  • 10
    • 0035162584 scopus 로고    scopus 로고
    • Tumour-related enzyme alterations in the clear cell type of human renal cell carcinoma identified by two-dimensional gel electrophoresis
    • Balabanov S, Zimmermann U, Protzel C, Scharf C, Klebingat KJ, Walther R. Tumour-related enzyme alterations in the clear cell type of human renal cell carcinoma identified by two-dimensional gel electrophoresis. Eur J Biochem 268: 5977-5980, 2001.
    • (2001) Eur J Biochem , vol.268 , pp. 5977-5980
    • Balabanov, S.1    Zimmermann, U.2    Protzel, C.3    Scharf, C.4    Klebingat, K.J.5    Walther, R.6
  • 11
    • 0032924895 scopus 로고    scopus 로고
    • The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis-preliminary findings
    • Banks RE, Dunn MJ, Forbes MA, Stanley A, Pappin D, Naven T, Gough M, Harnden P, Selby PJ. The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis-preliminary findings. Electrophoresis 20: 689-700, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 689-700
    • Banks, R.E.1    Dunn, M.J.2    Forbes, M.A.3    Stanley, A.4    Pappin, D.5    Naven, T.6    Gough, M.7    Harnden, P.8    Selby, P.J.9
  • 12
    • 33846884546 scopus 로고    scopus 로고
    • Proteomic approach to identification of novel kinase substrates in mesangial cells
    • Barati MT, Powell DW, McLeish KR. Proteomic approach to identification of novel kinase substrates in mesangial cells. Contrib Nephrol 141: 231-244, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 231-244
    • Barati, M.T.1    Powell, D.W.2    McLeish, K.R.3
  • 13
    • 24044432222 scopus 로고    scopus 로고
    • Large scale protein identification in intracellular aquaporin-2 vesicles from renal inner medullary collecting duct
    • Barile M, Pisitkun T, Yu MJ, Chou CL, Verbalis MJ, Shen RF, Knepper MA. Large scale protein identification in intracellular aquaporin-2 vesicles from renal inner medullary collecting duct. Mol Cell Proteomics 4: 1095-1106, 2005.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1095-1106
    • Barile, M.1    Pisitkun, T.2    Yu, M.J.3    Chou, C.L.4    Verbalis, M.J.5    Shen, R.F.6    Knepper, M.A.7
  • 14
    • 0036112490 scopus 로고    scopus 로고
    • Dysregulation of renal salt and water transport proteins in diabetic Zucker rats
    • Bickel CA, Knepper MA, Verbalis JG, Ecelbarger CA. Dysregulation of renal salt and water transport proteins in diabetic Zucker rats. Kidney Int 61: 2099-2110, 2002.
    • (2002) Kidney Int , vol.61 , pp. 2099-2110
    • Bickel, C.A.1    Knepper, M.A.2    Verbalis, J.G.3    Ecelbarger, C.A.4
  • 15
    • 0028577656 scopus 로고
    • Sequencing of proteins extracted from stones
    • Binette JP, Binette MB. Sequencing of proteins extracted from stones. Scanning Microsc 8: 233-239, 1994.
    • (1994) Scanning Microsc , vol.8 , pp. 233-239
    • Binette, J.P.1    Binette, M.B.2
  • 16
    • 0036380930 scopus 로고    scopus 로고
    • The kidney proteome: A hint of things to come
    • Bonventre JV. The kidney proteome: a hint of things to come. Kidney Int 62: 1470-1471, 2002.
    • (2002) Kidney Int , vol.62 , pp. 1470-1471
    • Bonventre, J.V.1
  • 19
    • 0028801548 scopus 로고
    • Electrophoretic, chromatographic and immunological studies of human urinary proteins
    • Bueler MR, Wiederkehr F, Vonderschmitt DJ. Electrophoretic, chromatographic and immunological studies of human urinary proteins. Electrophoresis 16: 124-134, 1995.
    • (1995) Electrophoresis , vol.16 , pp. 124-134
    • Bueler, M.R.1    Wiederkehr, F.2    Vonderschmitt, D.J.3
  • 22
    • 0036745418 scopus 로고    scopus 로고
    • Acute and chronic effect of dietary phosphorus restriction on protein expression in young rat renal proximal tubules
    • Cheung PY, Lai WP, Lau HY, Lo SC, Wong MS. Acute and chronic effect of dietary phosphorus restriction on protein expression in young rat renal proximal tubules. Proteomics 2: 1211-1219, 2002.
