메뉴 건너뛰기




Volumn 27, Issue 6, 2007, Pages 652-657

Proteomic Analysis in Pediatric Renal Disease

Author keywords

biomarkers; noninvasive; Pediatrics; urine proteomics

Indexed keywords

ALBUMIN; ALPHA 1 ANTICHYMOTRYPSIN; ALPHA 1 ANTITRYPSIN; CERULOPLASMIN; CILIARY NEUROTROPHIC FACTOR; HAPTOGLOBIN; STEROID; TAMM HORSFALL GLYCOPROTEIN; THYROXINE BINDING GLOBULIN; TRANSFERRIN;

EID: 36549036123     PISSN: 02709295     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semnephrol.2007.09.009     Document Type: Article
Times cited : (7)

References (26)
  • 2
    • 0035226437 scopus 로고    scopus 로고
    • Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. II. Limitations of complex mixture analyses
    • Davis M.T., Spahr C.S., McGinley M.D., et al. Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. II. Limitations of complex mixture analyses. Proteomics 1 (2001) 108-117
    • (2001) Proteomics , vol.1 , pp. 108-117
    • Davis, M.T.1    Spahr, C.S.2    McGinley, M.D.3
  • 3
    • 0035237935 scopus 로고    scopus 로고
    • Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest
    • Spahr C.S., Davis M.T., McGinley M.D., et al. Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics 1 (2001) 93-107
    • (2001) Proteomics , vol.1 , pp. 93-107
    • Spahr, C.S.1    Davis, M.T.2    McGinley, M.D.3
  • 4
    • 0036379687 scopus 로고    scopus 로고
    • Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation
    • Thongboonkerd V., McLeish K.R., Arthur J.M., et al. Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation. Kidney Int 62 (2002) 1461-1469
    • (2002) Kidney Int , vol.62 , pp. 1461-1469
    • Thongboonkerd, V.1    McLeish, K.R.2    Arthur, J.M.3
  • 5
    • 16544370448 scopus 로고    scopus 로고
    • Surfaced-enhanced laser desorption/ionization time-of-flight (SELDI-TOF) differentiation of serum protein profiles of BRCA-1 and sporadic breast cancer
    • Becker S., Cazares L.H., Watson P., et al. Surfaced-enhanced laser desorption/ionization time-of-flight (SELDI-TOF) differentiation of serum protein profiles of BRCA-1 and sporadic breast cancer. Ann Surg Oncol 11 (2004) 907-914
    • (2004) Ann Surg Oncol , vol.11 , pp. 907-914
    • Becker, S.1    Cazares, L.H.2    Watson, P.3
  • 6
    • 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 C.L., McGrath A.M., et al. 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 (2004) 1159-1174
    • (2004) Proteomics , vol.4 , pp. 1159-1174
    • Pieper, R.1    Gatlin, C.L.2    McGrath, A.M.3
  • 7
    • 2442670130 scopus 로고    scopus 로고
    • Proteomic patterns established with capillary electrophoresis and mass spectrometry for diagnostic purposes
    • Weissinger E.M., Wittke S., Kaiser T., et al. Proteomic patterns established with capillary electrophoresis and mass spectrometry for diagnostic purposes. Kidney Int 65 (2004) 2426-2434
    • (2004) Kidney Int , vol.65 , pp. 2426-2434
    • Weissinger, E.M.1    Wittke, S.2    Kaiser, T.3
  • 8
    • 33846815122 scopus 로고    scopus 로고
    • Proteomics profiling of urine with surface enhanced laser desorption/ionization time of flight mass spectrometry
    • Roelofsen H., Alvarez-Llamas G., Schepers M., et al. Proteomics profiling of urine with surface enhanced laser desorption/ionization time of flight mass spectrometry. Proteome Sci 5 (2007) 2
    • (2007) Proteome Sci , vol.5 , pp. 2
    • Roelofsen, H.1    Alvarez-Llamas, G.2    Schepers, M.3
  • 9
    • 32844469380 scopus 로고    scopus 로고
    • Glucocorticoids protect and enhance recovery of cultured murine podocytes via actin filament stabilization
    • Ransom R.F., Lam N.G., Hallett M.A., et al. Glucocorticoids protect and enhance recovery of cultured murine podocytes via actin filament stabilization. Kidney Int 68 (2005) 2473-2483
    • (2005) Kidney Int , vol.68 , pp. 2473-2483
    • Ransom, R.F.1    Lam, N.G.2    Hallett, M.A.3
  • 10