    • (2002) Proteomics , vol.2 , pp. 1211-1219
    • Cheung, P.Y.1    Lai, W.P.2    Lau, H.Y.3    Lo, S.C.4    Wong, M.S.5
  • 24
    • 0036120616 scopus 로고    scopus 로고
    • Laser capture microdissection and two-dimensional polyacrylamide gel electrophoresis: Evaluation of tissue preparation and sample limitations
    • Craven RA, Totty N, Harnden P, Selby PJ, Banks RE. Laser capture microdissection and two-dimensional polyacrylamide gel electrophoresis: evaluation of tissue preparation and sample limitations. Am J Pathol 160: 815-822, 2002.
    • (2002) Am J Pathol , vol.160 , pp. 815-822
    • Craven, R.A.1    Totty, N.2    Harnden, P.3    Selby, P.J.4    Banks, R.E.5
  • 25
    • 33846248808 scopus 로고    scopus 로고
    • Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis
    • Curthoys NP, Taylor L, Hoffert JD, Knepper MA. Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis. Am J Physiol Renal Physiol 291: F140-F147, 2006.
    • (2006) Am J Physiol Renal Physiol , vol.291
    • Curthoys, N.P.1    Taylor, L.2    Hoffert, J.D.3    Knepper, M.A.4
  • 26
    • 3042841949 scopus 로고    scopus 로고
    • Proteomic strategies and their application in studies of renal function
    • Cutillas P, Burlingame A, Unwin R. Proteomic strategies and their application in studies of renal function. News Physiol Sci 19: 114-119, 2004.
    • (2004) News Physiol Sci , vol.19 , pp. 114-119
    • Cutillas, P.1    Burlingame, A.2    Unwin, R.3
  • 31
    • 33846859711 scopus 로고    scopus 로고
    • Proteomics and sodium transport
    • Ecelbarger CA. Proteomics and sodium transport. Contrib Nephrol 141: 124-141, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 124-141
    • Ecelbarger, C.A.1
  • 32
    • 20544434111 scopus 로고    scopus 로고
    • Targeted proteomics using immunoblotting technique for studying dysregulation of ion transporters in renal disorders
    • Ecelbarger CA. Targeted proteomics using immunoblotting technique for studying dysregulation of ion transporters in renal disorders. Expert Rev Proteomics 1: 219-227, 2004.
    • (2004) Expert Rev Proteomics , vol.1 , pp. 219-227
    • Ecelbarger, C.A.1
  • 34
    • 0031427192 scopus 로고    scopus 로고
    • Mapping the protein composition of trans-Golgi network (TGN)-derived carrier vesicles from polarized MDCK cells
    • Fiedler K, Kellner R, Simons K. Mapping the protein composition of trans-Golgi network (TGN)-derived carrier vesicles from polarized MDCK cells. Electrophoresis 18: 2613-2619, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 2613-2619
    • Fiedler, K.1    Kellner, R.2    Simons, K.3
  • 35
    • 0027257099 scopus 로고
    • Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler K, Kobayashi T, Kurzchalia TV, Simons K. Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32: 6365-6373, 1993.
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1    Kobayashi, T.2    Kurzchalia, T.V.3    Simons, K.4
  • 36
    • 23144459134 scopus 로고    scopus 로고
    • Capillary electrophoresis coupled to mass spectrometry for clinical diagnostic purposes
    • Fliser D, Wittke S, Mischak H. Capillary electrophoresis coupled to mass spectrometry for clinical diagnostic purposes. Electrophoresis 26: 2708-2716, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 2708-2716
    • Fliser, D.1    Wittke, S.2    Mischak, H.3
  • 37
    • 0025818701 scopus 로고
    • Abnormal proximal tubule apical membrane protein composition in X-linked hypophosphatemic mice
    • Ford DM, Molitoris BA. Abnormal proximal tubule apical membrane protein composition in X-linked hypophosphatemic mice. Am J Physiol Renal Fluid Electrolyte Physiol 260: F317-F322, 1991.
    • (1991) Am J Physiol Renal Fluid Electrolyte Physiol , vol.260
    • Ford, D.M.1    Molitoris, B.A.2
  • 38
    • 0042232784 scopus 로고    scopus 로고
    • The use of SELDI ProteinChip array technology in renal disease research
    • Fung E, Diamond D, Simonsesn AH, Weinberger SR. The use of SELDI ProteinChip array technology in renal disease research. Methods Mol Med 86: 295-312, 2003.
    • (2003) Methods Mol Med , vol.86 , pp. 295-312
    • Fung, E.1    Diamond, D.2    Simonsesn, A.H.3    Weinberger, S.R.4
  • 39
    • 0028935921 scopus 로고
    • Evidence for the presence of abnormal proteins in the urine of recurrent stone formers
    • Grover PK, Resnick MI. Evidence for the presence of abnormal proteins in the urine of recurrent stone formers. J Urol 153: 1716-1721, 1995.
    • (1995) J Urol , vol.153 , pp. 1716-1721
    • Grover, P.K.1    Resnick, M.I.2
  • 40
    • 0033885949 scopus 로고    scopus 로고
    • Measuring gene expression by quantitative proteome analysis
    • Gygi SP, Rist B, Aebersold R. Measuring gene expression by quantitative proteome analysis. Curr Opin Biotechnol 11: 396-401, 2000.
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 396-401
    • Gygi, S.P.1    Rist, B.2    Aebersold, R.3
  • 41
  • 42
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi SP, Rochon Y, Franza BR, Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720-1730, 1999.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 43
    • 0037897721 scopus 로고    scopus 로고
    • Biomedical applications of capillary electrophoresis
    • Hempel G. Biomedical applications of capillary electrophoresis. Clin Chem Lab Med 41: 720-723, 2003.
    • (2003) Clin Chem Lab Med , vol.41 , pp. 720-723
    • Hempel, G.1
  • 44
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA. Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci USA 103: 7159-7164, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.F.4    Knepper, M.A.5
  • 45
    • 0346729893 scopus 로고    scopus 로고
    • Application of difference gel electrophoresis to the identification of inner medullary collecting duct proteins
    • Hoffert JD, van Balkom BW, Chou CL, Knepper MA. Application of difference gel electrophoresis to the identification of inner medullary collecting duct proteins. Am J Physiol Renal Physiol 286: F170-F179, 2004.
    • (2004) Am J Physiol Renal Physiol , vol.286
    • Hoffert, J.D.1    van Balkom, B.W.2    Chou, C.L.3    Knepper, M.A.4
  • 46
    • 33645263569 scopus 로고    scopus 로고
    • Combined proteomics and pathways analysis of collecting duct reveals a protein regulatory network activated in vasopressin escape
    • Hoorn EJ, Hoffert JD, Knepper MA. Combined proteomics and pathways analysis of collecting duct reveals a protein regulatory network activated in vasopressin escape. J Am Soc Nephrol 16: 2852-2863, 2005.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2852-2863
    • Hoorn, E.J.1    Hoffert, J.D.2    Knepper, M.A.3
  • 48
    • 0029805083 scopus 로고    scopus 로고
    • Endosomal fractions from viral K-ras-transformed MDCK cells reveal transformation specific changes on two-dimensional gel maps
    • Huber LA, Pasquali C, Gagescu R, Zuk A, Gruenberg J, Matlin KS. Endosomal fractions from viral K-ras-transformed MDCK cells reveal transformation specific changes on two-dimensional gel maps. Electrophoresis 17: 1734-1740, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 1734-1740
    • Huber, L.A.1    Pasquali, C.2    Gagescu, R.3    Zuk, A.4    Gruenberg, J.5    Matlin, K.S.6
  • 49
    • 0027517448 scopus 로고
    • Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane
    • Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K. Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol 123: 35-45, 1993.
    • (1993) J Cell Biol , vol.123 , pp. 35-45
    • Huber, L.A.1    Pimplikar, S.2    Parton, R.G.3    Virta, H.4    Zerial, M.5    Simons, K.6
  • 53
    • 0025153114 scopus 로고
    • The characterization of soluble matrix proteins in selected human renal calculi using two-dimensional polyacrylamide gel electrophoresis
    • Jones WT, Resnick MI. The characterization of soluble matrix proteins in selected human renal calculi using two-dimensional polyacrylamide gel electrophoresis. J Urol 144: 1010-1014, 1990.
    • (1990) J Urol , vol.144 , pp. 1010-1014
    • Jones, W.T.1    Resnick, M.I.2
  • 55
    • 0345731214 scopus 로고    scopus 로고
    • Detection of protein Z in a renal calculus composed of calcium oxalate monohydrate with the use of liquid chromatographymass spectrometry/mass spectrometry following two-dimensional polyacrylamide gel electrophoresis separation
    • Kaneko K, Yamanobe T, Nakagomi K, Mawatari K, Onoda M, Fujimori S. Detection of protein Z in a renal calculus composed of calcium oxalate monohydrate with the use of liquid chromatographymass spectrometry/mass spectrometry following two-dimensional polyacrylamide gel electrophoresis separation. Anal Biochem 324: 191-196, 2004.