    • 0030725737 scopus 로고    scopus 로고
    • Comparison of noninvasive methods for distinguishing steroid-sensitive nephrotic syndrome from focal glomerulosclerosis
    • Ramjee G., Coovadia H.M., and Adhikari M. Comparison of noninvasive methods for distinguishing steroid-sensitive nephrotic syndrome from focal glomerulosclerosis. J Lab Clin Med 129 (1997) 47-52
    • (1997) J Lab Clin Med , vol.129 , pp. 47-52
    • Ramjee, G.1    Coovadia, H.M.2    Adhikari, M.3
  • 11
    • 33947270262 scopus 로고    scopus 로고
    • Urine biomarkers predict the cause of glomerular disease
    • Varghese S.A., Powell T.B., Budisavljevic M.N., et al. Urine biomarkers predict the cause of glomerular disease. J Am Soc Nephrol 18 (2007) 913-922
    • (2007) J Am Soc Nephrol , vol.18 , pp. 913-922
    • Varghese, S.A.1    Powell, T.B.2    Budisavljevic, M.N.3
  • 12
    • 33746997398 scopus 로고    scopus 로고
    • Urine proteomic profiling of pediatric nephrotic syndrome
    • Khurana M., Traum A.Z., Aivado M., et al. Urine proteomic profiling of pediatric nephrotic syndrome. Pediatr Nephrol 21 (2006) 1257-1265
    • (2006) Pediatr Nephrol , vol.21 , pp. 1257-1265
    • Khurana, M.1    Traum, A.Z.2    Aivado, M.3
  • 13
    • 33746340251 scopus 로고    scopus 로고
    • Urinary proteome of steroid-sensitive and steroid-resistant idiopathic nephrotic syndrome of childhood
    • Woroniecki R.P., Orlova T.N., Mendelev N., et al. Urinary proteome of steroid-sensitive and steroid-resistant idiopathic nephrotic syndrome of childhood. Am J Nephrol 26 (2006) 258-267
    • (2006) Am J Nephrol , vol.26 , pp. 258-267
    • Woroniecki, R.P.1    Orlova, T.N.2    Mendelev, N.3
  • 14
    • 33750718487 scopus 로고    scopus 로고
    • Repetitive fragmentation products of albumin and alpha1-antitrypsin in glomerular diseases associated with nephrotic syndrome
    • Candiano G., Musante L., Bruschi M., et al. Repetitive fragmentation products of albumin and alpha1-antitrypsin in glomerular diseases associated with nephrotic syndrome. J Am Soc Nephrol 17 (2006) 3139-3148
    • (2006) J Am Soc Nephrol , vol.17 , pp. 3139-3148
    • Candiano, G.1    Musante, L.2    Bruschi, M.3
  • 15
    • 0022346215 scopus 로고
    • Carbamylation of proteins and sulfacetamide free fraction in serum in experimentally-induced high blood urea states
    • Erill S., du Souich P., and Courteau H. Carbamylation of proteins and sulfacetamide free fraction in serum in experimentally-induced high blood urea states. Res Commun Chem Pathol Pharmacol 50 (1985) 45-56
    • (1985) Res Commun Chem Pathol Pharmacol , vol.50 , pp. 45-56
    • Erill, S.1    du Souich, P.2    Courteau, H.3
  • 16
    • 0033081236 scopus 로고    scopus 로고
    • Carbamylation of cysteine: a potential artifact in peptide mapping of hemoglobins in the presence of urea
    • Lippincott J., and Apostol I. Carbamylation of cysteine: a potential artifact in peptide mapping of hemoglobins in the presence of urea. Anal Biochem 267 (1999) 57-64
    • (1999) Anal Biochem , vol.267 , pp. 57-64
    • Lippincott, J.1    Apostol, I.2
  • 17
    • 0015701357 scopus 로고
    • Further studies of urea-catalyzed phosphorylation reactions
    • Osterberg R., Orgel L.E., and Lohrmann R. Further studies of urea-catalyzed phosphorylation reactions. J Mol Evol 2 (1973) 231-234
    • (1973) J Mol Evol , vol.2 , pp. 231-234
    • Osterberg, R.1    Orgel, L.E.2    Lohrmann, R.3
  • 18
    • 0016864340 scopus 로고
    • Preparation and properties of three specific active derivatives of ribonuclease A obtained by methylation of methionine residues in 8 M urea
    • Strak G.R., and Link T.P. Preparation and properties of three specific active derivatives of ribonuclease A obtained by methylation of methionine residues in 8 M urea. Biochemistry 14 (1975) 4576-4581
    • (1975) Biochemistry , vol.14 , pp. 4576-4581
    • Strak, G.R.1    Link, T.P.2
  • 19
    • 0036441526 scopus 로고    scopus 로고