    • (2004) Anal Biochem , vol.324 , pp. 191-196
    • Kaneko, K.1    Yamanobe, T.2    Nakagomi, K.3    Mawatari, K.4    Onoda, M.5    Fujimori, S.6
  • 56
    • 0032746615 scopus 로고    scopus 로고
    • Alterations in rabbit kidney protein expression following lead exposure as analyzed by two-dimensional gel electrophoresis
    • Kanitz MH, Witzmann FA, Zhu H, Fultz CD, Skaggs S, Moorman WJ, Savage RE Jr. Alterations in rabbit kidney protein expression following lead exposure as analyzed by two-dimensional gel electrophoresis. Electrophoresis 20: 2977-2985, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 2977-2985
    • Kanitz, M.H.1    Witzmann, F.A.2    Zhu, H.3    Fultz, C.D.4    Skaggs, S.5    Moorman, W.J.6    Savage Jr., R.E.7
  • 57
    • 1442324406 scopus 로고    scopus 로고
    • Identification of manganese superoxide dismutase as a NO-regulated gene in rat glomerular mesangial cells by 2D gel electrophoresis
    • Keller T, Pleskova M, McDonald MC, Thiemermann C, Pfeilschifter J, Beck KF. Identification of manganese superoxide dismutase as a NO-regulated gene in rat glomerular mesangial cells by 2D gel electrophoresis. Nitric Oxide 9: 183-193, 2003.
    • (2003) Nitric Oxide , vol.9 , pp. 183-193
    • Keller, T.1    Pleskova, M.2    McDonald, M.C.3    Thiemermann, C.4    Pfeilschifter, J.5    Beck, K.F.6
  • 58
    • 0036649486 scopus 로고    scopus 로고
    • The role of proteomics in toxicology: Identification of biomarkers of toxicity by protein expression analysis
    • Kennedy S. The role of proteomics in toxicology: identification of biomarkers of toxicity by protein expression analysis. Biomarkers 7: 269-290, 2002.
    • (2002) Biomarkers , vol.7 , pp. 269-290
    • Kennedy, S.1
  • 62
    • 5444230176 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis: A fundamental tool for expression proteomics studies
    • Klein E, Klein JB, Thongboonkerd V. Two-dimensional gel electrophoresis: a fundamental tool for expression proteomics studies. Contrib Nephrol 141: 25-39, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 25-39
    • Klein, E.1    Klein, J.B.2    Thongboonkerd, V.3
  • 63
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues
    • Klose J. Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. Humangenetik 26: 231-243, 1975.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 64
    • 0036236142 scopus 로고    scopus 로고
    • Proteomics and the kidney
    • Knepper MA. Proteomics and the kidney. J Am Soc Nephrol 13: 1398-1408, 2002.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1398-1408
    • Knepper, M.A.1
  • 65
    • 0034786917 scopus 로고    scopus 로고
    • Targeted proteomics in the kidney using ensembles of antibodies
    • Knepper MA, Masilamani S. Targeted proteomics in the kidney using ensembles of antibodies. Acta Physiol Scand 173: 11-21, 2001.
    • (2001) Acta Physiol Scand , vol.173 , pp. 11-21
    • Knepper, M.A.1    Masilamani, S.2
  • 67
    • 18844370547 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery
    • Kolch W, Neususs C, Pelzing M, Mischak H. Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom Rev 24: 959-977, 2005.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3    Mischak, H.4
  • 68
    • 23244443876 scopus 로고    scopus 로고
    • Proteomic analysis reveals novel protein targets of S-nitrosylation in mesangial cells
    • Kuncewicz T, Sheta EA, Goldknopf IL, Kone BC. Proteomic analysis reveals novel protein targets of S-nitrosylation in mesangial cells. Contrib Nephrol 141: 221-230, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 221-230
    • Kuncewicz, T.1    Sheta, E.A.2    Goldknopf, I.L.3    Kone, B.C.4
  • 69
    • 15844398250 scopus 로고    scopus 로고
    • Micellar electrokinetic chromatographic and capillary zone electrophoretic methods for screening urinary biomarkers of human disorders: A critical review of the state-of-the-art
    • Ladarola P, Cetta G, Luisetti M, Annovazzi L, Casado B, Baraniuk J, Zanone C, Viglio S. Micellar electrokinetic chromatographic and capillary zone electrophoretic methods for screening urinary biomarkers of human disorders: a critical review of the state-of-the-art. Electrophoresis 26: 752-766, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 752-766
    • Ladarola, P.1    Cetta, G.2    Luisetti, M.3    Annovazzi, L.4    Casado, B.5    Baraniuk, J.6    Zanone, C.7    Viglio, S.8
  • 71
    • 11144302513 scopus 로고    scopus 로고
    • Identification of proteins in slow continuous ultrafiltrate by reversed-phase chromatography and proteomics
    • Lefler DM, Pafford RG, Black NA, Raymond JR, Arthur JM. Identification of proteins in slow continuous ultrafiltrate by reversed-phase chromatography and proteomics. J Proteome Res 3: 1254-1260, 2004.
    • (2004) J Proteome Res , vol.3 , pp. 1254-1260
    • Lefler, D.M.1    Pafford, R.G.2    Black, N.A.3    Raymond, J.R.4    Arthur, J.M.5
  • 72
    • 0037843285 scopus 로고    scopus 로고
    • Database for renal collecting duct regulatory and transporter proteins
    • Legato J, Knepper MA, Star RA, Mejia R. Database for renal collecting duct regulatory and transporter proteins. Physiol Genomics 13: 179-181, 2003.
    • (2003) Physiol Genomics , vol.13 , pp. 179-181
    • Legato, J.1    Knepper, M.A.2    Star, R.A.3    Mejia, R.4
  • 73
    • 4344565772 scopus 로고    scopus 로고
    • Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin
    • Lehtonen S, Lehtonen E, Kudlicka K, Holthofer H, Farquhar MG. Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin. Am J Pathol 165: 923-936, 2004.
    • (2004) Am J Pathol , vol.165 , pp. 923-936
    • Lehtonen, S.1    Lehtonen, E.2    Kudlicka, K.3    Holthofer, H.4    Farquhar, M.G.5
  • 75
    • 7644221212 scopus 로고    scopus 로고
    • Separation, identification of uremic middle molecules, and preliminary study on their toxicity
    • Li G, Chu J, Liu X, Yuan Z. Separation, identification of uremic middle molecules, and preliminary study on their toxicity. Clin Chim Acta 350: 89-98, 2004.
    • (2004) Clin Chim Acta , vol.350 , pp. 89-98
    • Li, G.1    Chu, J.2    Liu, X.3    Yuan, Z.4
  • 76
    • 11344292695 scopus 로고    scopus 로고
    • Genomic and proteomic profiling for biomarkers and signature profiles of toxicity
    • Merrick BA, Bruno ME. Genomic and proteomic profiling for biomarkers and signature profiles of toxicity. Curr Opin Mol Ther 6: 600-607, 2004.
    • (2004) Curr Opin Mol Ther , vol.6 , pp. 600-607
    • Merrick, B.A.1    Bruno, M.E.2
  • 80
    • 0034874634 scopus 로고    scopus 로고
    • Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry
    • Nedelkov D, Nelson RW. Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry. Am J Kidney Dis 38: 481-487, 2001.
    • (2001) Am J Kidney Dis , vol.38 , pp. 481-487
    • Nedelkov, D.1    Nelson, R.W.2
  • 81
    • 10744221488 scopus 로고    scopus 로고
    • Mass spectrometry for the detection of differentially expressed proteins: A comparison of surface-enhanced laser desorption/ionization and capillary electrophoresis/mass spectrometry
    • Neuhoff N, Kaiser T, Wittke S, Krebs R, Pitt A, Burchard A, Sundmacher A, Schlegelberger B, Kolch W, Mischak H. Mass spectrometry for the detection of differentially expressed proteins: a comparison of surface-enhanced laser desorption/ionization and capillary electrophoresis/mass spectrometry. Rapid Commun Mass Spectrom 18: 149-156, 2004.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 149-156
    • Neuhoff, N.1    Kaiser, T.2    Wittke, S.3    Krebs, R.4    Pitt, A.5    Burchard, A.6    Sundmacher, A.7    Schlegelberger, B.8    Kolch, W.9    Mischak, H.10
  • 82
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 85
    • 1442325443 scopus 로고    scopus 로고
    • Evidence for the existence of hypothetical proteins in human bronchial epithelial, fibroblast, amnion, lymphocyte, mesothelial and kidney cell lines
    • Oh JE, Krapfenbauer K, Fountoulakis M, Frischer T, Lubec G. Evidence for the existence of hypothetical proteins in human bronchial epithelial, fibroblast, amnion, lymphocyte, mesothelial and kidney cell lines. Amino Acids 26: 9-18, 2004.
    • (2004) Amino Acids , vol.26 , pp. 9-18
    • Oh, J.E.1    Krapfenbauer, K.2    Fountoulakis, M.3    Frischer, T.4    Lubec, G.5
  • 88
    • 0038650583 scopus 로고    scopus 로고
    • Comparative identification of prostanoid inducible proteins by LC-ESIMS/MS and MALDI-TOF mass spectrometry
    • Person MD, Lo HH, Towndrow KM, Jia Z, Monks TJ, Lau SS. Comparative identification of prostanoid inducible proteins by LC-ESIMS/MS and MALDI-TOF mass spectrometry. Chem Res Toxicol 16: 757-767, 2003.