    • Anti- and pro-oxidant effects of urate in copper-induced low-density lipoprotein oxidation
    • Filipe P., Haigle J., Freitas J., et al. Anti- and pro-oxidant effects of urate in copper-induced low-density lipoprotein oxidation. Eur J Biochem 269 (2002) 5474-5483
    • (2002) Eur J Biochem , vol.269 , pp. 5474-5483
    • Filipe, P.1    Haigle, J.2    Freitas, J.3
  • 20
    • 0032212580 scopus 로고    scopus 로고
    • Effect of uric acid and chemical analogues on oxidation of human low density lipoprotein in vitro
    • Schlotte V., Sevanian A., Hochstein P., et al. Effect of uric acid and chemical analogues on oxidation of human low density lipoprotein in vitro. Free Radic Biol Med 25 (1998) 839-847
    • (1998) Free Radic Biol Med , vol.25 , pp. 839-847
    • Schlotte, V.1    Sevanian, A.2    Hochstein, P.3
  • 21
    • 18844387655 scopus 로고    scopus 로고
    • Chronic exposure to ammonia alters the modulation of phosphorylation of microtubule-associated protein 2 by metabotropic glutamate receptors 1 and 5 in cerebellar neurons in culture
    • Llansola M., Erceg S., and Felipo V. Chronic exposure to ammonia alters the modulation of phosphorylation of microtubule-associated protein 2 by metabotropic glutamate receptors 1 and 5 in cerebellar neurons in culture. Neuroscience 133 (2005) 185-191
    • (2005) Neuroscience , vol.133 , pp. 185-191
    • Llansola, M.1    Erceg, S.2    Felipo, V.3
  • 22
    • 0036581130 scopus 로고    scopus 로고
    • Ammonia induces MK-801-sensitive nitration and phosphorylation of protein tyrosine residues in rat astrocytes
    • Schliess F., Gorg B., Fischer R., et al. Ammonia induces MK-801-sensitive nitration and phosphorylation of protein tyrosine residues in rat astrocytes. FASEB J 16 (2002) 739-741
    • (2002) FASEB J , vol.16 , pp. 739-741
    • Schliess, F.1    Gorg, B.2    Fischer, R.3
  • 23
    • 0023408979 scopus 로고
    • Acute effect of ammonia on branched-chain amino acid oxidation and incorporation into proteins in astrocytes and in neurons in primary cultures
    • Murthy C.R., and Hertz L. Acute effect of ammonia on branched-chain amino acid oxidation and incorporation into proteins in astrocytes and in neurons in primary cultures. J Neurochem 49 (1987) 735-741
    • (1987) J Neurochem , vol.49 , pp. 735-741
    • Murthy, C.R.1    Hertz, L.2
  • 24
    • 0023228127 scopus 로고
    • Comparison between acute and chronic effects of ammonia on branched-chain amino acid oxidation and incorporation into protein in primary cultures of astrocytes and of neurons
    • Murthy C.R., and Hertz L. Comparison between acute and chronic effects of ammonia on branched-chain amino acid oxidation and incorporation into protein in primary cultures of astrocytes and of neurons. J Neurosci Res 17 (1987) 271-276
    • (1987) J Neurosci Res , vol.17 , pp. 271-276
    • Murthy, C.R.1    Hertz, L.2
  • 25
    • 0026792869 scopus 로고
    • Ammonium chloride-induced acidosis increases protein breakdown and amino acid oxidation in humans
    • Reaich D., Channon S.M., Scrimgeour C.M., et al. Ammonium chloride-induced acidosis increases protein breakdown and amino acid oxidation in humans. Am J Physiol 263 (1992) E735-E739
    • (1992) Am J Physiol , vol.263
    • Reaich, D.1    Channon, S.M.2    Scrimgeour, C.M.3
  • 26
    • 3042665722 scopus 로고    scopus 로고
    • Low-molecular-weight human serum proteome using ultrafiltration, isoelectric focusing, and mass spectrometry
    • Harper R.G., Workman S.R., Schuetzner S., Timperman A.T., and Sutton J.N. Low-molecular-weight human serum proteome using ultrafiltration, isoelectric focusing, and mass spectrometry. Electrophoresis 25 (2004) 1299-1306
    • (2004) Electrophoresis , vol.25 , pp. 1299-1306
    • Harper, R.G.1    Workman, S.R.2    Schuetzner, S.3    Timperman, A.T.4    Sutton, J.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.