    • (2003) Chem Res Toxicol , vol.16 , pp. 757-767
    • Person, M.D.1    Lo, H.H.2    Towndrow, K.M.3    Jia, Z.4    Monks, T.J.5    Lau, S.S.6
  • 89
    • 11144356366 scopus 로고    scopus 로고
    • Characterization of the human urinary proteome: A method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots
    • Pieper R, Gatlin CL, McGrath AM, Makusky AJ, Mondal M, Seonarain M, Field E, Schatz CR, Estock MA, Ahmed N, Anderson NG, Steiner S. Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots. Proteomics 4: 1159-1174, 2004.
    • (2004) Proteomics , vol.4 , pp. 1159-1174
    • Pieper, R.1    Gatlin, C.L.2    McGrath, A.M.3    Makusky, A.J.4    Mondal, M.5    Seonarain, M.6    Field, E.7    Schatz, C.R.8    Estock, M.A.9    Ahmed, N.10    Anderson, N.G.11    Steiner, S.12
  • 91
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun T, Shen RF, Knepper MA. Identification and proteomic profiling of exosomes in human urine. Proc Natl Acad Sci USA 101: 13368-13373, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 92
    • 0025887765 scopus 로고
    • Immunomagnetic separation, primary culture, and characterization of cortical thick ascending limb plus distal convoluted tubule cells from mouse kidney
    • Pizzonia JH, Gesek FA, Kennedy SM, Coutermarsh BA, Backsai BJ, Friedman PA. Immunomagnetic separation, primary culture, and characterization of cortical thick ascending limb plus distal convoluted tubule cells from mouse kidney. In Vitro Cell Dev Biol 27A: 409-416, 1991.
    • (1991) In Vitro Cell Dev Biol , vol.27 A , pp. 409-416
    • Pizzonia, J.H.1    Gesek, F.A.2    Kennedy, S.M.3    Coutermarsh, B.A.4    Backsai, B.J.5    Friedman, P.A.6
  • 93
    • 0035674978 scopus 로고    scopus 로고
    • Specific lectin binding to beta1 integrin and fibronectin on the apical membrane of Madin-Darby canine kidney cells
    • Praetorius J, Backlund P, Yergey AL, Spring KR. Specific lectin binding to beta1 integrin and fibronectin on the apical membrane of Madin-Darby canine kidney cells. J Membr Biol 184: 273-281, 2001.
    • (2001) J Membr Biol , vol.184 , pp. 273-281
    • Praetorius, J.1    Backlund, P.2    Yergey, A.L.3    Spring, K.R.4
  • 94
    • 16344378038 scopus 로고    scopus 로고
    • Podocyte proteomics
    • Ransom RF. Podocyte proteomics. Contrib Nephrol 141: 189-211, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 189-211
    • Ransom, R.F.1
  • 95
    • 16244409244 scopus 로고    scopus 로고
    • Differential proteomic analysis of proteins induced by glucocorticoids in cultured murine podocytes
    • Ransom RF, Vega-Warner V, Smoyer WE, Klein J. Differential proteomic analysis of proteins induced by glucocorticoids in cultured murine podocytes. Kidney Int 67: 1275-1285, 2005.
    • (2005) Kidney Int , vol.67 , pp. 1275-1285
    • Ransom, R.F.1    Vega-Warner, V.2    Smoyer, W.E.3    Klein, J.4
  • 96
    • 0025002268 scopus 로고
    • Parathyroid hormone-induced alterations of protein content and phosphorylation in enriched apical membranes of opossum kidney cells
    • Reshkin SJ, Wuarin F, Biber J, Murer H. Parathyroid hormone-induced alterations of protein content and phosphorylation in enriched apical membranes of opossum kidney cells. J Biol Chem 265: 15261-15266, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 15261-15266
    • Reshkin, S.J.1    Wuarin, F.2    Biber, J.3    Murer, H.4
  • 98
    • 0031828575 scopus 로고    scopus 로고
    • The role of the PHEX gene (PEX) in families with X-linked hypophosphataemic rickets
    • Rowe PS. The role of the PHEX gene (PEX) in families with X-linked hypophosphataemic rickets. Curr Opin Nephrol Hypertens 7: 367-376, 1998.
    • (1998) Curr Opin Nephrol Hypertens , vol.7 , pp. 367-376
    • Rowe, P.S.1
  • 103
    • 16244419727 scopus 로고    scopus 로고
    • Proteomic-based identification of cleaved urinary beta2-microglobulin as a potential marker for acute tubular injury in renal allografts
    • Schaub S, Wilkins JA, Antonovici M, Krokhin O, Weiler T, Rush D, Nickerson P. Proteomic-based identification of cleaved urinary beta2-microglobulin as a potential marker for acute tubular injury in renal allografts. Am J Transplant 5: 729-738, 2005.
    • (2005) Am J Transplant , vol.5 , pp. 729-738
    • Schaub, S.1    Wilkins, J.A.2    Antonovici, M.3    Krokhin, O.4    Weiler, T.5    Rush, D.6    Nickerson, P.7
  • 105
    • 0345865198 scopus 로고    scopus 로고
    • Identification of connexin-43 interacting proteins
    • Singh D, Lampe PD. Identification of connexin-43 interacting proteins. Cell Commun Adhes 10: 215-220, 2003.
    • (2003) Cell Commun Adhes , vol.10 , pp. 215-220
    • Singh, D.1    Lampe, P.D.2
  • 107
    • 16544371132 scopus 로고    scopus 로고
    • The potential of protein-detecting microarrays for clinical diagnostics
    • Smith AH, Vrtis JM, Kodadek T. The potential of protein-detecting microarrays for clinical diagnostics. Adv Clin Chem 38: 217-238, 2004.
    • (2004) Adv Clin Chem , vol.38 , pp. 217-238
    • Smith, A.H.1    Vrtis, J.M.2    Kodadek, T.3
  • 109
    • 4043094133 scopus 로고    scopus 로고
    • Proteomics in nephrology: Current status and future directions
    • Thongboonkerd V. Proteomics in nephrology: current status and future directions. Am J Nephrol 24: 360-378, 2004.
    • (2004) Am J Nephrol , vol.24 , pp. 360-378
    • Thongboonkerd, V.1
  • 113
    • 1542440372 scopus 로고    scopus 로고
    • Proteomic identification of a large complement of rat urinary proteins
    • Thongboonkerd V, Klein JB, Arthur JM. Proteomic identification of a large complement of rat urinary proteins. Nephron Exp Nephrol 95: e69-e78, 2003.
    • (2003) Nephron Exp Nephrol , vol.95
    • Thongboonkerd, V.1    Klein, J.B.2    Arthur, J.M.3
  • 115
    • 16344384394 scopus 로고    scopus 로고
    • Renal and urinary proteomics: Current applications and challenges
    • Thongboonkerd V, Malasit P. Renal and urinary proteomics: current applications and challenges. Proteomics 5: 1033-1042, 2005.
    • (2005) Proteomics , vol.5 , pp. 1033-1042
    • Thongboonkerd, V.1    Malasit, P.2
  • 117
    • 0037348603 scopus 로고    scopus 로고
    • 11-Deoxy,16,16-dimethyl prostaglandin E2 induces specific proteins in association with its ability to protect against oxidative stress
    • Towndrow KM, Jia Z, Lo HH, Person MD, Monks TJ, Lau SS. 11-Deoxy,16,16-dimethyl prostaglandin E2 induces specific proteins in association with its ability to protect against oxidative stress. Chem Res Toxicol 16: 312-319, 2003.
    • (2003) Chem Res Toxicol , vol.16 , pp. 312-319
    • Towndrow, K.M.1    Jia, Z.2    Lo, H.H.3    Person, M.D.4    Monks, T.J.5    Lau, S.S.6
  • 118
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18: 2071-2077, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 119
    • 0033406771 scopus 로고    scopus 로고
    • Urological malignancies and the proteomic-genomic interface
    • Unwin RD, Knowles MA, Selby PJ, Banks RE. Urological malignancies and the proteomic-genomic interface. Electrophoresis 20: 3629-3637, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 3629-3637
    • Unwin, R.D.1    Knowles, M.A.2    Selby, P.J.3    Banks, R.E.4
  • 120
    • 24944440037 scopus 로고    scopus 로고
    • Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells
    • Unwin RD, Pierce A, Watson RB, Sternberg DW, Whetton AD. Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells. Mol Cell Proteomics 4: 924-935, 2005.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 924-935
    • Unwin, R.D.1    Pierce, A.2    Watson, R.B.3    Sternberg, D.W.4    Whetton, A.D.5
  • 121
    • 24944499837 scopus 로고    scopus 로고
    • Nek8 mutation causes overexpression of galectin-1, sorcin, and vimentin and accumulation of the major urinary protein in renal cysts of jck mice
    • Valkova N, Yunis R, Mak SK, Kang K, Kultz D. Nek8 mutation causes overexpression of galectin-1, sorcin, and vimentin and accumulation of the major urinary protein in renal cysts of jck mice. Mol Cell Proteomics 4: 1009-1018, 2005.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1009-1018
    • Valkova, N.1    Yunis, R.2    Mak, S.K.3    Kang, K.4    Kultz, D.5
  • 122
    • 0942301312 scopus 로고    scopus 로고
    • Proteomic analysis of long-term vasopressin action in the inner medullary collecting duct of the Brattleboro rat
    • van Balkom BW, Hoffert JD, Chou CL, Knepper MA. Proteomic analysis of long-term vasopressin action in the inner medullary collecting duct of the Brattleboro rat. Am J Physiol Renal Physiol 286: F216-F224, 2004.
    • (2004) Am J Physiol Renal Physiol , vol.286
    • van Balkom, B.W.1    Hoffert, J.D.2    Chou, C.L.3    Knepper, M.A.4
  • 124
    • 33747618049 scopus 로고    scopus 로고
    • Automated quantification tool for high-throughput proteomics using stable isotope labeling and LC-MSn
    • Wang G, Wu WW, Pisitkun T, Hoffert JD, Knepper MA, Shen RF. Automated quantification tool for high-throughput proteomics using stable isotope labeling and LC-MSn. Anal Chem 78: 5752-5761, 2006.
    • (2006) Anal Chem , vol.78 , pp. 5752-5761
    • Wang, G.1    Wu, W.W.2    Pisitkun, T.3    Hoffert, J.D.4    Knepper, M.A.5    Shen, R.F.6
  • 126
    • 3142542638 scopus 로고    scopus 로고
    • A proteomic analysis of proteins removed by ultrafiltration during extracorporeal renal replacement therapy
    • Ward RA, Brinkley KA. A proteomic analysis of proteins removed by ultrafiltration during extracorporeal renal replacement therapy. Contrib Nephrol 141: 280-291, 2004.
    • (2004) Contrib Nephrol , vol.141 , pp. 280-291
    • Ward, R.A.1    Brinkley, K.A.2
  • 127
    • 13944257472 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination
    • Warren MR, Parker CE, Mocanu V, Klapper D, Borchers CH. Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination. Rapid Commun Mass Spectrom 19: 429-437, 2005.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 429-437
    • Warren, M.R.1    Parker, C.E.2    Mocanu, V.3    Klapper, D.4    Borchers, C.H.5
  • 128
    • 0038573965 scopus 로고    scopus 로고
    • Capillary electrophoresis-a high performance analytical separation technique
    • Watzig H, Gunter S. Capillary electrophoresis-a high performance analytical separation technique. Clin Chem Lab Med 41: 724-738, 2003.
    • (2003) Clin Chem Lab Med , vol.41 , pp. 724-738
    • Watzig, H.1    Gunter, S.2
  • 132
    • 0033919087 scopus 로고    scopus 로고
    • Toxicity of chemical mixtures: Proteomic analysis of persisting liver and kidney protein alterations induced by repeated exposure of rats to JP-8 jet fuel vapor
    • Witzmann FA, Carpenter RL, Ritchie GD, Wilson CL, Nordholm AF, Rossi J III. Toxicity of chemical mixtures: proteomic analysis of persisting liver and kidney protein alterations induced by repeated exposure of rats to JP-8 jet fuel vapor. Electrophoresis 21: 2138-2147, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 2138-2147
    • Witzmann, F.A.1    Carpenter, R.L.2    Ritchie, G.D.3    Wilson, C.L.4    Nordholm, A.F.5    Rossi III, J.6
  • 134
    • 0031760088 scopus 로고    scopus 로고
    • Differential expression of cytosolic proteins in the rat kidney cortex and medulla: Preliminary proteomics
    • Witzmann FA, Fultz CD, Grant RA, Wright LS, Kornguth SE, Siegel FL. Differential expression of cytosolic proteins in the rat kidney cortex and medulla: preliminary proteomics. Electrophoresis 19: 2491-2497, 1998.
    • (1998) Electrophoresis , vol.19 , pp. 2491-2497
    • Witzmann, F.A.1    Fultz, C.D.2    Grant, R.A.3    Wright, L.S.4    Kornguth, S.E.5    Siegel, F.L.6
  • 136
    • 0030049530 scopus 로고    scopus 로고
    • Toxicant-induced alterations in two-dimensional electrophoretic patterns of hepatic and renal stress proteins
    • Witzmann FA, Fultz CD, Lipscomb JC. Toxicant-induced alterations in two-dimensional electrophoretic patterns of hepatic and renal stress proteins. Electrophoresis 17: 198-202, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 198-202
    • Witzmann, F.A.1    Fultz, C.D.2    Lipscomb, J.C.3


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